title: Enzymatic hydrolysis of whey proteins: I. Kinetic models.
abstract: 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.
authors.affiliation: Departamento de Ingeniería Química, Facultad de Ciencias, Universidad de Granada, Granada 18071, Spain.
authors.forename: P
authors.initials: P
authors.lastname: Gonzàlez-Tello
authors.forename: F
authors.initials: F
authors.lastname: Camacho
authors.forename: E
authors.initials: E
authors.lastname: Jurado
authors.forename: M P
authors.initials: MP
authors.lastname: Páez
authors.forename: E M
authors.initials: EM
authors.lastname: Guadix