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Enzymatic hydrolysis of whey proteins: I. Kinetic models

1994; Wiley; Volume: 44; Issue: 4 Linguagem: Inglês

10.1002/bit.260440415

1097-0290

P. González‐Tello, F. Camacho, E. Jurado, M. P. Páez, Emilia M. Guadix,

Proteins in Food Systems

We have studied the enzymatic hydrolysis of whey proteins at pH 8 and50 degrees C with two proteases of bacterial origin, MKC Protease 660 L, and one of animal origin, PEM 2500 S. Our results show that a greater degree of hydrolysis is achieved under the same experimental conditions with the bacterial proteases than with the animal one. In our interpretation of the results we propose a mechanism in which the hydrolytic reaction is a zero-order one for the substrate, and the enzyme denaturalizes simultaneously via a second-order kinetic process due to free enzyme attacking enzyme bound to the substrate. Our results also indicate that there is an irreversible serine-protease inhibitor in whey proteins. (c) 1994 John Wiley & Sons, Inc.