Dino

Hydrolase

9 Results Found

Pectolyase Y-23 (A. Niger)

Highly purified enzyme from Aspergillus niger used for isolation of biologically active protoplasts from a wide spectrum of higher plants and tissues.

Pectolyase Y-23 (A.Japonicus)

Pectolyase Y-23 is a highly purified maceration enzyme from Aspergillus japonicus. It contains two types of pectinase such as endopolygalacturonase and endo-pectin lyase in high activity. Included is a maceration stimulating factor which stimulates tissue maceration by both pectinases. Pectolyase Y-23 is a highly purified maceration enzyme from Aspergillus japonicus. It contains two types of pectinase such as endopolygalacturonase and endo-pectin lyase in high activity. Included is a maceration stimulating factor which stimulates tissue maceration by both pectinases. Unit Definition: One unit is defined as an increase in A235 by 1.0 in the reaction mixture per minute.

Hyaluronidase (From Streptomyces Hyalurolyticus)

Synonyms: Hyaluronate lyase; Hyaluronidase; Mucinase. The hyaluronidase is purified from Streptomyces hyalurolyticus. This enzyme belongs to the endo-beta-hexosaminidase and endo-eliminase type enzyme that produces oligo-saccharide (unsaturated tetraose and pentose) by hydrolyzing the beta-1,4-linkage of hyaluronic acid. Hyaluronidase is stable in both high temperature and acid or alkaline range. It has high substrate specificity and hydrolyzes hyaluronic acid only in mucopolysaccharide. From Streptomyces hyalurolyticus
Lyophilized, salt-free
Activity: ∼2000 units/mg
Protease and lysozyme free
Each vial contains 100 U
Enzyme activity is determined by a change in optical density in a hyaluronic acid solution. It is compared to a hyaluronidase International Standard expressed as I.U.
See Enzymes and Substrates in the Immunobiologicals section for further details.

Proline Specific Endopeptidase (From Flavobacterium Meningosepticum)

Proline Specific Endopeptidase specifically cleaves peptide bonds on the carboxy side of proline residues. Much slower hydrolysis is observed on the carboxy side of alanine residues. This enzyme is very close, in its properties, to a post-proline cleaving enzyme. The substrates have been found to have the general structure Y-Pro-X, where Y is a peptide or N-protected amino acid and X may be an amino acid, peptide, amide or ester.

Protease (S. Aureus) V.8

Protease V.8 specifically cleaves peptide bonds on the COOH terminal side of either aspartic or glutamic acids. In the presence of ammonium, the specificity is limited to glutamic sites.

Protease Inhibitor Cocktail Kit

Protease Inhibitor Cocktail Kit

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Cellulase Y-C (From Trichoderma Viride)

Cellulase Y-C enzyme retains very high filter paper decomposing activity and showed an appreciable amount of hemicellulase. Actually, this enzyme removed cell walls from plant tissues in shorter incubation period without loss of biological activity of the materials.

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