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Heat‐Stability of Milk‐Clotting Enzymes in Conditions Encountered in Swiss Cheese Making
Author(s) -
GARNOT PASCALINE,
MOLLE DANIEL
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.tb13975.x
Subject(s) - chymosin , chemistry , protease , pepsin , proteases , heat stability , food science , mucor , enzyme , biochemistry , chromatography , materials science , penicillium , composite material
Chymosin is inactivated in gelled milk at pH 6.50 at 53°C according to a biphasic kinetic. Both phases appear to follow first‐order kinetics. The D‐value for the first phase is 30 min. In the same medium, the Mucor miehei and Mucor pusillus proteases are much more stable (D 53°C > 100 min) while bovine pepsin, a heat‐labile Mucor miehei protease and the Endothia parasitica protease are rapidly inactivated (D 53°C < 10 min). pH appears to be the most important parameter for heat stability. Protein and calcium concentrations affect the resistance to heat treatment. A residual activity of chymosin in Swiss‐type curd will be very weak at the most unless the curd is cooked at pH < 6.50.