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<rss xmlns:itunes="http://www.itunes.com/dtds/podcast-1.0.dtd" xmlns:atom="http://www.w3.org/2005/Atom" xmlns:podcast="https://podcastindex.org/namespace/1.0" xmlns:media="http://search.yahoo.com/mrss/" version="2.0"><channel><title>Jack Forst's show</title><link>https://www.spreaker.com/podcast/jack-forst-s-show--2276036</link><description><![CDATA[]]></description><atom:link href="https://www.spreaker.com/show/2276036/episodes/feed" rel="self" type="application/rss+xml"/><language>zh</language><category>Society &amp; Culture</category><copyright>Copyright Jack Forst</copyright><image><url>https://d3wo5wojvuv7l.cloudfront.net/images.spreaker.com/nuvolari-assets/green_square_mic.jpg</url><title>Jack Forst's show</title><link>https://www.spreaker.com/podcast/jack-forst-s-show--2276036</link></image><lastBuildDate>Thu, 06 Apr 2023 18:42:12 +0000</lastBuildDate><itunes:author>Jack Forst</itunes:author><itunes:owner><itunes:name>Jack Forst</itunes:name><itunes:email>feeds@spreaker.com</itunes:email></itunes:owner><itunes:image href="https://d3wo5wojvuv7l.cloudfront.net/images.spreaker.com/nuvolari-assets/green_square_mic.jpg"/><itunes:category text="Society &amp; Culture"/><itunes:explicit>clean</itunes:explicit><itunes:type>episodic</itunes:type><item><title>superoxide dismutase</title><link>https://www.spreaker.com/episode/superoxide-dismutase--14221246</link><description><![CDATA[Superoxide dismutase (SOD) catalyzes the dismutation of superoxide radicals to hydrogen peroxide and molecular oxygen. SOD plays a critical role in the defense of cells against the toxic effects of oxygen radicals. SOD competes with nitric oxide (NO) for superoxide anion (which reacts with NO to form peroxynitrite), thereby SOD promotes the activity of NO. SOD has also been shown to suppress apoptosis in cultured rat ovarian follicles, neural cell lines, and transgenic mice by preventing the conversion of NO to peroxynitrate, an inducer of apoptosis.<br /><a href="https://www.creative-enzymes.com/product/native-bovine-superoxide-dismutase_1456.html" rel="noopener">https://www.creative-enzymes.com/product/native-bovine-superoxide-dismutase_1456.html</a>]]></description><guid isPermaLink="false">https://api.spreaker.com/episode/14221246</guid><pubDate>Wed, 07 Mar 2018 03:13:44 +0000</pubDate><enclosure url="https://api.spreaker.com/download/episode/14221246/superoxide_dismutase.mp3" length="354010" type="audio/mpeg"/><itunes:author>Jack Forst</itunes:author><itunes:subtitle>Superoxide dismutase (SOD) catalyzes the dismutation of superoxide radicals to hydrogen peroxide and molecular oxygen. SOD plays a critical role in the defense of cells against the toxic effects of oxygen radicals. SOD competes with nitric oxide (NO)...</itunes:subtitle><itunes:summary><![CDATA[Superoxide dismutase (SOD) catalyzes the dismutation of superoxide radicals to hydrogen peroxide and molecular oxygen. SOD plays a critical role in the defense of cells against the toxic effects of oxygen radicals. SOD competes with nitric oxide (NO) for superoxide anion (which reacts with NO to form peroxynitrite), thereby SOD promotes the activity of NO. SOD has also been shown to suppress apoptosis in cultured rat ovarian follicles, neural cell lines, and transgenic mice by preventing the conversion of NO to peroxynitrate, an inducer of apoptosis.<br /><a href="https://www.creative-enzymes.com/product/native-bovine-superoxide-dismutase_1456.html" rel="noopener">https://www.creative-enzymes.com/product/native-bovine-superoxide-dismutase_1456.html</a>]]></itunes:summary><itunes:duration>23</itunes:duration><itunes:explicit>clean</itunes:explicit><itunes:image href="https://d3wo5wojvuv7l.cloudfront.net/images.spreaker.com/nuvolari-assets/green_square_mic.jpg"/><itunes:episodeType>full</itunes:episodeType></item><item><title>lipoamide dehydrogenase</title><link>https://www.spreaker.com/episode/lipoamide-dehydrogenase--14220816</link><description><![CDATA[Lipoamide dehydrogenase (or diaphorase) catalyzes the following reaction: Lipoamide + NADH + H+ → Dihydrolipoamide + NAD+. The enzyme occurs in mammalian and microbial cells and it catalyzes a number of reactions which involve NAD+ or NADH. Lipoamide dehydrogenase from porcine heart contains two polypeptide chains which are similar. It has two molecules of tightly bound flavin adenine dinucleotide (FAD). The molecular weight of the porcine heart enzyme is between 100,000 and 114,000.<br /><a href="https://www.creative-enzymes.com/similar/LD_394.html" rel="noopener">https://www.creative-enzymes.com/similar/LD_394.html</a>]]></description><guid isPermaLink="false">https://api.spreaker.com/episode/14220816</guid><pubDate>Wed, 07 Mar 2018 02:12:55 +0000</pubDate><enclosure url="https://api.spreaker.com/download/episode/14220816/lipoamide_dehydrogenase.mp3" length="354010" type="audio/mpeg"/><itunes:author>Jack Forst</itunes:author><itunes:subtitle>Lipoamide dehydrogenase (or diaphorase) catalyzes the following reaction: Lipoamide + NADH + H+ → Dihydrolipoamide + NAD+. The enzyme occurs in mammalian and microbial cells and it catalyzes a number of reactions which involve NAD+ or NADH. Lipoamide...</itunes:subtitle><itunes:summary><![CDATA[Lipoamide dehydrogenase (or diaphorase) catalyzes the following reaction: Lipoamide + NADH + H+ → Dihydrolipoamide + NAD+. The enzyme occurs in mammalian and microbial cells and it catalyzes a number of reactions which involve NAD+ or NADH. Lipoamide dehydrogenase from porcine heart contains two polypeptide chains which are similar. It has two molecules of tightly bound flavin adenine dinucleotide (FAD). The molecular weight of the porcine heart enzyme is between 100,000 and 114,000.<br /><a href="https://www.creative-enzymes.com/similar/LD_394.html" rel="noopener">https://www.creative-enzymes.com/similar/LD_394.html</a>]]></itunes:summary><itunes:duration>23</itunes:duration><itunes:explicit>clean</itunes:explicit><itunes:image href="https://d3wo5wojvuv7l.cloudfront.net/images.spreaker.com/nuvolari-assets/green_square_mic.jpg"/><itunes:episodeType>full</itunes:episodeType></item><item><title>succinyl-coa synthetase</title><link>https://www.spreaker.com/episode/succinyl-coa-synthetase--14210319</link><guid isPermaLink="false">https://api.spreaker.com/episode/14210319</guid><pubDate>Tue, 06 Mar 2018 04:04:04 +0000</pubDate><enclosure url="https://api.spreaker.com/download/episode/14210319/succinyl_coa_synthetase.mp3" length="354010" type="audio/mpeg"/><itunes:author>Jack Forst</itunes:author><itunes:duration>23</itunes:duration><itunes:explicit>clean</itunes:explicit><itunes:image href="https://d3wo5wojvuv7l.cloudfront.net/images.spreaker.com/nuvolari-assets/green_square_mic.jpg"/><itunes:episodeType>full</itunes:episodeType></item><item><title>papain from papaya</title><link>https://www.spreaker.com/episode/papain-from-papaya--14209810</link><guid isPermaLink="false">https://api.spreaker.com/episode/14209810</guid><pubDate>Tue, 06 Mar 2018 02:23:08 +0000</pubDate><enclosure url="https://api.spreaker.com/download/episode/14209810/papain_from_papaya.mp3" length="354010" type="audio/mpeg"/><itunes:author>Jack Forst</itunes:author><itunes:duration>23</itunes:duration><itunes:explicit>clean</itunes:explicit><itunes:image href="https://d3wo5wojvuv7l.cloudfront.net/images.spreaker.com/nuvolari-assets/green_square_mic.jpg"/><itunes:episodeType>full</itunes:episodeType></item><item><title>serrapeptase research</title><link>https://www.spreaker.com/episode/serrapeptase-research--14199827</link><description><![CDATA[1. As pharmaceutical raw materials manufacturing injection, oral agents, executive standard: YBH Clinic： Used for anti-inflammation, eliminate swelling. Promote the dissolution of sputum, thick liquid to drain. Promote the migration of antibiotics to lesion. 2. Plant and animal protein hydrolysate powder (HAP, HVP) production applications The flora and fauna of macromolecular protein hydrolysis into small molecular peptides or amino acids, to facilitate the effective absorption and utilization of protein. 3. The application of baking industry To improve the luster of the finished products, make cookies section distinct, uniform structure, SongShuang crisp taste. 4. The application of soybean protein isolated Reduce the viscosity, improved the functional characteristics of soybean protein isolated 5. Production application of yeast extract, yeast extract Improve the utilization rate of the end product of protein and flavor 6. The beer industry Used in beer production, proteins can be ruled out "cold cloudy" phenomenon 7. Application of textile industry Processing of wool, and improve quality 8. Application of leather industry Made from the hair removal agent. 9. Application of feed industry To improve protein utilization and lower costs.<br /><a href="https://www.creative-enzymes.com/product/native-serratia-sp-serrapeptase_1700.html" rel="noopener">https://www.creative-enzymes.com/product/native-serratia-sp-serrapeptase_1700.html</a>]]></description><guid isPermaLink="false">https://api.spreaker.com/episode/14199827</guid><pubDate>Mon, 05 Mar 2018 03:41:39 +0000</pubDate><enclosure url="https://api.spreaker.com/download/episode/14199827/serrapeptase_research.mp3" length="354010" type="audio/mpeg"/><itunes:author>Jack Forst</itunes:author><itunes:subtitle>1. As pharmaceutical raw materials manufacturing injection, oral agents, executive standard: YBH Clinic： Used for anti-inflammation, eliminate swelling. Promote the dissolution of sputum, thick liquid to drain. Promote the migration of antibiotics to...</itunes:subtitle><itunes:summary><![CDATA[1. As pharmaceutical raw materials manufacturing injection, oral agents, executive standard: YBH Clinic： Used for anti-inflammation, eliminate swelling. Promote the dissolution of sputum, thick liquid to drain. Promote the migration of antibiotics to lesion. 2. Plant and animal protein hydrolysate powder (HAP, HVP) production applications The flora and fauna of macromolecular protein hydrolysis into small molecular peptides or amino acids, to facilitate the effective absorption and utilization of protein. 3. The application of baking industry To improve the luster of the finished products, make cookies section distinct, uniform structure, SongShuang crisp taste. 4. The application of soybean protein isolated Reduce the viscosity, improved the functional characteristics of soybean protein isolated 5. Production application of yeast extract, yeast extract Improve the utilization rate of the end product of protein and flavor 6. The beer industry Used in beer production, proteins can be ruled out "cold cloudy" phenomenon 7. Application of textile industry Processing of wool, and improve quality 8. Application of leather industry Made from the hair removal agent. 9. Application of feed industry To improve protein utilization and lower costs.<br /><a href="https://www.creative-enzymes.com/product/native-serratia-sp-serrapeptase_1700.html" rel="noopener">https://www.creative-enzymes.com/product/native-serratia-sp-serrapeptase_1700.html</a>]]></itunes:summary><itunes:duration>23</itunes:duration><itunes:explicit>clean</itunes:explicit><itunes:image href="https://d3wo5wojvuv7l.cloudfront.net/images.spreaker.com/nuvolari-assets/green_square_mic.jpg"/><itunes:episodeType>full</itunes:episodeType></item><item><title>galactose dehydrogenase</title><link>https://www.spreaker.com/episode/galactose-dehydrogenase--14199469</link><description><![CDATA[In enzymology, a galactose 1-dehydrogenase (EC 1.1.1.48) is an enzyme that catalyzes the chemical reaction: D-galactose + NAD+ rightleftharpoons D-galactono-1,4-lactone + NADH + H+. Thus, the two substrates of this enzyme are D-galactose and NAD+, whereas its 3 products are D-galactono-1,4-lactone, NADH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. This enzyme participates in galactose metabolism. An aldose 1-epimerase (EC 5.1.3.3) is an enzyme that catalyzes the chemical reaction:alpha-D-glucose↔ beta-D-glucose. Hence, this enzyme has one substrate, alpha-D-glucose, and one product, beta-D-glucose. This enzyme belongs to the family of isomerases, specifically those racemases and epimerases acting on carbohydrates and derivatives. This enzyme participates in glycolysis and gluconeogenesis.<br /><a href="https://www.creative-enzymes.com/similar/Galactose-Dehydrogenase-Galactose-Mutarotase_295.html" rel="noopener">https://www.creative-enzymes.com/similar/Galactose-Dehydrogenase-Galactose-Mutarotase_295.html</a>]]></description><guid isPermaLink="false">https://api.spreaker.com/episode/14199469</guid><pubDate>Mon, 05 Mar 2018 02:06:34 +0000</pubDate><enclosure url="https://api.spreaker.com/download/episode/14199469/galactose_dehydrogenase.mp3" length="354010" type="audio/mpeg"/><itunes:author>Jack Forst</itunes:author><itunes:subtitle>In enzymology, a galactose 1-dehydrogenase (EC 1.1.1.48) is an enzyme that catalyzes the chemical reaction: D-galactose + NAD+ rightleftharpoons D-galactono-1,4-lactone + NADH + H+. Thus, the two substrates of this enzyme are D-galactose and NAD+,...