5 Results Found

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 Inhibitor Cocktail Kit

Protease Inhibitor Cocktail Kit


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.

  • 1