Purification and characterization of an extracellular proteinase from Brevibacterium linens

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Abstract
The alkaline proteinase of Brevibacterium linens was partially purified through ultrafiltration and chromatography on Sephacryl S-200. The molecular weight of this enzyme was determined by gel electrophoresis in polyacrylamide to be 52,000-55,000. The proteinase hydrolyses natural polypeptides such as casein, haemoglobin, bovine serum albumin, and ovalbumin. An apparent Km for casein was determined to be 1.3 mg .cntdot. mL-1. The original pH for caseinolytic activity was between 7.0 and 8.5 at the optimal temperature of 45.degree. C. The isolated enzyme is thermolabile: incubation at 50.degree. C destroyed proteolytic activity. Substrate proteins have a stabilizing effect. Our inhibition studies revealed that the B. linens proteinase belongs to the serine proteinase class.

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