</itunes:subtitle><itunes:summary><![CDATA[In enzymology, a galactose 1-dehydrogenase (EC 1.1.1.48) is an enzyme that catalyzes the chemical reaction: D-galactose + NAD+ rightleftharpoons D-galactono-1,4-lactone + NADH + H+. Thus, the two substrates of this enzyme are D-galactose and NAD+, whereas its 3 products are D-galactono-1,4-lactone, NADH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. This enzyme participates in galactose metabolism. An aldose 1-epimerase (EC 5.1.3.3) is an enzyme that catalyzes the chemical reaction:alpha-D-glucose↔ beta-D-glucose. Hence, this enzyme has one substrate, alpha-D-glucose, and one product, beta-D-glucose. This enzyme belongs to the family of isomerases, specifically those racemases and epimerases acting on carbohydrates and derivatives. This enzyme participates in glycolysis and gluconeogenesis.<br /><a href="https://www.creative-enzymes.com/similar/Galactose-Dehydrogenase-Galactose-Mutarotase_295.html" rel="noopener">https://www.creative-enzymes.com/similar/Galactose-Dehydrogenase-Galactose-Mutarotase_295.html</a>]]></itunes:summary><itunes:duration>23</itunes:duration><itunes:explicit>clean</itunes:explicit><itunes:image href="https://d3wo5wojvuv7l.cloudfront.net/images.spreaker.com/nuvolari-assets/green_square_mic.jpg"/><itunes:episodeType>full</itunes:episodeType></item><item><title>achromopeptidase</title><link>https://www.spreaker.com/episode/achromopeptidase--14179193</link><description><![CDATA[Lysyl endopeptidase (EC 3.4.21.50, Achromobacter proteinase I, Achromobacter lyticus alkaline proteinase I, protease I, achromopeptidase, lysyl bond specific proteinase) is an enzyme. This enzyme catalyses the following chemical reaction:Preferential cleavage:Lys-, including-Lys-Pro-. This enzyme is isolated from Achromobacter lyticus.<br /><a href="https://www.creative-enzymes.com/product/native-bacteria-achromopeptidase_948.html" rel="noopener">https://www.creative-enzymes.com/product/native-bacteria-achromopeptidase_948.html</a>]]></description><guid isPermaLink="false">https://api.spreaker.com/episode/14179193</guid><pubDate>Fri, 02 Mar 2018 03:34:47 +0000</pubDate><enclosure url="https://api.spreaker.com/download/episode/14179193/achromopeptidase.mp3" length="417958" type="audio/mpeg"/><itunes:author>Jack Forst</itunes:author><itunes:subtitle>Lysyl endopeptidase (EC 3.4.21.50, Achromobacter proteinase I, Achromobacter lyticus alkaline proteinase I, protease I, achromopeptidase, lysyl bond specific proteinase) is an enzyme. This enzyme catalyses the following chemical reaction:Preferential...</itunes:subtitle><itunes:summary><![CDATA[Lysyl endopeptidase (EC 3.4.21.50, Achromobacter proteinase I, Achromobacter lyticus alkaline proteinase I, protease I, achromopeptidase, lysyl bond specific proteinase) is an enzyme. This enzyme catalyses the following chemical reaction:Preferential cleavage:Lys-, including-Lys-Pro-. This enzyme is isolated from Achromobacter lyticus.<br /><a href="https://www.creative-enzymes.com/product/native-bacteria-achromopeptidase_948.html" rel="noopener">https://www.creative-enzymes.com/product/native-bacteria-achromopeptidase_948.html</a>]]></itunes:summary><itunes:duration>27</itunes:duration><itunes:explicit>clean</itunes:explicit><itunes:image href="https://d3wo5wojvuv7l.cloudfront.net/images.spreaker.com/nuvolari-assets/green_square_mic.jpg"/><itunes:episodeType>full</itunes:episodeType></item><item><title>native hnmt enzyme</title><link>https://www.spreaker.com/episode/native-hnmt-enzyme--14170815</link><description><![CDATA[(HNMT) is the enzyme which catalyzes the n-methylation of histamine as follows: Histamine + S-Adenosyl methionine ------> (SAM)methyladed Histamine. The mechanism involves the transfer of an active methyl group from S-Adenosyl methionine (SAM) to histamine. Histamine is present in most of mammalian tissues and HNMT is the enzyme responsible for inactivation of histamine in mammals. Methylation is major route of histamine metabolism. HNMT has been used to measure histamine by radio-enzymatic method. HNMT has been purified from rat kidney. Molecular weight equals 33,400, pH optimum is 8.00-8.25. We have also purified it from bovine kidney which seems to be very similar to rat kidney.]]></description><guid isPermaLink="false">https://api.spreaker.com/episode/14170815</guid><pubDate>Thu, 01 Mar 2018 04:21:49 +0000</pubDate><enclosure url="https://api.spreaker.com/download/episode/14170815/native_hnmt_enzyme.mp3" length="417958" type="audio/mpeg"/><itunes:author>Jack Forst</itunes:author><itunes:subtitle>(HNMT) is the enzyme which catalyzes the n-methylation of histamine as follows: Histamine + S-Adenosyl methionine ------&gt; (SAM)methyladed Histamine. The mechanism involves the transfer of an active methyl group from S-Adenosyl methionine (SAM) to...</itunes:subtitle><itunes:summary><![CDATA[(HNMT) is the enzyme which catalyzes the n-methylation of histamine as follows: Histamine + S-Adenosyl methionine ------> (SAM)methyladed Histamine. The mechanism involves the transfer of an active methyl group from S-Adenosyl methionine (SAM) to histamine. Histamine is present in most of mammalian tissues and HNMT is the enzyme responsible for inactivation of histamine in mammals. Methylation is major route of histamine metabolism. HNMT has been used to measure histamine by radio-enzymatic method. HNMT has been purified from rat kidney. Molecular weight equals 33,400, pH optimum is 8.00-8.25. We have also purified it from bovine kidney which seems to be very similar to rat kidney.]]></itunes:summary><itunes:duration>27</itunes:duration><itunes:explicit>clean</itunes:explicit><itunes:image href="https://d3wo5wojvuv7l.cloudfront.net/images.spreaker.com/nuvolari-assets/green_square_mic.jpg"/><itunes:episodeType>full</itunes:episodeType></item><item><title>map kinase</title><link>https://www.spreaker.com/episode/map-kinase--13998743</link><description><![CDATA[Mitogen-activated protein kinases (MAPK) are protein kinases that are specific to the amino acids serine, threonine, and tyrosine. MAPKs belong to the CMGC (CDK/MAPK/GSK3/CLK) kinase group. MAPKs are involved in directing cellular responses to a diverse array of stimuli, such as mitogens, osmotic stress, heat shock and proinflammatory cytokines. They regulate cell functions including proliferation, gene expression, differentiation, mitosis, cell survival, and apoptosis.<br /><a href="https://www.creative-enzymes.com/similar/MAP-Kinase_438.html" rel="noopener">https://www.creative-enzymes.com/similar/MAP-Kinase_438.html</a>]]></description><guid isPermaLink="false">https://api.spreaker.com/episode/13998743</guid><pubDate>Thu, 08 Feb 2018 03:39:27 +0000</pubDate><enclosure url="https://api.spreaker.com/download/episode/13998743/map_kinase.mp3" length="417958" type="audio/mpeg"/><itunes:author>Jack Forst</itunes:author><itunes:subtitle>Mitogen-activated protein kinases (MAPK) are protein kinases that are specific to the amino acids serine, threonine, and tyrosine. MAPKs belong to the CMGC (CDK/MAPK/GSK3/CLK) kinase group. MAPKs are involved in directing cellular responses to a...</itunes:subtitle><itunes:summary><![CDATA[Mitogen-activated protein kinases (MAPK) are protein kinases that are specific to the amino acids serine, threonine, and tyrosine. MAPKs belong to the CMGC (CDK/MAPK/GSK3/CLK) kinase group. MAPKs are involved in directing cellular responses to a diverse array of stimuli, such as mitogens, osmotic stress, heat shock and proinflammatory cytokines. They regulate cell functions including proliferation, gene expression, differentiation, mitosis, cell survival, and apoptosis.<br /><a href="https://www.creative-enzymes.com/similar/MAP-Kinase_438.html" rel="noopener">https://www.creative-enzymes.com/similar/MAP-Kinase_438.html</a>]]></itunes:summary><itunes:duration>27</itunes:duration><itunes:explicit>clean</itunes:explicit><itunes:image href="https://d3wo5wojvuv7l.cloudfront.net/images.spreaker.com/nuvolari-assets/green_square_mic.jpg"/><itunes:episodeType>full</itunes:episodeType></item><item><title>ferredoxin reductase</title><link>https://www.spreaker.com/episode/ferredoxin-reductase--13989166</link><description><![CDATA[Ferredoxin-NADP+ reductase catalyzes the reversible conversion of reduced ferredoxin to oxidized ferredoxin during photosynthesis. Ferredoxin-NADP (H) reductase constitutes a family of hydrophilic FAD-containing monomeric enzymes that deliver NADPH or low potential one-electron donors to redox-based metabolisms in plastids, mitochondria, and bacteria.<br /><a href="https://www.creative-enzymes.com/similar/FNR_280.html" rel="noopener">https://www.creative-enzymes.com/similar/FNR_280.html</a>]]></description><guid isPermaLink="false">https://api.spreaker.com/episode/13989166</guid><pubDate>Wed, 07 Feb 2018 03:35:43 +0000</pubDate><enclosure url="https://api.spreaker.com/download/episode/13989166/ferredoxin_reductase.mp3" length="417958" type="audio/mpeg"/><itunes:author>Jack Forst</itunes:author><itunes:subtitle>Ferredoxin-NADP+ reductase catalyzes the reversible conversion of reduced ferredoxin to oxidized ferredoxin during photosynthesis. Ferredoxin-NADP (H) reductase constitutes a family of hydrophilic FAD-containing monomeric enzymes that deliver NADPH or...</itunes:subtitle><itunes:summary><![CDATA[Ferredoxin-NADP+ reductase catalyzes the reversible conversion of reduced ferredoxin to oxidized ferredoxin during photosynthesis. Ferredoxin-NADP (H) reductase constitutes a family of hydrophilic FAD-containing monomeric enzymes that deliver NADPH or low potential one-electron donors to redox-based metabolisms in plastids, mitochondria, and bacteria.<br /><a href="https://www.creative-enzymes.com/similar/FNR_280.html" rel="noopener">https://www.creative-enzymes.com/similar/FNR_280.html</a>]]></itunes:summary><itunes:duration>27</itunes:duration><itunes:explicit>clean</itunes:explicit><itunes:image href="https://d3wo5wojvuv7l.cloudfront.net/images.spreaker.com/nuvolari-assets/green_square_mic.jpg"/><itunes:episodeType>full</itunes:episodeType></item><item><title>glucokinase</title><link>https://www.spreaker.com/episode/glucokinase--13988705</link><description><![CDATA[Glucokinase (GK; EC 2.7.1.2) is an enzyme that facilitates phosphorylation of glucose to glucose-6-phosphate. Glucokinase occurs in cells in the liver, pancreas, gut, and brain of humans and most other vertebrates. In each of these organs it plays an important role in the regulation of carbohydrate metabolism by acting as a glucose sensor, triggering shifts in metabolism or cell function in response to rising or falling levels of glucose, such as occur after a meal or when fasting. Mutations of the gene for this enzyme can cause unusual forms of diabetes or hypoglycemia.<br /><a href="https://www.creative-enzymes.com/similar/GCK_302.html" rel="noopener">https://www.creative-enzymes.com/similar/GCK_302.html</a>]]></description><guid isPermaLink="false">https://api.spreaker.com/episode/13988705</guid><pubDate>Wed, 07 Feb 2018 02:13:50 +0000</pubDate><enclosure url="https://api.spreaker.com/download/episode/13988705/glucokinase.mp3" length="417958" type="audio/mpeg"/><itunes:author>Jack Forst</itunes:author><itunes:subtitle>Glucokinase (GK; EC 2.7.1.2) is an enzyme that facilitates phosphorylation of glucose to glucose-6-phosphate. Glucokinase occurs in cells in the liver, pancreas, gut, and brain of humans and most other vertebrates. In each of these organs it plays an...</itunes:subtitle><itunes:summary><![CDATA[Glucokinase (GK; EC 2.7.1.2) is an enzyme that facilitates phosphorylation of glucose to glucose-6-phosphate. Glucokinase occurs in cells in the liver, pancreas, gut, and brain of humans and most other vertebrates. In each of these organs it plays an important role in the regulation of carbohydrate metabolism by acting as a glucose sensor, triggering shifts in metabolism or cell function in response to rising or falling levels of glucose, such as occur after a meal or when fasting. Mutations of the gene for this enzyme can cause unusual forms of diabetes or hypoglycemia.<br /><a href="https://www.creative-enzymes.com/similar/GCK_302.html" rel="noopener">https://www.creative-enzymes.com/similar/GCK_302.html</a>]]></itunes:summary><itunes:duration>27</itunes:duration><itunes:explicit>clean</itunes:explicit><itunes:image href="https://d3wo5wojvuv7l.cloudfront.net/images.spreaker.com/nuvolari-assets/green_square_mic.jpg"/><itunes:episodeType>full</itunes:episodeType></item><item><title>glucoamylase</title><link>https://www.spreaker.com/episode/glucoamylase--13980096</link><description><![CDATA[Glucan 1,4-alpha-glucosidase is an enzyme located on the brush border of the small intestine with system name 4-alpha-D-glucan glucohydrolase. This enzyme catalyses the following chemical reaction: Hydrolysis of terminal (1->4)-linked alpha-D-glucose residues successively from non-reducing ends of the chains with release of beta-D-glucose. Most forms of the enzyme can rapidly hydrolyse 1,6-alpha-D-glycosidic bonds when the next bond in the sequence is 1,4.<br /><a href="https://www.creative-enzymes.com/product/native-rhizopus-sp-glucoamylase_786.html" rel="noopener">https://www.creative-enzymes.com/product/native-rhizopus-sp-glucoamylase_786.html</a>]]></description><guid isPermaLink="false">https://api.spreaker.com/episode/13980096</guid><pubDate>Tue, 06 Feb 2018 02:18:50 +0000</pubDate><enclosure url="https://api.spreaker.com/download/episode/13980096/glucoamylase.mp3" length="417958" type="audio/mpeg"/><itunes:author>Jack Forst</itunes:author><itunes:subtitle>Glucan 1,4-alpha-glucosidase is an enzyme located on the brush border of the small intestine with system name 4-alpha-D-glucan glucohydrolase. This enzyme catalyses the following chemical reaction: Hydrolysis of terminal (1-&gt;4)-linked alpha-D-glucose...