Chemical and Physico-chemical Properties of Bacterial Proteinase*

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Abstract
The physico-chemical and chemical properties of purified bacterial proteinase were reported. The enzyme has a pH optimum for activity at 7-8.5, hydrolyzes casein optimally at 50[degree]-70[degree]C, and is most stable at pH 6.5-10 and at temperatures below 35[degree]C. The electrophoretic mobility at pH 3.00 indicated the acidic nature of the enzyme protein and suggested the presence of a large number of free acidic groups in the enzyme molecule. The enzyme has a sedimentation constant of 1.58 S from which its molecular weight was calulated to be 27,000*2,500. The amino-acid composition of the enzyme protein showed that it contained no cystine residues. The enzyme was not inactivated by the addition of thiol reagents, indicating that it is a non-sulfhydryl enzyme.

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