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Effect of Heat‐Stable Proteases on the Kinetic Parameters of Milk Clotting by Chymosin
Author(s) -
JACKMAN D. M.,
PATEL T. R.,
HAARD N. F.
Publication year - 1985
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.1365-2621.1985.tb13754.x
Subject(s) - chymosin , proteases , protease , casein , chemistry , food science , clotting time , hydrolysis , raw milk , cheesemaking , enzyme , biochemistry , coagulation , psychology , psychiatry
The milk clotting per unit casein hydrolytic activities of proteases from 14 psychrotrophic pseudomonad isolates of raw milk ranged from 0.77 to 9.97 at 30°C. The milk clotting activities of chymodn and T16 protease were not completely additive, especially at high chymosin concentration when clotting time was relatively fast. The T16 protease was not effective in catalyzing the enzymic step of milk clbtting at O°C in the time expected on the basis of its milk clotting at 30°C. Milk incubated with the T25 motease for 8 days at 4°C and then clotted with chymosin at 30°C exhibited weak curd consistency.