</itunes:subtitle><itunes:summary><![CDATA[Glucan 1,4-alpha-glucosidase is an enzyme located on the brush border of the small intestine with system name 4-alpha-D-glucan glucohydrolase. This enzyme catalyses the following chemical reaction: Hydrolysis of terminal (1->4)-linked alpha-D-glucose residues successively from non-reducing ends of the chains with release of beta-D-glucose. Most forms of the enzyme can rapidly hydrolyse 1,6-alpha-D-glycosidic bonds when the next bond in the sequence is 1,4.<br /><a href="https://www.creative-enzymes.com/product/native-rhizopus-sp-glucoamylase_786.html" rel="noopener">https://www.creative-enzymes.com/product/native-rhizopus-sp-glucoamylase_786.html</a>]]></itunes:summary><itunes:duration>27</itunes:duration><itunes:explicit>clean</itunes:explicit><itunes:image href="https://d3wo5wojvuv7l.cloudfront.net/images.spreaker.com/nuvolari-assets/green_square_mic.jpg"/><itunes:episodeType>full</itunes:episodeType></item><item><title>glucose oxidase</title><link>https://www.spreaker.com/episode/glucose-oxidase--13971858</link><description><![CDATA[The glucose oxidase enzyme (GOx) also known as notatin (EC number 1.1.3.4) is an oxido-reductase that catalyses the oxidation of glucose to hydrogen peroxide and D-glucono-δ-lactone. This enzyme is produced by certain species of fungi and insects and displays antibacterial activity when oxygen and glucose are present.<br /><a href="https://www.creative-enzymes.com/product/native-aspergillus-sp-glucose-oxidase_789.html" rel="noopener">https://www.creative-enzymes.com/product/native-aspergillus-sp-glucose-oxidase_789.html</a>]]></description><guid isPermaLink="false">https://api.spreaker.com/episode/13971858</guid><pubDate>Mon, 05 Feb 2018 03:48:08 +0000</pubDate><enclosure url="https://api.spreaker.com/download/episode/13971858/glucose_oxidase.mp3" length="417958" type="audio/mpeg"/><itunes:author>Jack Forst</itunes:author><itunes:subtitle>The glucose oxidase enzyme (GOx) also known as notatin (EC number 1.1.3.4) is an oxido-reductase that catalyses the oxidation of glucose to hydrogen peroxide and D-glucono-δ-lactone. This enzyme is produced by certain species of fungi and insects and...</itunes:subtitle><itunes:summary><![CDATA[The glucose oxidase enzyme (GOx) also known as notatin (EC number 1.1.3.4) is an oxido-reductase that catalyses the oxidation of glucose to hydrogen peroxide and D-glucono-δ-lactone. This enzyme is produced by certain species of fungi and insects and displays antibacterial activity when oxygen and glucose are present.<br /><a href="https://www.creative-enzymes.com/product/native-aspergillus-sp-glucose-oxidase_789.html" rel="noopener">https://www.creative-enzymes.com/product/native-aspergillus-sp-glucose-oxidase_789.html</a>]]></itunes:summary><itunes:duration>27</itunes:duration><itunes:explicit>clean</itunes:explicit><itunes:image href="https://d3wo5wojvuv7l.cloudfront.net/images.spreaker.com/nuvolari-assets/green_square_mic.jpg"/><itunes:episodeType>full</itunes:episodeType></item><item><title>papain powder</title><link>https://www.spreaker.com/episode/papain-powder--13971532</link><description><![CDATA[Papain papaya latex has antifungal activity against C. albicans. It is a cysteine protease that cleaves peptide bonds of basic amino acids, leucine, or glycine.<br /><a href="https://www.creative-enzymes.com/product/native-papaya-latex-papain_963.html" rel="noopener">https://www.creative-enzymes.com/product/native-papaya-latex-papain_963.html</a>]]></description><guid isPermaLink="false">https://api.spreaker.com/episode/13971532</guid><pubDate>Mon, 05 Feb 2018 02:01:33 +0000</pubDate><enclosure url="https://api.spreaker.com/download/episode/13971532/papain_powder.mp3" length="417958" type="audio/mpeg"/><itunes:author>Jack Forst</itunes:author><itunes:subtitle>Papain papaya latex has antifungal activity against C. albicans. It is a cysteine protease that cleaves peptide bonds of basic amino acids, leucine, or glycine.&#13;
https://www.creative-enzymes.com/product/native-papaya-latex-papain_963.html</itunes:subtitle><itunes:summary><![CDATA[Papain papaya latex has antifungal activity against C. albicans. It is a cysteine protease that cleaves peptide bonds of basic amino acids, leucine, or glycine.<br /><a href="https://www.creative-enzymes.com/product/native-papaya-latex-papain_963.html" rel="noopener">https://www.creative-enzymes.com/product/native-papaya-latex-papain_963.html</a>]]></itunes:summary><itunes:duration>27</itunes:duration><itunes:explicit>clean</itunes:explicit><itunes:image href="https://d3wo5wojvuv7l.cloudfront.net/images.spreaker.com/nuvolari-assets/green_square_mic.jpg"/><itunes:episodeType>full</itunes:episodeType></item><item><title>native thio-nadh enzyme</title><link>https://www.spreaker.com/episode/native-thio-nadh-enzyme--13951405</link><description><![CDATA[Spectrophotometric assays are often used to quantify the enzymatic activity of alcohol dehydrogenases, because the reduction of NAD+ to NADH during oxidation of alcohols can be conveniently detected at 340 nm. However, substrate specificity of alcohol dehydrogenases could be very broad, covering many primary and secondary alcohols. For instance, the enzyme from the animal, but not the yeast, also catalyzes oxidation of cyclic secondary alcohols. Therefore, the conventional assay method could be problematic under some the reaction conditions. Furthermore, in some cases the only available sample could be a mixture of alcohol dehydrogenase isozymes or alcohol dehydrogenases with other enzymes, which makes activity measurement even more difficult. Creative Enzymes established robust activity assays that accurately measure the activity of alcohol dehydrogenases under convoluted conditions, such as bovine liver extracts or fermentation lysates, and even in the presence of unconventional substrates other than ethanol. Deep understanding of the properties of alcohol dehydrogenases enables us to face the most challenging activity measurement. In addition to the traditional spectrophotometric assays, we have also developed colorimetric assays that could satisfy special needs such as quick activity screening or reporting enzyme activity in special systems.<br /><a href="https://www.creative-enzymes.com/service/enzyme-activity-measurement-for-alcohol-dehydrogenases-using-spectrophotometric-assays_14.html" rel="noopener">https://www.creative-enzymes.com/service/enzyme-activity-measurement-for-alcohol-dehydrogenases-using-spectrophotometric-assays_14.html</a>]]></description><guid isPermaLink="false">https://api.spreaker.com/episode/13951405</guid><pubDate>Fri, 02 Feb 2018 03:44:12 +0000</pubDate><enclosure url="https://api.spreaker.com/download/episode/13951405/native_thio_nadh_enzyme.mp3" length="417958" type="audio/mpeg"/><itunes:author>Jack Forst</itunes:author><itunes:subtitle>Spectrophotometric assays are often used to quantify the enzymatic activity of alcohol dehydrogenases, because the reduction of NAD+ to NADH during oxidation of alcohols can be conveniently detected at 340 nm. However, substrate specificity of alcohol...</itunes:subtitle><itunes:summary><![CDATA[Spectrophotometric assays are often used to quantify the enzymatic activity of alcohol dehydrogenases, because the reduction of NAD+ to NADH during oxidation of alcohols can be conveniently detected at 340 nm. However, substrate specificity of alcohol dehydrogenases could be very broad, covering many primary and secondary alcohols. For instance, the enzyme from the animal, but not the yeast, also catalyzes oxidation of cyclic secondary alcohols. Therefore, the conventional assay method could be problematic under some the reaction conditions. Furthermore, in some cases the only available sample could be a mixture of alcohol dehydrogenase isozymes or alcohol dehydrogenases with other enzymes, which makes activity measurement even more difficult. Creative Enzymes established robust activity assays that accurately measure the activity of alcohol dehydrogenases under convoluted conditions, such as bovine liver extracts or fermentation lysates, and even in the presence of unconventional substrates other than ethanol. Deep understanding of the properties of alcohol dehydrogenases enables us to face the most challenging activity measurement. In addition to the traditional spectrophotometric assays, we have also developed colorimetric assays that could satisfy special needs such as quick activity screening or reporting enzyme activity in special systems.<br /><a href="https://www.creative-enzymes.com/service/enzyme-activity-measurement-for-alcohol-dehydrogenases-using-spectrophotometric-assays_14.html" rel="noopener">https://www.creative-enzymes.com/service/enzyme-activity-measurement-for-alcohol-dehydrogenases-using-spectrophotometric-assays_14.html</a>]]></itunes:summary><itunes:duration>27</itunes:duration><itunes:explicit>clean</itunes:explicit><itunes:image href="https://d3wo5wojvuv7l.cloudfront.net/images.spreaker.com/nuvolari-assets/green_square_mic.jpg"/><itunes:episodeType>full</itunes:episodeType></item><item><title>β-nadp-k enzyme</title><link>https://www.spreaker.com/episode/b-nadp-k-enzyme--13943317</link><description><![CDATA[β-Nicotinamide adenine dinucleotide 2′-phosphate (NADP+) and β-Nicotinamide adenine dinucleotide 2′-phosphate, reduced (NADPH) comprise a coenzyme redox pair (NADP+:NADPH) involved in a wide range of enzyme catalyzed oxidation reduction reactions. The NADP+/NADPH redox pair facilitates electron transfer in anabolic reactions such as lipid and cholesterol biosynthesis and fatty acyl chain elongation. The NADP+/NADPH redox pair is used in a variety of antioxidation mechanism where it protects agains reactive oxidation species accumulation. NADPH is generated in vivio by the pentose phosphate pathway (PPP).<br /><a href="https://www.creative-enzymes.com/similar/-NADPK_783.html" rel="noopener">https://www.creative-enzymes.com/similar/-NADPK_783.html</a>]]></description><guid isPermaLink="false">https://api.spreaker.com/episode/13943317</guid><pubDate>Thu, 01 Feb 2018 04:12:32 +0000</pubDate><enclosure url="https://api.spreaker.com/download/episode/13943317/nadp_k_enzyme.mp3" length="290062" type="audio/mpeg"/><itunes:author>Jack Forst</itunes:author><itunes:subtitle>β-Nicotinamide adenine dinucleotide 2′-phosphate (NADP+) and β-Nicotinamide adenine dinucleotide 2′-phosphate, reduced (NADPH) comprise a coenzyme redox pair (NADP+:NADPH) involved in a wide range of enzyme catalyzed oxidation reduction reactions. The...</itunes:subtitle><itunes:summary><![CDATA[β-Nicotinamide adenine dinucleotide 2′-phosphate (NADP+) and β-Nicotinamide adenine dinucleotide 2′-phosphate, reduced (NADPH) comprise a coenzyme redox pair (NADP+:NADPH) involved in a wide range of enzyme catalyzed oxidation reduction reactions. The NADP+/NADPH redox pair facilitates electron transfer in anabolic reactions such as lipid and cholesterol biosynthesis and fatty acyl chain elongation. The NADP+/NADPH redox pair is used in a variety of antioxidation mechanism where it protects agains reactive oxidation species accumulation. NADPH is generated in vivio by the pentose phosphate pathway (PPP).<br /><a href="https://www.creative-enzymes.com/similar/-NADPK_783.html" rel="noopener">https://www.creative-enzymes.com/similar/-NADPK_783.html</a>]]></itunes:summary><itunes:duration>19</itunes:duration><itunes:explicit>clean</itunes:explicit><itunes:image href="https://d3wo5wojvuv7l.cloudfront.net/images.spreaker.com/nuvolari-assets/green_square_mic.jpg"/><itunes:episodeType>full</itunes:episodeType></item><item><title>trypsin &amp; chymotrypsin</title><link>https://www.spreaker.com/episode/trypsin-chymotrypsin--13745562</link><description><![CDATA[Trypsin-Chymotrypsin is the co-crystal of Chymotrypsin and Trypsin so it has the properties of both. The activity of hydrolyzing casein is as much as Chymotrypsin. But the activity of its Chemotrypsin to hydrolyze N-Benzoyl-L-tyrosine ethyl ester（BTEE）is three times higher than Chemotrypsin.The activity of hydrolyze ester bond similar to that of Trypsin. It is stable when dry and easy to be inactivated in solutions. The optimum pH is 7.0-8.0. The high purity Trypsin-Chymotrypsin is purified by re-crystallization, and then by Ion Exchange Chromatography and ultra-filtration.<br /><a href="https://www.creative-enzymes.com/similar/trypsinchymotrypsin_697.html" rel="noopener">https://www.creative-enzymes.com/similar/trypsinchymotrypsin_697.html</a>]]></description><guid isPermaLink="false">https://api.spreaker.com/episode/13745562</guid><pubDate>Mon, 08 Jan 2018 03:08:00 +0000</pubDate><enclosure url="https://api.spreaker.com/download/episode/13745562/trypsin_chymotrypsin.mp3" length="161331" type="audio/mpeg"/><itunes:author>Jack Forst</itunes:author><itunes:subtitle>Trypsin-Chymotrypsin is the co-crystal of Chymotrypsin and Trypsin so it has the properties of both. The activity of hydrolyzing casein is as much as Chymotrypsin. But the activity of its Chemotrypsin to hydrolyze N-Benzoyl-L-tyrosine ethyl...</itunes:subtitle><itunes:summary><![CDATA[Trypsin-Chymotrypsin is the co-crystal of Chymotrypsin and Trypsin so it has the properties of both. The activity of hydrolyzing casein is as much as Chymotrypsin. But the activity of its Chemotrypsin to hydrolyze N-Benzoyl-L-tyrosine ethyl ester（BTEE）is three times higher than Chemotrypsin.The activity of hydrolyze ester bond similar to that of Trypsin. It is stable when dry and easy to be inactivated in solutions. The optimum pH is 7.0-8.0. The high purity Trypsin-Chymotrypsin is purified by re-crystallization, and then by Ion Exchange Chromatography and ultra-filtration.<br /><a href="https://www.creative-enzymes.com/similar/trypsinchymotrypsin_697.html" rel="noopener">https://www.creative-enzymes.com/similar/trypsinchymotrypsin_697.html</a>]]></itunes:summary><itunes:duration>11</itunes:duration><itunes:explicit>clean</itunes:explicit><itunes:image href="https://d3wo5wojvuv7l.cloudfront.net/images.spreaker.com/nuvolari-assets/green_square_mic.jpg"/><itunes:episodeType>full</itunes:episodeType></item><item><title>phe-ammonia-lyase</title><link>https://www.spreaker.com/episode/phe-ammonia-lyase--13734495</link><description><![CDATA[Phenylalanine Ammonia-Lyase from Rhodotorula glutinis can be cleaved and inactivated by the proteases chymotrypsin, subtilisin, and trypsin.<br /><a href="https://www.creative-enzymes.com/product/native-rhodotorula-glutinis-phenylalanine-ammonialyase_1354.html" rel="noopener">https://www.creative-enzymes.com/product/native-rhodotorula-glutinis-phenylalanine-ammonialyase_1354.html</a>]]></description><guid isPermaLink="false">https://api.spreaker.com/episode/13734495</guid><pubDate>Sat, 06 Jan 2018 05:44:02 +0000</pubDate><enclosure url="https://api.spreaker.com/download/episode/13734495/phe_ammonia_lyase.mp3" length="161331" type="audio/mpeg"/><itunes:author>Jack Forst</itunes:author><itunes:subtitle>Phenylalanine Ammonia-Lyase from Rhodotorula glutinis can be cleaved and inactivated by the proteases chymotrypsin, subtilisin, and trypsin.
