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Native Rhodopseudomonas sphaeroides ?-Hydroxybutyrate Dehydrogenase LAB GRADE 97%

In mammalian systems, β-hydroxybutyrate dehydrogenase is localized on the inner mitochondrial membrane and requires phosphatidyl choline for activity. In contrast, the enzyme from Pseudomonas is a soluble cytosolic enzyme that does not require a phospholipid allosteric activator. The enzyme is required for the utilization of ketone bodies as a source of metabolic energy. It catalyzes the oxidation of 3-hydroxybutyrate to acetoacetate, the first step in the conversion of ketone bodies to citric acid, which is then further metabolized via the tricarboxylic acid cycle (Krebs cycle).http://www.creative-enzymes.com/product/Native-Rhodopseudomonas-Sphaeroides-Hydroxybutyrate-Dehydrogenase_1073.html

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Native Rice ?-Glucosidase LAB GRADE 97%

Alpha-glucosidase is a glucosidase located in the brush border of the small intestine that acts upon 1,4-alpha bonds. This is in contrast to beta-glucosidase. Alpha-glucosidase breaks down starch and disaccharides to glucose. Maltase, a similar enzyme that cleaves maltose, is nearly functionally equivalent.http://www.creative-enzymes.com/product/Native-Rice-Glucosidase_1495.html

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Native Saccharomyces cerevisiae Adenosine-5'-triphosphate Sulfurylase LAB GRADE 97%

In enzymology, a sulfate adenylyltransferase (EC 2.7.7.4) is an enzyme that catalyzes the chemical reaction:ATP + sulfate↔ diphosphate + adenylyl sulfate. Thus, the two substRates of this enzyme are ATP and sulfate, whereas its two products are diphosphate and adenylyl sulfate. This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing nucleotide groups (nucleotidyltransferases). This enzyme participates in 3 metabolic pathways:purine metabolism, selenoamino acid metabolism, and sulfur metabolism.http://www.creative-enzymes.com/product/Native-Saccharomyces-Cerevisiae-Adenosine5triphosphate-Sulfurylase_1044.html

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Native Saccharomyces cerevisiae Alcohol Dehydrogenase LAB GRADE 97%

Alcohol dehydrogenases (ADH) are a group of dehydrogenase enzymes that occur in many organisms and facilitate the interconversion between alcohols and aldehydes or ketones with the reduction of nicotinamide adenine dinucleotide (NAD+ to NADH). In Humans and many other animals, they serve to break down alcohols that otherwise are toxic, and they also participate in geneRation of useful aldehyde, ketone, or alcohol groups during biosynthesis of various metabolites. In yeast, plants, and many bacteria, some alcohol dehydrogenases catalyze the opposite reaction as part of fermentation to ensure a constant supply of NAD+.http://www.creative-enzymes.com/product/Native-Saccharomyces-Cerevisiae-Alcohol-Dehydrogenase_1048.html

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Native Schizophyllum commune Cholesterol Esterase LAB GRADE 97%

Sterol esterase belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. The systematic name of this enzyme class is steryl-ester acylhydrolase. This enzyme participates in bile acid biosynthesis.http://www.creative-enzymes.com/product/Native-Schizophyllum-Commune-Cholesterol-Esterase_729.html

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Native Sheep 6-Phosphogluconic Dehydrogenase LAB GRADE 96%

In enzymology, a phosphogluconate dehydrogenase (decarboxylating) (EC 1.1.1.44) is an enzyme that catalyzes the chemical reaction:6-phospho-D-gluconate + NADP+↔ D-ribulose 5-phosphate + CO2 + NADPH. Thus, the two substRates of this enzyme are 6-phospho-D-gluconate and NADP+, whereas its 3 products are D-ribulose 5-phosphate, CO2, and NADPH. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor.http://www.creative-enzymes.com/product/Native-Sheep-6Phosphogluconic-Dehydrogenase_1016.html

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Native Spinach Aldolase LAB GRADE 97%

Fructose-bisphosphate aldolase (EC 4.1.2.13), often just aldolase, is an enzyme catalyzing a reversible reaction that splits the aldol, fructose 1,6-bisphosphate, into the triose phosphates dihydroxyacetone phosphate (DHAP) and glyceraldehyde 3-phosphate (G3P). Aldolase can also produce DHAP from other (3S,4R)-ketose 1-phosphates such as fructose 1-phosphate and sedoheptulose 1,7-bisphosphate. Gluconeogenesis and the Calvin cycle, which are anabolic pathways, use the reverse reaction. Glycolysis, a catabolic pathway, uses the forward reaction. Aldolase is divided into two classes by mechanism.http://www.creative-enzymes.com/product/Native-Spinach-Aldolase_1053.html

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Native Streptococcus hemolyticus Streptokinase LAB GRADE

Streptokinase (SK) is an enzyme secreted by several species of streptococci that can bind and activate human plasminogen. SK is used as an effective and inexpensive thrombolysis medication in some cases of myocardial infarction (heart attack) and pulmonary embolism. Streptokinase belongs to a group of medications known as fibrinolytics, and complexes of streptokinase with human plasminogen can hydrolytically activate other unbound plasminogen by activating through bond cleavage to produce plasmin.http://www.creative-enzymes.com/product/Native-Streptococcus-Hemolyticus-Streptokinase_855.html
 

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Native Streptomyces griseus Aminopeptidase I LAB GRADE 97%

Aminopeptidase I from S. griseus has a fairly broad specificity, being able to remove the N-terminal residue of most proteins, except where the penultimate residue is an imino acid. It contains two Zn2+ binding sites. Aminopeptidase I from S. griseus is inhibited by 1,10-phenanthroline and is activated six-fold by Ca2+, which also stabilizes it against heat inactivation. This monomeric zinc metalloprotein has an isoelectric point (pI) of 5.4.http://www.creative-enzymes.com/product/Native-Streptomyces-Griseus-Aminopeptidase-I_1057.html

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Native Streptomyces sp. Alkalophilic proteinase LAB GRADE

This enzyme is more active at a higher pH range than the known alkaline protease, showing the proteolytic activity even in 0.2N NaOH solution. This enzyme is useful for proteolysis of insoluble protein and for structure investigation of protein.http://www.creative-enzymes.com/product/Native-Streptomyces-Sp-Alkalophilic-Proteinase_779.html
 

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