ISSN:
0006-3592
Schlagwort(e):
whey proteins
;
proteases
;
enzymatic hydrolysis
;
peptides
;
Chemistry
;
Biochemistry and Biotechnology
Quelle:
Wiley InterScience Backfile Collection 1832-2000
Thema:
Biologie
,
Werkstoffwissenschaften, Fertigungsverfahren, Fertigung
Notizen:
We have studied the enzymatic hydrolysis of whey proteins at pH 8 and50°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. © 1994 John Wiley & Sons, Inc.
Zusätzliches Material:
9 Ill.
Materialart:
Digitale Medien
URL:
http://dx.doi.org/10.1002/bit.260440415
