Degradation of Casein Components by Acid Protease of Bovine Milk

Abstract
Degradation of .alpha.s1-, .beta.- and .kappa.-caseins by an acid protease of bovine milk was studied by disc and urea-sodium dodecyl-sulfate electrophoresis. The acid protease converted .alpha.s1-casein into a fragment, with a mobility equal in disc and urea-sodium dodecylsulfate electrophoresis to that of .alpha.s1-I casein produced by the action of chymosin. New bands, with mobilities equal in disc and urea-sodium dodecylsulfate electrophoresis to those of .beta.-I and .beta.-II fractions produced by chymosin action, appeared by the action of acid protease on .beta.-casein. A para-.kappa.-casein-like protein was formed from .kappa.-casein by the acid protease. The para-.kappa.-casein-like protein was formed much slower by the acid protease than was para-.kappa.-casein by chymosin.

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