Abstract
Activated enzyme extracts of adult bovine abomasum (adult bovine rennet) tissues contained 5 to 15% milk clotting activity attributable to pepsin. Starch gel electrophoresis in urea and mercaptoethanol revealed different patterns than for calf rennet extract. Differences also were in casein-agar gel diffusion patterns at pH 6.8. Lipolytic activities were similar. Proteolytic activity on casein substrate at pH 9.0 was evident in adult bovine but not in calf rennet or in swine pepsin. However, milk clotting activities in adult bovine and calf rennets were destroyed at comparable rates at pH 9.0. Proteolytic activity of adult bovine rennet was significantly reduced by milk clotting activation at pH 2.0. Casein-agar gel diffusion at pH 9.0 was useful in detecting blends of adult bovine and calf rennet. Adult bovine rennet could be detected at 1% concentration. Accelerated ripening and proteolytic activity studies of adult bovine and calf rennet at pH 5.2 indicated possible differences in their effects upon the aging properties of cheese.
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