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A Comparison of Dogfish and Bovine Chymotrypsins in Relation to Protein Hydrolysis
Author(s) -
RAMAKRISHNA MALLUR,
HULTIN HERBERT O.,
ATALLAH MOKHTAR T.
Publication year - 1987
Publication title -
journal of food science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.772
H-Index - 150
eISSN - 1750-3841
pISSN - 0022-1147
DOI - 10.1111/j.1365-2621.1987.tb14043.x
Subject(s) - enzyme , chymotrypsin , chemistry , hydrolysis , protease , peptide bond , biochemistry , chromatography , trypsin
An extracellular protease, chymotrypsin, from a low temperature‐adapted poikilotherm (dogfish) was compared with the bovine enzyme against several protein substrates to determine potential advantages in the use of an enzyme adapted to functioning in a low temperature environment. In general, the dogfish enzyme showed a higher rate of reaction and hydrolyzed more peptide bonds than did the bovine enzyme whether the substrates were soluble or insoluble proteins. Dogfish chymotrypsin was slow to produce clotting of milk, but once formed the clot had good stability. The bovine enzyme was more efficient in incorporating methionine into soy protein in a piasteintype reaction.