Effect of heat-induced complexes of kappa -casein with beta -lactogloblin on progress of casein proteolysis by rennin, protease from Mucor pusillus Lindt and papain

Damicz, W.; Dziuba, J.; Smoragiewicz, W.; Zbikowska, A.

Zeszyty Naukowe Akademii Rolniczo Technicznej w Olsztynie (151, Technologia Zywnosci 8): 81-88

1976


Accession: 000351525

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Abstract
(i) Crystalline chymosin [see DSA 37, 7324], (ii) Mucor pusillus Lindt protease preparation (Meito Sangyo Co., Japan) or (iii) purified papain (Fluka AG, Buchs, St. Gallen, Switzerland) were added (in quantities required to coagulate skim-milk (pH 6.6) at 32 deg C in 30 min) to solutions containing 0.5, 1.0, 1.5, 2.0 or 2.5% casein prepared from basal solution of 4% casein + 1% whey proteins (pH 6.6 or 5.5) and either unheated or heat-treated at 72 deg or 85 deg C for 15 s. Incubation was at 32 deg C and the quantities of non-protein N liberated in 5 min were determined. The affinity and proteolytic activity of the enzyme preparations tested towards casein decreased in order (iii)>(ii)>(i). The nature and intensity of the effect of heat treatment of kinetics of casein hydrolysis depended on the extent of complexing between kappa -casein and beta -lactoglobulin and on the specificity and pH optimum of the enzymic action.