https://www.creative-enzymes.com/product/native-rhodotorula-glutinis-phenylalanine-ammonialyase_1354.html</itunes:subtitle><itunes:summary><![CDATA[Phenylalanine Ammonia-Lyase from Rhodotorula glutinis can be cleaved and inactivated by the proteases chymotrypsin, subtilisin, and trypsin.<br /><a href="https://www.creative-enzymes.com/product/native-rhodotorula-glutinis-phenylalanine-ammonialyase_1354.html" rel="noopener">https://www.creative-enzymes.com/product/native-rhodotorula-glutinis-phenylalanine-ammonialyase_1354.html</a>]]></itunes:summary><itunes:duration>11</itunes:duration><itunes:explicit>clean</itunes:explicit><itunes:image href="https://d3wo5wojvuv7l.cloudfront.net/images.spreaker.com/nuvolari-assets/green_square_mic.jpg"/><itunes:episodeType>full</itunes:episodeType></item><item><title>chymotrypsin</title><link>https://www.spreaker.com/episode/chymotrypsin--13734015</link><description><![CDATA[Chymotrypsin is a digestive enzyme component of pancreatic juice acting in the duodenum where it performs proteolysis, the breakdown of proteins and polypeptides. Chymotrypsin preferentially cleaves peptide amide bonds where the carboxyl side of the amide bond (the P1 position) is a large hydrophobic amino acid (tyrosine, tryptophan, and phenylalanine). These amino acids contain an aromatic ring in their sidechain that fits into a 'hydrophobic pocket' (the S1 position) of the enzyme. It is activated in the presence of trypsin.<br /><a href="https://www.creative-enzymes.com/product/chymotrypsin_823.html" rel="noopener">https://www.creative-enzymes.com/product/chymotrypsin_823.html</a>]]></description><guid isPermaLink="false">https://api.spreaker.com/episode/13734015</guid><pubDate>Sat, 06 Jan 2018 02:55:20 +0000</pubDate><enclosure url="https://api.spreaker.com/download/episode/13734015/chymotrypsin.mp3" length="225697" type="audio/mpeg"/><itunes:author>Jack Forst</itunes:author><itunes:subtitle>Chymotrypsin is a digestive enzyme component of pancreatic juice acting in the duodenum where it performs proteolysis, the breakdown of proteins and polypeptides. Chymotrypsin preferentially cleaves peptide amide bonds where the carboxyl side of the...</itunes:subtitle><itunes:summary><![CDATA[Chymotrypsin is a digestive enzyme component of pancreatic juice acting in the duodenum where it performs proteolysis, the breakdown of proteins and polypeptides. Chymotrypsin preferentially cleaves peptide amide bonds where the carboxyl side of the amide bond (the P1 position) is a large hydrophobic amino acid (tyrosine, tryptophan, and phenylalanine). These amino acids contain an aromatic ring in their sidechain that fits into a 'hydrophobic pocket' (the S1 position) of the enzyme. It is activated in the presence of trypsin.<br /><a href="https://www.creative-enzymes.com/product/chymotrypsin_823.html" rel="noopener">https://www.creative-enzymes.com/product/chymotrypsin_823.html</a>]]></itunes:summary><itunes:duration>15</itunes:duration><itunes:explicit>clean</itunes:explicit><itunes:image href="https://d3wo5wojvuv7l.cloudfront.net/images.spreaker.com/nuvolari-assets/green_square_mic.jpg"/><itunes:episodeType>full</itunes:episodeType></item><item><title>acyl coa oxidase</title><link>https://www.spreaker.com/episode/acyl-coa-oxidase--13733630</link><description><![CDATA[In enzymology, an acyl-CoA oxidase (EC 1.3.3.6) is an enzyme that catalyzes the chemical reaction acyl-CoA + O2↔ trans-2, 3-dehydroacyl-CoA + H2O2. Thus, the two substrates of this enzyme are acyl-CoA and O2, whereas its two products are trans-2, 3-dehydroacyl-CoA and H2O2. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with oxygen as acceptor. This enzyme participates in 3 metabolic pathways: fatty acid metabolism, polyunsaturated fatty acid biosynthesis, and ppar signaling pathway. It employs one cofactor, FAD.<br /><a href="https://www.creative-enzymes.com/product/acylcoa-oxidase-recombinant_3318.html" rel="noopener">https://www.creative-enzymes.com/product/acylcoa-oxidase-recombinant_3318.html</a>]]></description><guid isPermaLink="false">https://api.spreaker.com/episode/13733630</guid><pubDate>Sat, 06 Jan 2018 01:56:03 +0000</pubDate><enclosure url="https://api.spreaker.com/download/episode/13733630/acyl_coa_oxidase.mp3" length="97801" type="audio/mpeg"/><itunes:author>Jack Forst</itunes:author><itunes:subtitle>In enzymology, an acyl-CoA oxidase (EC 1.3.3.6) is an enzyme that catalyzes the chemical reaction acyl-CoA + O2↔ trans-2, 3-dehydroacyl-CoA + H2O2. Thus, the two substrates of this enzyme are acyl-CoA and O2, whereas its two products are trans-2,...</itunes:subtitle><itunes:summary><![CDATA[In enzymology, an acyl-CoA oxidase (EC 1.3.3.6) is an enzyme that catalyzes the chemical reaction acyl-CoA + O2↔ trans-2, 3-dehydroacyl-CoA + H2O2. Thus, the two substrates of this enzyme are acyl-CoA and O2, whereas its two products are trans-2, 3-dehydroacyl-CoA and H2O2. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with oxygen as acceptor. This enzyme participates in 3 metabolic pathways: fatty acid metabolism, polyunsaturated fatty acid biosynthesis, and ppar signaling pathway. It employs one cofactor, FAD.<br /><a href="https://www.creative-enzymes.com/product/acylcoa-oxidase-recombinant_3318.html" rel="noopener">https://www.creative-enzymes.com/product/acylcoa-oxidase-recombinant_3318.html</a>]]></itunes:summary><itunes:duration>7</itunes:duration><itunes:explicit>clean</itunes:explicit><itunes:image href="https://d3wo5wojvuv7l.cloudfront.net/images.spreaker.com/nuvolari-assets/green_square_mic.jpg"/><itunes:episodeType>full</itunes:episodeType></item><item><title>pectinase</title><link>https://www.spreaker.com/episode/pectinase--13727494</link><description><![CDATA[Pectolytic enzyme preparation produced from a selected strain of Aspergillus niger:contains mainly pectintranseliminase, polygalacturonase, and pectinesterase and small amounts of hemicellulases and cellulases. Pectinases hydrolyses pectin, which is a component of the cell wall. They may attack methyl-esterified pectin or de-esterified pectin. It is a source of pectinase activity, also containing cellulase and hemicellulase activities.Pectinase catalyzes the random hydrolysis of a-(1-4)-Dgalactosiduronic linkages in pectin and other galacturonans.<br /><a href="https://www.creative-enzymes.com/product/native-aspergillus-niger-pectinase_958.html" rel="noopener">https://www.creative-enzymes.com/product/native-aspergillus-niger-pectinase_958.html</a>]]></description><guid isPermaLink="false">https://api.spreaker.com/episode/13727494</guid><pubDate>Fri, 05 Jan 2018 04:01:05 +0000</pubDate><enclosure url="https://api.spreaker.com/download/episode/13727494/pectinase.mp3" length="161331" type="audio/mpeg"/><itunes:author>Jack Forst</itunes:author><itunes:subtitle>Pectolytic enzyme preparation produced from a selected strain of Aspergillus niger:contains mainly pectintranseliminase, polygalacturonase, and pectinesterase and small amounts of hemicellulases and cellulases. Pectinases hydrolyses pectin, which is a...</itunes:subtitle><itunes:summary><![CDATA[Pectolytic enzyme preparation produced from a selected strain of Aspergillus niger:contains mainly pectintranseliminase, polygalacturonase, and pectinesterase and small amounts of hemicellulases and cellulases. Pectinases hydrolyses pectin, which is a component of the cell wall. They may attack methyl-esterified pectin or de-esterified pectin. It is a source of pectinase activity, also containing cellulase and hemicellulase activities.Pectinase catalyzes the random hydrolysis of a-(1-4)-Dgalactosiduronic linkages in pectin and other galacturonans.<br /><a href="https://www.creative-enzymes.com/product/native-aspergillus-niger-pectinase_958.html" rel="noopener">https://www.creative-enzymes.com/product/native-aspergillus-niger-pectinase_958.html</a>]]></itunes:summary><itunes:duration>11</itunes:duration><itunes:explicit>clean</itunes:explicit><itunes:image href="https://d3wo5wojvuv7l.cloudfront.net/images.spreaker.com/nuvolari-assets/green_square_mic.jpg"/><itunes:episodeType>full</itunes:episodeType></item><item><title>chondroitinase b</title><link>https://www.spreaker.com/episode/chondroitinase-b--13726832</link><description><![CDATA[In enzymology, a chondroitin B lyase (EC 4.2.2.19) is an enzyme that catalyzes the chemical reaction:Eliminative cleavage of dermatan sulfate containing 1,4-beta-D-hexosaminyl and 1,3-beta-D-glucurosonyl or 1,3-alpha-L-iduronosyl linkages to disaccharides containing 4-deoxy-beta-D-gluc-4-enuronosyl groups to yield a 4,5-unsaturated dermatan-sulfate disaccharide (deltaUA-GalNAc-4S). This enzyme belongs to the family of lyases, specifically those carbon-oxygen lyases acting on polysaccharides.<br /><a href="https://www.creative-enzymes.com/product/chondroitinase-b-from-flavobacterium-heparinum-recombinant_1543.html" rel="noopener">https://www.creative-enzymes.com/product/chondroitinase-b-from-flavobacterium-heparinum-recombinant_1543.html</a>]]></description><guid isPermaLink="false">https://api.spreaker.com/episode/13726832</guid><pubDate>Fri, 05 Jan 2018 02:11:52 +0000</pubDate><enclosure url="https://api.spreaker.com/download/episode/13726832/chondroitinase_b.mp3" length="161331" type="audio/mpeg"/><itunes:author>Jack Forst</itunes:author><itunes:subtitle>In enzymology, a chondroitin B lyase (EC 4.2.2.19) is an enzyme that catalyzes the chemical reaction:Eliminative cleavage of dermatan sulfate containing 1,4-beta-D-hexosaminyl and 1,3-beta-D-glucurosonyl or 1,3-alpha-L-iduronosyl linkages to...</itunes:subtitle><itunes:summary><![CDATA[In enzymology, a chondroitin B lyase (EC 4.2.2.19) is an enzyme that catalyzes the chemical reaction:Eliminative cleavage of dermatan sulfate containing 1,4-beta-D-hexosaminyl and 1,3-beta-D-glucurosonyl or 1,3-alpha-L-iduronosyl linkages to disaccharides containing 4-deoxy-beta-D-gluc-4-enuronosyl groups to yield a 4,5-unsaturated dermatan-sulfate disaccharide (deltaUA-GalNAc-4S). This enzyme belongs to the family of lyases, specifically those carbon-oxygen lyases acting on polysaccharides.<br /><a href="https://www.creative-enzymes.com/product/chondroitinase-b-from-flavobacterium-heparinum-recombinant_1543.html" rel="noopener">https://www.creative-enzymes.com/product/chondroitinase-b-from-flavobacterium-heparinum-recombinant_1543.html</a>]]></itunes:summary><itunes:duration>11</itunes:duration><itunes:explicit>clean</itunes:explicit><itunes:image href="https://d3wo5wojvuv7l.cloudfront.net/images.spreaker.com/nuvolari-assets/green_square_mic.jpg"/><itunes:episodeType>full</itunes:episodeType></item><item><title>phosphoriboisomerase</title><link>https://www.spreaker.com/episode/phosphoriboisomerase--13720872</link><description><![CDATA[Phosphoriboisomerase is responsible for the converstion of ribose 5-phosphate to ribulose 5-phosphate.<br /><a href="https://www.creative-enzymes.com/product/native-spinach-phosphoriboisomerase_1394.html" rel="noopener">https://www.creative-enzymes.com/product/native-spinach-phosphoriboisomerase_1394.html</a>]]></description><guid isPermaLink="false">https://api.spreaker.com/episode/13720872</guid><pubDate>Thu, 04 Jan 2018 03:56:59 +0000</pubDate><enclosure url="https://api.spreaker.com/download/episode/13720872/phosphoriboisomerase.mp3" length="161331" type="audio/mpeg"/><itunes:author>Jack Forst</itunes:author><itunes:subtitle>Phosphoriboisomerase is responsible for the converstion of ribose 5-phosphate to ribulose 5-phosphate.
