Abstract
SummaryThe milk-clotting and proteolytic activities of rennet, bovine pepsin and porcine pepsin were compared. The milk-clotting activity of porcine pepsin was extremely pH-dependent around pH 6·6 and coagulation did not occur above pH 6·68. The clotting activity of bovine pepsin was slightly more dependent on pH than that of rennet but no rapid drop-off in activity occurred as with porcine pepsin. Temperature influenced the clotting activity of rennet and bovine pepsin similarly but the behaviour of porcine pepsin was markedly different.For equal milk-clotting activity, the proteolytic activities of rennet and bovine pepsin were approximately equal and substantially lower than that of porcine pepsin. Electrophoretic examination showed that the proteolysis products of rennet and bovine pepsin were similar and quite different from those produced by porcine pepsin.The suitability of bovine pepsin as a rennet substitute is discussed.
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