Studies on the properties of cow's-milk tributyrinases and their interaction with milk proteins

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Abstract
1. The tributyrinases in milk are mainly associated with casein micelles. Dilution or addition of sodium chloride increases the enzyme activity, probably by dissociating the micelle-tributyrinase complexes. 2. Tributyrinase activities of milks activated by dilution and sodium chloride addition were in the range 0.2-1.7muequiv. of acid liberated/ml. of milk/min. from tributyrin emulsion at pH8.5 and 25 degrees . The enzymes have a bivalent-cation requirement for full activity and are rather unstable when separated from casein. 3. Ultracentrifugation of skim milks containing sodium chloride (0.75m) gave preparations low in casein but containing about 70% of the milk tributyrinases. The tributyrinases in such preparations appear to be bound in complexes of molecular weight about 350000. Dilution may result in dissociation to give the free enzymes. 4. Pancreatic lipase also formed complexes with casein micelles, but wheat-germ esterase, xanthine oxidase, milk alkaline phosphatase and other enzymes did not.

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