https://www.creative-enzymes.com/product/native-spinach-phosphoriboisomerase_1394.html</itunes:subtitle><itunes:summary><![CDATA[Phosphoriboisomerase is responsible for the converstion of ribose 5-phosphate to ribulose 5-phosphate.<br /><a href="https://www.creative-enzymes.com/product/native-spinach-phosphoriboisomerase_1394.html" rel="noopener">https://www.creative-enzymes.com/product/native-spinach-phosphoriboisomerase_1394.html</a>]]></itunes:summary><itunes:duration>11</itunes:duration><itunes:explicit>clean</itunes:explicit><itunes:image href="https://d3wo5wojvuv7l.cloudfront.net/images.spreaker.com/nuvolari-assets/green_square_mic.jpg"/><itunes:episodeType>full</itunes:episodeType></item><item><title>pustulanase</title><link>https://www.spreaker.com/episode/pustulanase--13713935</link><description><![CDATA[A thermostable β-1,6-endoglucanase or pustulanase (E.C. 3.2.1.75) which catalyses the cleavage of β-1,6 bonds in pustulan and other beta-glucans containing 1,6 linked glucose units. The enzyme is now a component in a standard assay for beta-glucan from Baker’s yeast as documented in US Pharmacopeia Food and Chemicals Index.<br /><a href="https://www.creative-enzymes.com/similar/pustulanase_622.html" rel="noopener">https://www.creative-enzymes.com/similar/pustulanase_622.html</a>]]></description><guid isPermaLink="false">https://api.spreaker.com/episode/13713935</guid><pubDate>Wed, 03 Jan 2018 04:00:44 +0000</pubDate><enclosure url="https://api.spreaker.com/download/episode/13713935/pustulanase.mp3" length="161331" type="audio/mpeg"/><itunes:author>Jack Forst</itunes:author><itunes:subtitle>A thermostable β-1,6-endoglucanase or pustulanase (E.C. 3.2.1.75) which catalyses the cleavage of β-1,6 bonds in pustulan and other beta-glucans containing 1,6 linked glucose units. The enzyme is now a component in a standard assay for beta-glucan...</itunes:subtitle><itunes:summary><![CDATA[A thermostable β-1,6-endoglucanase or pustulanase (E.C. 3.2.1.75) which catalyses the cleavage of β-1,6 bonds in pustulan and other beta-glucans containing 1,6 linked glucose units. The enzyme is now a component in a standard assay for beta-glucan from Baker’s yeast as documented in US Pharmacopeia Food and Chemicals Index.<br /><a href="https://www.creative-enzymes.com/similar/pustulanase_622.html" rel="noopener">https://www.creative-enzymes.com/similar/pustulanase_622.html</a>]]></itunes:summary><itunes:duration>11</itunes:duration><itunes:explicit>clean</itunes:explicit><itunes:image href="https://d3wo5wojvuv7l.cloudfront.net/images.spreaker.com/nuvolari-assets/green_square_mic.jpg"/><itunes:episodeType>full</itunes:episodeType></item><item><title>acetyltransferase</title><link>https://www.spreaker.com/episode/acetyltransferase--13526485</link><description><![CDATA[Chloramphenicol acetyltransferase (or CAT) is a bacterial enzyme (EC 2.3.1.28) that detoxifies the antibiotic chloramphenicol and is responsible for chloramphenicol resistance in bacteria. This enzyme covalently attaches an acetyl group from acetyl-CoA to chloramphenicol, which prevents chloramphenicol from binding to ribosomes. A histidine residue, located in the C-terminal section of the enzyme, plays a central role in its catalytic mechanism.<br /><a href="https://www.creative-enzymes.com/similar/Chloramphenicol-Acetyltransferase_124.html" rel="noopener">https://www.creative-enzymes.com/similar/Chloramphenicol-Acetyltransferase_124.html</a>]]></description><guid isPermaLink="false">https://api.spreaker.com/episode/13526485</guid><pubDate>Thu, 07 Dec 2017 04:10:18 +0000</pubDate><enclosure url="https://api.spreaker.com/download/episode/13526485/fpg_protein.mp3" length="161331" type="audio/mpeg"/><itunes:author>Jack Forst</itunes:author><itunes:subtitle>Chloramphenicol acetyltransferase (or CAT) is a bacterial enzyme (EC 2.3.1.28) that detoxifies the antibiotic chloramphenicol and is responsible for chloramphenicol resistance in bacteria. This enzyme covalently attaches an acetyl group from...</itunes:subtitle><itunes:summary><![CDATA[Chloramphenicol acetyltransferase (or CAT) is a bacterial enzyme (EC 2.3.1.28) that detoxifies the antibiotic chloramphenicol and is responsible for chloramphenicol resistance in bacteria. This enzyme covalently attaches an acetyl group from acetyl-CoA to chloramphenicol, which prevents chloramphenicol from binding to ribosomes. A histidine residue, located in the C-terminal section of the enzyme, plays a central role in its catalytic mechanism.<br /><a href="https://www.creative-enzymes.com/similar/Chloramphenicol-Acetyltransferase_124.html" rel="noopener">https://www.creative-enzymes.com/similar/Chloramphenicol-Acetyltransferase_124.html</a>]]></itunes:summary><itunes:duration>11</itunes:duration><itunes:explicit>clean</itunes:explicit><itunes:image href="https://d3wo5wojvuv7l.cloudfront.net/images.spreaker.com/nuvolari-assets/green_square_mic.jpg"/><itunes:episodeType>full</itunes:episodeType></item><item><title>carbonic anhydrase</title><link>https://www.spreaker.com/episode/carbonic-anhydrase--13518485</link><description><![CDATA[The carbonic anhydrases (or carbonate dehydratases) form a family of enzymes that catalyze the rapid interconversion of carbon dioxide and water to bicarbonate and protons (or vice versa), a reversible reaction that occurs relatively slowly in the absence of a catalyst. The active site of most carbonic anhydrases contains a zinc ion; they are therefore classified as metalloenzymes.<br /><a href="https://www.creative-enzymes.com/product/native-bovine-carbonic-anhydrase_1545.html" rel="noopener">https://www.creative-enzymes.com/product/native-bovine-carbonic-anhydrase_1545.html</a>]]></description><guid isPermaLink="false">https://api.spreaker.com/episode/13518485</guid><pubDate>Wed, 06 Dec 2017 04:05:40 +0000</pubDate><enclosure url="https://api.spreaker.com/download/episode/13518485/carbonic_anhydrase.mp3" length="161331" type="audio/mpeg"/><itunes:author>Jack Forst</itunes:author><itunes:subtitle>The carbonic anhydrases (or carbonate dehydratases) form a family of enzymes that catalyze the rapid interconversion of carbon dioxide and water to bicarbonate and protons (or vice versa), a reversible reaction that occurs relatively slowly in the...</itunes:subtitle><itunes:summary><![CDATA[The carbonic anhydrases (or carbonate dehydratases) form a family of enzymes that catalyze the rapid interconversion of carbon dioxide and water to bicarbonate and protons (or vice versa), a reversible reaction that occurs relatively slowly in the absence of a catalyst. The active site of most carbonic anhydrases contains a zinc ion; they are therefore classified as metalloenzymes.<br /><a href="https://www.creative-enzymes.com/product/native-bovine-carbonic-anhydrase_1545.html" rel="noopener">https://www.creative-enzymes.com/product/native-bovine-carbonic-anhydrase_1545.html</a>]]></itunes:summary><itunes:duration>11</itunes:duration><itunes:explicit>clean</itunes:explicit><itunes:image href="https://d3wo5wojvuv7l.cloudfront.net/images.spreaker.com/nuvolari-assets/green_square_mic.jpg"/><itunes:episodeType>full</itunes:episodeType></item><item><title>tannase</title><link>https://www.spreaker.com/episode/tannase--13509516</link><description><![CDATA[Tannase catalyzes the hydrolysis of tannic acid to produce gallic acid and glucose.<br /><a href="https://www.creative-enzymes.com/product/native-aspergillus-ficuum-tannase_1460.html" rel="noopener">https://www.creative-enzymes.com/product/native-aspergillus-ficuum-tannase_1460.html</a>]]></description><guid isPermaLink="false">https://api.spreaker.com/episode/13509516</guid><pubDate>Tue, 05 Dec 2017 03:37:25 +0000</pubDate><enclosure url="https://api.spreaker.com/download/episode/13509516/tannase.mp3" length="161331" type="audio/mpeg"/><itunes:author>Jack Forst</itunes:author><itunes:subtitle>Tannase catalyzes the hydrolysis of tannic acid to produce gallic acid and glucose.
