Abstract
The proteolytic activity of an industrial preparation of neutral protease from Bacillus subtilis has been tested on caseins and whey proteins of cow's milk. Electrophoretic analysis of κ-casein hydrolysate showed that only electropositive products can be found. Hydrolysis of β-casein generated compounds with low electrophoretic mobility as did hydrolysis of γ-casein. β-Lactoglobulin and immunoglobulins were heavily damaged, whereas α-lactalbumin was slightly hydrolyzed. Because of its wide spectrum of activity and interesting thermophilic properties, this enzymatic preparation can be applied to other fields in the food industry.
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