A milk clotting enzyme with low proteolytic activity was extracted with ammonium sulfate, at 0.40‐0.65 saturation, from sodom apple leaves. The enzyme with apparently a basic isoelectric point was activated by cysteine and was more active at 65°C than at 35°C. Milk clotting activity increased with pH at 65°C, with the enzyme being almost twice as active at pH 6.4 as at pH 5.4‐5.7. Storage at 4°C for 15 days resulted in a 30‐50% loss in enzyme activity.
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Aworh et al. (1986) studied this question.
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