https://www.creative-enzymes.com/product/native-aspergillus-ficuum-tannase_1460.html</itunes:subtitle><itunes:summary><![CDATA[Tannase catalyzes the hydrolysis of tannic acid to produce gallic acid and glucose.<br /><a href="https://www.creative-enzymes.com/product/native-aspergillus-ficuum-tannase_1460.html" rel="noopener">https://www.creative-enzymes.com/product/native-aspergillus-ficuum-tannase_1460.html</a>]]></itunes:summary><itunes:duration>11</itunes:duration><itunes:explicit>clean</itunes:explicit><itunes:image href="https://d3wo5wojvuv7l.cloudfront.net/images.spreaker.com/nuvolari-assets/green_square_mic.jpg"/><itunes:episodeType>full</itunes:episodeType></item><item><title>galactosidase enzyme</title><link>https://www.spreaker.com/episode/galactosidase-enzyme--13509125</link><description><![CDATA[β-galactosidase, also called beta-gal or β-gal, is a hydrolase enzyme that catalyzes the hydrolysis of β-galactosides into monosaccharides. Substrates of different β-galactosidases include ganglioside GM1, lactosylceramides, lactose, and various glycoproteins.<br /><a href="https://www.creative-enzymes.com/product/native-escherichia-coli-galactosidase_785.html" rel="noopener">https://www.creative-enzymes.com/product/native-escherichia-coli-galactosidase_785.html</a>]]></description><guid isPermaLink="false">https://api.spreaker.com/episode/13509125</guid><pubDate>Tue, 05 Dec 2017 02:24:12 +0000</pubDate><enclosure url="https://api.spreaker.com/download/episode/13509125/galactosidase_enzyme.mp3" length="225697" type="audio/mpeg"/><itunes:author>Jack Forst</itunes:author><itunes:subtitle>β-galactosidase, also called beta-gal or β-gal, is a hydrolase enzyme that catalyzes the hydrolysis of β-galactosides into monosaccharides. Substrates of different β-galactosidases include ganglioside GM1, lactosylceramides, lactose, and various...</itunes:subtitle><itunes:summary><![CDATA[β-galactosidase, also called beta-gal or β-gal, is a hydrolase enzyme that catalyzes the hydrolysis of β-galactosides into monosaccharides. Substrates of different β-galactosidases include ganglioside GM1, lactosylceramides, lactose, and various glycoproteins.<br /><a href="https://www.creative-enzymes.com/product/native-escherichia-coli-galactosidase_785.html" rel="noopener">https://www.creative-enzymes.com/product/native-escherichia-coli-galactosidase_785.html</a>]]></itunes:summary><itunes:duration>15</itunes:duration><itunes:explicit>clean</itunes:explicit><itunes:image href="https://d3wo5wojvuv7l.cloudfront.net/images.spreaker.com/nuvolari-assets/green_square_mic.jpg"/><itunes:episodeType>full</itunes:episodeType></item><item><title>catalase</title><link>https://www.spreaker.com/episode/catalase--13500531</link><description><![CDATA[Catalase is a common enzyme found in nearly all living organisms, where it functions to catalyze the decomposition of hydrogen peroxide to water and oxygen. Catalase has one of the highest turnover numbers of all enzymes; one molecule of catalase can convert millions of molecules of hydrogen peroxide to water and oxygen per second. Catalase is a tetramer of four polypeptide chains, each over 500 amino acids long. It contains four porphyrin heme (iron) groups that allow the enzyme to react with the hydrogen peroxide. The optimum pH for catalase is approximately 7, while the optimum temperature varies by species.<br /><a href="https://www.creative-enzymes.com/product/native-aspergillus-sp-catalase_727.html" rel="noopener">https://www.creative-enzymes.com/product/native-aspergillus-sp-catalase_727.html</a>]]></description><guid isPermaLink="false">https://api.spreaker.com/episode/13500531</guid><pubDate>Mon, 04 Dec 2017 04:08:35 +0000</pubDate><enclosure url="https://api.spreaker.com/download/episode/13500531/catalase.mp3" length="225697" type="audio/mpeg"/><itunes:author>Jack Forst</itunes:author><itunes:subtitle>Catalase is a common enzyme found in nearly all living organisms, where it functions to catalyze the decomposition of hydrogen peroxide to water and oxygen. Catalase has one of the highest turnover numbers of all enzymes; one molecule of catalase can...</itunes:subtitle><itunes:summary><![CDATA[Catalase is a common enzyme found in nearly all living organisms, where it functions to catalyze the decomposition of hydrogen peroxide to water and oxygen. Catalase has one of the highest turnover numbers of all enzymes; one molecule of catalase can convert millions of molecules of hydrogen peroxide to water and oxygen per second. Catalase is a tetramer of four polypeptide chains, each over 500 amino acids long. It contains four porphyrin heme (iron) groups that allow the enzyme to react with the hydrogen peroxide. The optimum pH for catalase is approximately 7, while the optimum temperature varies by species.<br /><a href="https://www.creative-enzymes.com/product/native-aspergillus-sp-catalase_727.html" rel="noopener">https://www.creative-enzymes.com/product/native-aspergillus-sp-catalase_727.html</a>]]></itunes:summary><itunes:duration>15</itunes:duration><itunes:explicit>clean</itunes:explicit><itunes:image href="https://d3wo5wojvuv7l.cloudfront.net/images.spreaker.com/nuvolari-assets/green_square_mic.jpg"/><itunes:episodeType>full</itunes:episodeType></item><item><title>mannosamine dehydrogenase</title><link>https://www.spreaker.com/episode/mannosamine-dehydrogenase--13500349</link><description><![CDATA[N-acylmannosamine 1-dehydrogenase is involved in sialic acid catabolism in bacteria. The most common form of sialic acid is Neu5Ac (N-acetylneuraminic acid), which is considered as a biomarker for some tumoral and inflammatory states, rendering its quantification in serum important. In microgranisms, Neu5Ac splits to pyruvate and ManNAc. Usually, biological processes converse this intermediate into fructose 1,6-bisphosphate through a series of enzymes catalyze. However, there is a unique pathway exists in a soil bacterium Flavobacterium sp. 141-8, which is correlated to its ability to grow on ManNAc as the sole carbon source. The unique enzyme is N-acyl-D-mannosamine dehydrogenase, which has not been found in any other microorganism. Little studies on this unique pathway has been done, and the consecutive reactions following N-acetylmannosaminic acid still remain unknown. Thus, scientists are keen to understand this enzyme and pathway. This enzyme is currently sold commercially as a part of the sialic acid assay kit for clinical testing. While many other potential applications awaits until the enzyme is better studied and characterized. Whether your interest lies in pathway studies or enzyme development from new sources, Creative Enzymes will support your research by providing accurate enzyme assay services.<br /><a href="https://www.creative-enzymes.com/service/Enzyme-Activity-Measurement-Of-NAcylmannosamine-1Dehydrogenase-Using-Spectrophotometric-Assays_105.html" rel="noopener">https://www.creative-enzymes.com/service/Enzyme-Activity-Measurement-Of-NAcylmannosamine-1Dehydrogenase-Using-Spectrophotometric-Assays_105.html</a>]]></description><guid isPermaLink="false">https://api.spreaker.com/episode/13500349</guid><pubDate>Mon, 04 Dec 2017 03:23:24 +0000</pubDate><enclosure url="https://api.spreaker.com/download/episode/13500349/mannosamine_dehydrogenase.mp3" length="225697" type="audio/mpeg"/><itunes:author>Jack Forst</itunes:author><itunes:subtitle>N-acylmannosamine 1-dehydrogenase is involved in sialic acid catabolism in bacteria. The most common form of sialic acid is Neu5Ac (N-acetylneuraminic acid), which is considered as a biomarker for some tumoral and inflammatory states, rendering its...</itunes:subtitle><itunes:summary><![CDATA[N-acylmannosamine 1-dehydrogenase is involved in sialic acid catabolism in bacteria. The most common form of sialic acid is Neu5Ac (N-acetylneuraminic acid), which is considered as a biomarker for some tumoral and inflammatory states, rendering its quantification in serum important. In microgranisms, Neu5Ac splits to pyruvate and ManNAc. Usually, biological processes converse this intermediate into fructose 1,6-bisphosphate through a series of enzymes catalyze. However, there is a unique pathway exists in a soil bacterium Flavobacterium sp. 141-8, which is correlated to its ability to grow on ManNAc as the sole carbon source. The unique enzyme is N-acyl-D-mannosamine dehydrogenase, which has not been found in any other microorganism. Little studies on this unique pathway has been done, and the consecutive reactions following N-acetylmannosaminic acid still remain unknown. Thus, scientists are keen to understand this enzyme and pathway. This enzyme is currently sold commercially as a part of the sialic acid assay kit for clinical testing. While many other potential applications awaits until the enzyme is better studied and characterized. Whether your interest lies in pathway studies or enzyme development from new sources, Creative Enzymes will support your research by providing accurate enzyme assay services.<br /><a href="https://www.creative-enzymes.com/service/Enzyme-Activity-Measurement-Of-NAcylmannosamine-1Dehydrogenase-Using-Spectrophotometric-Assays_105.html" rel="noopener">https://www.creative-enzymes.com/service/Enzyme-Activity-Measurement-Of-NAcylmannosamine-1Dehydrogenase-Using-Spectrophotometric-Assays_105.html</a>]]></itunes:summary><itunes:duration>15</itunes:duration><itunes:explicit>clean</itunes:explicit><itunes:image href="https://d3wo5wojvuv7l.cloudfront.net/images.spreaker.com/nuvolari-assets/green_square_mic.jpg"/><itunes:episodeType>full</itunes:episodeType></item><item><title>fpg protein</title><link>https://www.spreaker.com/episode/fpg-protein--13480264</link><description><![CDATA[Fpg protein, a key enzyme in the DNA base excision repair pathway (BER), catalyses the excision of a broad spectrum of modified purines such as formamidopyrimidine (Fapy) and 8-oxoguanine (8-oxo-G). Fpg possess both DNA glycosylase activity that removes the mutated base and AP-lyase activity that releases ribose, leaving both 5'-and 3'-phosphorylated ends in the DNA. Several analytical methods based on Fpg protein activity in vitro were developed for detection and quantitation of oxidative damage to DNA mainly for FapyA, FapyG and 8-oxo-G. The fpg gene was cloned by Boiteux, et al. Fpg protein possess a zinc finger motif at its C-terminus (one zinc atom per molecule). This region is responsible for the DNA binding and AP-lyase activity. In addition, its N-terminal proline was found to act as a nucleophile to produce a Schiff base intermediate, which is essential for enzyme action.<br /><a href="https://www.creative-enzymes.com/product/fpg-protein-from-escherichia-coli-recombinant_1177.html" rel="noopener">https://www.creative-enzymes.com/product/fpg-protein-from-escherichia-coli-recombinant_1177.html</a>]]></description><guid isPermaLink="false">https://api.spreaker.com/episode/13480264</guid><pubDate>Fri, 01 Dec 2017 08:22:02 +0000</pubDate><enclosure url="https://api.spreaker.com/download/episode/13480264/fpg_protein.mp3" length="161331" type="audio/mpeg"/><itunes:author>Jack Forst</itunes:author><itunes:subtitle>Fpg protein, a key enzyme in the DNA base excision repair pathway (BER), catalyses the excision of a broad spectrum of modified purines such as formamidopyrimidine (Fapy) and 8-oxoguanine (8-oxo-G). Fpg possess both DNA glycosylase activity that...</itunes:subtitle><itunes:summary><![CDATA[Fpg protein, a key enzyme in the DNA base excision repair pathway (BER), catalyses the excision of a broad spectrum of modified purines such as formamidopyrimidine (Fapy) and 8-oxoguanine (8-oxo-G). Fpg possess both DNA glycosylase activity that removes the mutated base and AP-lyase activity that releases ribose, leaving both 5'-and 3'-phosphorylated ends in the DNA. Several analytical methods based on Fpg protein activity in vitro were developed for detection and quantitation of oxidative damage to DNA mainly for FapyA, FapyG and 8-oxo-G. The fpg gene was cloned by Boiteux, et al. Fpg protein possess a zinc finger motif at its C-terminus (one zinc atom per molecule). This region is responsible for the DNA binding and AP-lyase activity. In addition, its N-terminal proline was found to act as a nucleophile to produce a Schiff base intermediate, which is essential for enzyme action.<br /><a href="https://www.creative-enzymes.com/product/fpg-protein-from-escherichia-coli-recombinant_1177.html" rel="noopener">https://www.creative-enzymes.com/product/fpg-protein-from-escherichia-coli-recombinant_1177.html</a>]]></itunes:summary><itunes:duration>11</itunes:duration><itunes:explicit>clean</itunes:explicit><itunes:image href="https://d3wo5wojvuv7l.cloudfront.net/images.spreaker.com/nuvolari-assets/green_square_mic.jpg"/><itunes:episodeType>full</itunes:episodeType></item><item><title>carboxypeptidase p</title><link>https://www.spreaker.com/episode/carboxypeptidase-p--13479759</link><description><![CDATA[Membrane Pro-Xaa carboxypeptidase (EC 3.4.17.16, carboxypeptidase P, microsomal carboxypeptidase) is an enzyme. This enzyme catalyses the following chemical reaction:Release of a C-terminal residue other than proline, by preferential cleavage of a prolyl bond. This is one of the renal brush border exopeptidases.<br /><a href="https://www.creative-enzymes.com/product/native-penicillium-janthinellum-carboxypeptidase-p_1588.html" rel="noopener">https://www.creative-enzymes.com/product/native-penicillium-janthinellum-carboxypeptidase-p_1588.html</a>]]></description><guid isPermaLink="false">https://api.spreaker.com/episode/13479759</guid><pubDate>Fri, 01 Dec 2017 06:36:24 +0000</pubDate><enclosure url="https://api.spreaker.com/download/episode/13479759/carboxypeptidase_p.mp3" length="161331" type="audio/mpeg"/><itunes:author>Jack Forst</itunes:author><itunes:subtitle>Membrane Pro-Xaa carboxypeptidase (EC 3.4.17.16, carboxypeptidase P, microsomal carboxypeptidase) is an enzyme. This enzyme catalyses the following chemical reaction:Release of a C-terminal residue other than proline, by preferential cleavage of a...</itunes:subtitle><itunes:summary><![CDATA[Membrane Pro-Xaa carboxypeptidase (EC 3.4.17.16, carboxypeptidase P, microsomal carboxypeptidase) is an enzyme. This enzyme catalyses the following chemical reaction:Release of a C-terminal residue other than proline, by preferential cleavage of a prolyl bond. This is one of the renal brush border exopeptidases.<br /><a href="https://www.creative-enzymes.com/product/native-penicillium-janthinellum-carboxypeptidase-p_1588.html" rel="noopener">https://www.creative-enzymes.com/product/native-penicillium-janthinellum-carboxypeptidase-p_1588.html</a>]]></itunes:summary><itunes:duration>11</itunes:duration><itunes:explicit>clean</itunes:explicit><itunes:image href="https://d3wo5wojvuv7l.cloudfront.net/images.spreaker.com/nuvolari-assets/green_square_mic.jpg"/><itunes:episodeType>full</itunes:episodeType></item><item><title>pepsin powder</title><link>https://www.spreaker.com/episode/pepsin-powder--13447082</link><description><![CDATA[Pepsin is one of the principal protein degrading or proteolytic enzymes in the digestive system. During the process of digestion, Pepsin acts on the complex dietary protein and breaks up into peptides and amino acids which can be readily absorbed by the intestinal lining. It helps in digestive disturbance in general and as a result of impaired production of gastric juice. It acts as an adjunct in the treatment of anemic conditions, especially during slimming diet when protein intake increases. It is used as research tool in protein analysis and as digestive syrup in heart burn, acid indigestion and sour stomach. It is also used in tablets for increasing appetite and in the preparation of cheese and other protein-containing foods.<br /><a href="https://www.creative-enzymes.com/product/Native-Porcine-Pepsin_1726.html" rel="noopener">https://www.creative-enzymes.com/product/Native-Porcine-Pepsin_1726.html</a>]]></description><guid isPermaLink="false">https://api.spreaker.com/episode/13447082</guid><pubDate>Tue, 28 Nov 2017 06:18:30 +0000</pubDate><enclosure url="https://api.spreaker.com/download/episode/13447082/pepsin.mp3" length="161331" type="audio/mpeg"/><itunes:author>Jack Forst</itunes:author><itunes:subtitle>Pepsin is one of the principal protein degrading or proteolytic enzymes in the digestive system. During the process of digestion, Pepsin acts on the complex dietary protein and breaks up into peptides and amino acids which can be readily absorbed by...</itunes:subtitle><itunes:summary><![CDATA[Pepsin is one of the principal protein degrading or proteolytic enzymes in the digestive system. During the process of digestion, Pepsin acts on the complex dietary protein and breaks up into peptides and amino acids which can be readily absorbed by the intestinal lining. It helps in digestive disturbance in general and as a result of impaired production of gastric juice. It acts as an adjunct in the treatment of anemic conditions, especially during slimming diet when protein intake increases. It is used as research tool in protein analysis and as digestive syrup in heart burn, acid indigestion and sour stomach. It is also used in tablets for increasing appetite and in the preparation of cheese and other protein-containing foods.<br /><a href="https://www.creative-enzymes.com/product/Native-Porcine-Pepsin_1726.html" rel="noopener">https://www.creative-enzymes.com/product/Native-Porcine-Pepsin_1726.html</a>]]></itunes:summary><itunes:duration>11</itunes:duration><itunes:explicit>clean</itunes:explicit><itunes:image href="https://d3wo5wojvuv7l.cloudfront.net/images.spreaker.com/nuvolari-assets/green_square_mic.jpg"/><itunes:episodeType>full</itunes:episodeType></item><item><title>glucoamylase</title><link>https://www.spreaker.com/episode/glucoamylase--13446969</link><description><![CDATA[Glucan 1,4-alpha-glucosidase is an enzyme located on the brush border of the small intestine with system name 4-alpha-D-glucan glucohydrolase. This enzyme catalyses the following chemical reaction: Hydrolysis of terminal (1->4)-linked alpha-D-glucose residues successively from non-reducing ends of the chains with release of beta-D-glucose. Most forms of the enzyme can rapidly hydrolyse 1,6-alpha-D-glycosidic bonds when the next bond in the sequence is 1,4.<br /><a href="https://www.creative-enzymes.com/product/Native-Rhizopus-Sp-Glucoamylase_786.html" rel="noopener">https://www.creative-enzymes.com/product/Native-Rhizopus-Sp-Glucoamylase_786.html</a>]]></description><guid isPermaLink="false">https://api.spreaker.com/episode/13446969</guid><pubDate>Tue, 28 Nov 2017 05:49:37 +0000</pubDate><enclosure url="https://api.spreaker.com/download/episode/13446969/glucoamylase_enzyme.mp3" length="161331" type="audio/mpeg"/><itunes:author>Jack Forst</itunes:author><itunes:subtitle>Glucan 1,4-alpha-glucosidase is an enzyme located on the brush border of the small intestine with system name 4-alpha-D-glucan glucohydrolase. This enzyme catalyses the following chemical reaction: Hydrolysis of terminal (1-&gt;4)-linked alpha-D-glucose...</itunes:subtitle><itunes:summary><![CDATA[Glucan 1,4-alpha-glucosidase is an enzyme located on the brush border of the small intestine with system name 4-alpha-D-glucan glucohydrolase. This enzyme catalyses the following chemical reaction: Hydrolysis of terminal (1->4)-linked alpha-D-glucose residues successively from non-reducing ends of the chains with release of beta-D-glucose. Most forms of the enzyme can rapidly hydrolyse 1,6-alpha-D-glycosidic bonds when the next bond in the sequence is 1,4.<br /><a href="https://www.creative-enzymes.com/product/Native-Rhizopus-Sp-Glucoamylase_786.html" rel="noopener">https://www.creative-enzymes.com/product/Native-Rhizopus-Sp-Glucoamylase_786.html</a>]]></itunes:summary><itunes:duration>11</itunes:duration><itunes:explicit>clean</itunes:explicit><itunes:image href="https://d3wo5wojvuv7l.cloudfront.net/images.spreaker.com/nuvolari-assets/green_square_mic.jpg"/><itunes:episodeType>full</itunes:episodeType></item><item><title>Molecular-Mechanism-of-ATP-synthesis_U_mZGTB5uKg</title><link>https://www.spreaker.com/episode/molecular-mechanism-of-atp-synthesis-u-mzgtb5ukg--12570168</link><description><![CDATA[Native β-nad enzyme is a coenzyme found in all living cells. The compound is a dinucleotide, because it consists of two nucleotides joined through their phosphate groups. One nucleotide contains an adenine base and the other nicotinamide. Nicotinamide adenine dinucleotide exists in two forms, an oxidized and reduced form abbreviated as NAD+ and NADH respectively.<br /><br /><a href="http://www.creative-enzymes.com/similar/-NAD_780.html" rel="noopener">http://www.creative-enzymes.com/similar/-NAD_780.html</a>]]></description><guid isPermaLink="false">https://api.spreaker.com/episode/12570168</guid><pubDate>Mon, 14 Aug 2017 07:42:04 +0000</pubDate><enclosure url="https://api.spreaker.com/download/episode/12570168/molecular_mechanism_of_atp_synthesis_u_mzgtb5ukg.mp3" length="2203586" type="audio/mpeg"/><itunes:author>Jack Forst</itunes:author><itunes:subtitle>Native β-nad enzyme is a coenzyme found in all living cells. The compound is a dinucleotide, because it consists of two nucleotides joined through their phosphate groups. One nucleotide contains an adenine base and the other nicotinamide. Nicotinamide...</itunes:subtitle><itunes:summary><![CDATA[Native β-nad enzyme is a coenzyme found in all living cells. The compound is a dinucleotide, because it consists of two nucleotides joined through their phosphate groups. One nucleotide contains an adenine base and the other nicotinamide. Nicotinamide adenine dinucleotide exists in two forms, an oxidized and reduced form abbreviated as NAD+ and NADH respectively.<br /><br /><a href="http://www.creative-enzymes.com/similar/-NAD_780.html" rel="noopener">http://www.creative-enzymes.com/similar/-NAD_780.html</a>]]></itunes:summary><itunes:duration>134</itunes:duration><itunes:keywords>native β-nad enzyme</itunes:keywords><itunes:explicit>clean</itunes:explicit><itunes:image href="https://d3wo5wojvuv7l.cloudfront.net/images.spreaker.com/nuvolari-assets/green_square_mic.jpg"/><itunes:episodeType>full</itunes:episodeType></item><item><title>Glucosidase-Protein_Q4WKt57Q0js</title><link>https://www.spreaker.com/episode/glucosidase-protein-q4wkt57q0js--12334688</link><description><![CDATA[Together with glycosyltransferases, glycosidases form the major catalytic machinery for the synthesis and breakage of glycosidic bonds.<br /><a href="http://www.creative-enzymes.com/product/native-microorganism-glucosidase-maltase-_790.html" rel="noopener">http://www.creative-enzymes.com/product/native-microorganism-glucosidase-maltase-_790.html</a>]]></description><guid isPermaLink="false">https://api.spreaker.com/episode/12334688</guid><pubDate>Wed, 12 Jul 2017 08:04:40 +0000</pubDate><enclosure url="https://api.spreaker.com/download/episode/12334688/glucosidase_protein_q4wkt57q0js.mp3" length="0" type="audio/mpeg"/><itunes:author>Jack Forst</itunes:author><itunes:subtitle>Together with glycosyltransferases, glycosidases form the major catalytic machinery for the synthesis and breakage of glycosidic bonds.
http://www.creative-enzymes.com/product/native-microorganism-glucosidase-maltase-_790.html</itunes:subtitle><itunes:summary><![CDATA[Together with glycosyltransferases, glycosidases form the major catalytic machinery for the synthesis and breakage of glycosidic bonds.<br /><a href="http://www.creative-enzymes.com/product/native-microorganism-glucosidase-maltase-_790.html" rel="noopener">http://www.creative-enzymes.com/product/native-microorganism-glucosidase-maltase-_790.html</a>]]></itunes:summary><itunes:duration>44</itunes:duration><itunes:keywords>glucosidase alpha</itunes:keywords><itunes:explicit>clean</itunes:explicit><itunes:image href="https://d3wo5wojvuv7l.cloudfront.net/images.spreaker.com/nuvolari-assets/green_square_mic.jpg"/><itunes:episodeType>full</itunes:episodeType></item><item><title>Xanthohumol-Isoxanthohumol-frequency-cyclization-DFT-Gaussian_d51X57wc4_Q</title><link>https://www.spreaker.com/episode/xanthohumol-isoxanthohumol-frequency-cyclization-dft-gaussian-d51x57wc4-q--12334679</link><description><![CDATA[Xanthohumol may be dissolved in DMSO (35mg/ml) or Ethanol (35mg/ml).<br /><a href="http://www.creative-enzymes.com/product/Xanthohumol_3007.html" rel="noopener">http://www.creative-enzymes.com/product/Xanthohumol_3007.html</a>]]></description><guid isPermaLink="false">https://api.spreaker.com/episode/12334679</guid><pubDate>Wed, 12 Jul 2017 08:00:40 +0000</pubDate><enclosure url="https://api.spreaker.com/download/episode/12334679/xanthohumol_isoxanthohumol_frequency_cyclization_dft_gaussian_d51x57wc4_q.mp3" length="0" type="audio/mpeg"/><itunes:author>Jack Forst</itunes:author><itunes:subtitle>Xanthohumol may be dissolved in DMSO (35mg/ml) or Ethanol (35mg/ml).
http://www.creative-enzymes.com/product/Xanthohumol_3007.html</itunes:subtitle><itunes:summary><![CDATA[Xanthohumol may be dissolved in DMSO (35mg/ml) or Ethanol (35mg/ml).<br /><a href="http://www.creative-enzymes.com/product/Xanthohumol_3007.html" rel="noopener">http://www.creative-enzymes.com/product/Xanthohumol_3007.html</a>]]></itunes:summary><itunes:duration>21</itunes:duration><itunes:keywords>xanthohumol</itunes:keywords><itunes:explicit>clean</itunes:explicit><itunes:image href="https://d3wo5wojvuv7l.cloudfront.net/images.spreaker.com/nuvolari-assets/green_square_mic.jpg"/><itunes:episodeType>full</itunes:episodeType></item><item><title>How-to-use-MTP-Kit-Mifepristone-and-Misoprostol-Pill_wr-6ZyI7cYI</title><link>https://www.spreaker.com/episode/how-to-use-mtp-kit-mifepristone-and-misoprostol-pill-wr-6zyi7cyi--12334668</link><description><![CDATA[Mifepristone is progesterone receptor antagonist which stimulates prolactin secretion and also acts as Pgp inhibitor.<br /><a href="http://www.creative-enzymes.com/product/Mifepristone_2567.html" rel="noopener">http://www.creative-enzymes.com/product/Mifepristone_2567.html</a>]]></description><guid isPermaLink="false">https://api.spreaker.com/episode/12334668</guid><pubDate>Wed, 12 Jul 2017 07:58:27 +0000</pubDate><enclosure url="https://api.spreaker.com/download/episode/12334668/how_to_use_mtp_kit_mifepristone_and_misoprostol_pill_wr_6zyi7cyi.mp3" length="0" type="audio/mpeg"/><itunes:author>Jack Forst</itunes:author><itunes:subtitle>Mifepristone is progesterone receptor antagonist which stimulates prolactin secretion and also acts as Pgp inhibitor.
http://www.creative-enzymes.com/product/Mifepristone_2567.html</itunes:subtitle><itunes:summary><![CDATA[Mifepristone is progesterone receptor antagonist which stimulates prolactin secretion and also acts as Pgp inhibitor.<br /><a href="http://www.creative-enzymes.com/product/Mifepristone_2567.html" rel="noopener">http://www.creative-enzymes.com/product/Mifepristone_2567.html</a>]]></itunes:summary><itunes:duration>56</itunes:duration><itunes:keywords>mifepristone</itunes:keywords><itunes:explicit>clean</itunes:explicit><itunes:image href="https://d3wo5wojvuv7l.cloudfront.net/images.spreaker.com/nuvolari-assets/green_square_mic.jpg"/><itunes:episodeType>full</itunes:episodeType></item><item><title>MUSE alprostadil</title><link>https://www.spreaker.com/episode/muse-alprostadil--12044868</link><description><![CDATA[Muse Suppository is used for erectile dysfunction, weak erections, impotence and other conditions.<br /><a href="http://www.creative-enzymes.com/product/Alprostadil_3135.html" rel="noopener">http://www.creative-enzymes.com/product/Alprostadil_3135.html</a>]]></description><guid isPermaLink="false">https://api.spreaker.com/episode/12044868</guid><pubDate>Tue, 06 Jun 2017 09:02:51 +0000</pubDate><enclosure url="https://api.spreaker.com/download/episode/12044868/muse_alprostadil.mp3" length="0" type="audio/mpeg"/><itunes:author>Jack Forst</itunes:author><itunes:subtitle>Muse Suppository is used for erectile dysfunction, weak erections, impotence and other conditions.
http://www.creative-enzymes.com/product/Alprostadil_3135.html</itunes:subtitle><itunes:summary><![CDATA[Muse Suppository is used for erectile dysfunction, weak erections, impotence and other conditions.<br /><a href="http://www.creative-enzymes.com/product/Alprostadil_3135.html" rel="noopener">http://www.creative-enzymes.com/product/Alprostadil_3135.html</a>]]></itunes:summary><itunes:duration>550</itunes:duration><itunes:keywords>muse suppository</itunes:keywords><itunes:explicit>clean</itunes:explicit><itunes:image href="https://d3wo5wojvuv7l.cloudfront.net/images.spreaker.com/nuvolari-assets/green_square_mic.jpg"/><itunes:episodeType>full</itunes:episodeType></item><item><title>Doxycycline Treats Bacterial Infections and Prevents Malaria Infections - Overview</title><link>https://www.spreaker.com/episode/doxycycline-treats-bacterial-infections-and-prevents-malaria-infections-overview--12044855</link><description><![CDATA[Find patient medical information for Doxycycline hyclate on WebMD including its uses, side effects and safety, interactions, pictures, warnings and user ratings.<a href="http://www.creative-enzymes.com/product/Doxycycline-Hyclate_2517.html" rel="noopener">http://www.creative-enzymes.com/product/Doxycycline-Hyclate_2517.html</a>]]></description><guid isPermaLink="false">https://api.spreaker.com/episode/12044855</guid><pubDate>Tue, 06 Jun 2017 08:58:40 +0000</pubDate><enclosure url="https://api.spreaker.com/download/episode/12044855/doxycycline_treats_bacterial_infections_and_prevents_malaria_infections_overview.mp3" length="0" type="audio/mpeg"/><itunes:author>Jack Forst</itunes:author><itunes:subtitle>Find patient medical information for Doxycycline hyclate on WebMD including its uses, side effects and safety, interactions, pictures, warnings and user ratings.http://www.creative-enzymes.com/product/Doxycycline-Hyclate_2517.html</itunes:subtitle><itunes:summary><![CDATA[Find patient medical information for Doxycycline hyclate on WebMD including its uses, side effects and safety, interactions, pictures, warnings and user ratings.<a href="http://www.creative-enzymes.com/product/Doxycycline-Hyclate_2517.html" rel="noopener">http://www.creative-enzymes.com/product/Doxycycline-Hyclate_2517.html</a>]]></itunes:summary><itunes:duration>61</itunes:duration><itunes:keywords>doxycycline hyclate</itunes:keywords><itunes:explicit>clean</itunes:explicit><itunes:image href="https://d3wo5wojvuv7l.cloudfront.net/images.spreaker.com/nuvolari-assets/green_square_mic.jpg"/><itunes:episodeType>full</itunes:episodeType></item><item><title>abortion mifepristone misoprostol</title><link>https://www.spreaker.com/episode/abortion-mifepristone-misoprostol--12044843</link><description><![CDATA[Mifepristone, also known as RU-486, is a medication typically used with misoprostol to bring about an abortion.<br /><a href="http://www.creative-enzymes.com/product/Mifepristone_2567.html" rel="noopener">http://www.creative-enzymes.com/product/Mifepristone_2567.html</a>]]></description><guid isPermaLink="false">https://api.spreaker.com/episode/12044843</guid><pubDate>Tue, 06 Jun 2017 08:53:19 +0000</pubDate><enclosure url="https://api.spreaker.com/download/episode/12044843/abortion_mifepristone_misoprostol.mp3" length="0" type="audio/mpeg"/><itunes:author>Jack Forst</itunes:author><itunes:subtitle>Mifepristone, also known as RU-486, is a medication typically used with misoprostol to bring about an abortion.
http://www.creative-enzymes.com/product/Mifepristone_2567.html</itunes:subtitle><itunes:summary><![CDATA[Mifepristone, also known as RU-486, is a medication typically used with misoprostol to bring about an abortion.<br /><a href="http://www.creative-enzymes.com/product/Mifepristone_2567.html" rel="noopener">http://www.creative-enzymes.com/product/Mifepristone_2567.html</a>]]></itunes:summary><itunes:duration>190</itunes:duration><itunes:keywords>mifepristone</itunes:keywords><itunes:explicit>clean</itunes:explicit><itunes:image href="https://d3wo5wojvuv7l.cloudfront.net/images.spreaker.com/nuvolari-assets/green_square_mic.jpg"/><itunes:episodeType>full</itunes:episodeType></item><item><title>Benefits of Papaya and Papain Enzymes Innerzyme Papaya Enzyme Chewable Bloating Gas Heartburn</title><link>https://www.spreaker.com/episode/benefits-of-papaya-and-papain-enzymes-innerzyme-papaya-enzyme-chewable-bloating-gas-heartburn--11950088</link><description><![CDATA[Papain papaya enzyme latex has antifungal activity against C. albicans. It is a cysteine protease that cleaves peptide bonds of basic amino acids, leucine, or glycine.<br /><a href="http://www.creative-enzymes.com/product/native-papaya-latex-papain_963.html" rel="noopener">http://www.creative-enzymes.com/product/native-papaya-latex-papain_963.html</a>]]></description><guid isPermaLink="false">https://api.spreaker.com/episode/11950088</guid><pubDate>Thu, 25 May 2017 08:29:26 +0000</pubDate><enclosure url="https://api.spreaker.com/download/episode/11950088/benefits_of_papaya_and_papain_enzymes_innerzyme_papaya_enzyme_chewable_bloating_gas_heartburn.mp3" length="0" type="audio/mpeg"/><itunes:author>Jack Forst</itunes:author><itunes:subtitle>Papain papaya enzyme latex has antifungal activity against C. albicans. It is a cysteine protease that cleaves peptide bonds of basic amino acids, leucine, or glycine.
http://www.creative-enzymes.com/product/native-papaya-latex-papain_963.html</itunes:subtitle><itunes:summary><![CDATA[Papain papaya enzyme latex has antifungal activity against C. albicans. It is a cysteine protease that cleaves peptide bonds of basic amino acids, leucine, or glycine.<br /><a href="http://www.creative-enzymes.com/product/native-papaya-latex-papain_963.html" rel="noopener">http://www.creative-enzymes.com/product/native-papaya-latex-papain_963.html</a>]]></itunes:summary><itunes:duration>124</itunes:duration><itunes:explicit>clean</itunes:explicit><itunes:image href="https://d3wo5wojvuv7l.cloudfront.net/images.spreaker.com/nuvolari-assets/green_square_mic.jpg"/><itunes:episodeType>full</itunes:episodeType></item><item><title>Purine Nucleoside Phosphorylase- Physiology Biochemistry and Mechanism</title><link>https://www.spreaker.com/episode/purine-nucleoside-phosphorylase-physiology-biochemistry-and-mechanism--11950079</link><description><![CDATA[In enzymology, a purine-nucleoside phosphorylase (EC 2.4.2.1) is an enzyme that catalyzes the chemical reaction: purine nucleoside + phosphate ↔ purine + alpha-D-ribose 1-phosphate. Thus, the two substrates of this enzyme are purine nucleoside and phosphate, whereas its two products are purine and alpha-D-ribose 1-phosphate. This enzyme belongs to the family of glycosyltransferases, specifically the pentosyltransferases.<br /><a href="http://www.creative-enzymes.com/product/native-microorganism-purinenucleoside-phosphorylase_812.html" rel="noopener">http://www.creative-enzymes.com/product/native-microorganism-purinenucleoside-phosphorylase_812.html</a>]]></description><guid isPermaLink="false">https://api.spreaker.com/episode/11950079</guid><pubDate>Thu, 25 May 2017 08:27:08 +0000</pubDate><enclosure url="https://api.spreaker.com/download/episode/11950079/purine_nucleoside_phosphorylase_physiology_biochemistry_and_mechanism.mp3" length="0" type="audio/mpeg"/><itunes:author>Jack Forst</itunes:author><itunes:subtitle>In enzymology, a purine-nucleoside phosphorylase (EC 2.4.2.1) is an enzyme that catalyzes the chemical reaction: purine nucleoside + phosphate ↔ purine + alpha-D-ribose 1-phosphate. Thus, the two substrates of this enzyme are purine nucleoside and...</itunes:subtitle><itunes:summary><![CDATA[In enzymology, a purine-nucleoside phosphorylase (EC 2.4.2.1) is an enzyme that catalyzes the chemical reaction: purine nucleoside + phosphate ↔ purine + alpha-D-ribose 1-phosphate. Thus, the two substrates of this enzyme are purine nucleoside and phosphate, whereas its two products are purine and alpha-D-ribose 1-phosphate. This enzyme belongs to the family of glycosyltransferases, specifically the pentosyltransferases.<br /><a href="http://www.creative-enzymes.com/product/native-microorganism-purinenucleoside-phosphorylase_812.html" rel="noopener">http://www.creative-enzymes.com/product/native-microorganism-purinenucleoside-phosphorylase_812.html</a>]]></itunes:summary><itunes:duration>1118</itunes:duration><itunes:explicit>clean</itunes:explicit><itunes:image href="https://d3wo5wojvuv7l.cloudfront.net/images.spreaker.com/nuvolari-assets/green_square_mic.jpg"/><itunes:episodeType>full</itunes:episodeType></item><item><title>5 benefits of papain powder</title><link>https://www.spreaker.com/episode/5-benefits-of-papain-powder--11628952</link><description><![CDATA[More about papain powder: <a href="http://www.creative-enzymes.com/product/native-papaya-latex-papain_963.html" rel="noopener">http://www.creative-enzymes.com/product/native-papaya-latex-papain_963.html</a>]]></description><guid isPermaLink="false">https://api.spreaker.com/episode/11628952</guid><pubDate>Fri, 14 Apr 2017 03:38:49 +0000</pubDate><enclosure url="https://api.spreaker.com/download/episode/11628952/5_benefits_of_papain_powder.mp3" length="0" type="audio/mpeg"/><itunes:author>Jack Forst</itunes:author><itunes:subtitle>More about papain powder: http://www.creative-enzymes.com/product/native-papaya-latex-papain_963.html</itunes:subtitle><itunes:summary><![CDATA[More about papain powder: <a href="http://www.creative-enzymes.com/product/native-papaya-latex-papain_963.html" rel="noopener">http://www.creative-enzymes.com/product/native-papaya-latex-papain_963.html</a>]]></itunes:summary><itunes:duration>40</itunes:duration><itunes:explicit>clean</itunes:explicit><itunes:image href="https://d3wo5wojvuv7l.cloudfront.net/images.spreaker.com/nuvolari-assets/green_square_mic.jpg"/><itunes:episodeType>full</itunes:episodeType></item><item><title>AP Biology Lab 2- Enzyme Catalysis</title><link>https://www.spreaker.com/episode/ap-biology-lab-2-enzyme-catalysis--11628948</link><description><![CDATA[Catalase<br /><a href="http://www.creative-enzymes.com/product/Catalase_727.html" rel="noopener">http://www.creative-enzymes.com/product/Catalase_727.html</a>]]></description><guid isPermaLink="false">https://api.spreaker.com/episode/11628948</guid><pubDate>Fri, 14 Apr 2017 03:37:47 +0000</pubDate><enclosure url="https://api.spreaker.com/download/episode/11628948/ap_biology_lab_2_enzyme_catalysis.mp3" length="0" type="audio/mpeg"/><itunes:author>Jack Forst</itunes:author><itunes:subtitle>Catalase
http://www.creative-enzymes.com/product/Catalase_727.html</itunes:subtitle><itunes:summary><![CDATA[Catalase<br /><a href="http://www.creative-enzymes.com/product/Catalase_727.html" rel="noopener">http://www.creative-enzymes.com/product/Catalase_727.html</a>]]></itunes:summary><itunes:duration>406</itunes:duration><itunes:explicit>clean</itunes:explicit><itunes:image href="https://d3wo5wojvuv7l.cloudfront.net/images.spreaker.com/nuvolari-assets/green_square_mic.jpg"/><itunes:episodeType>full</itunes:episodeType></item></channel></rss>
