Cornell Research Foundation Inc.

Todd W Gusek

John E Kinsella

David B Wilson

An exocellular protease from Thermomonospora fusca YX and a process for producing the protease which has the following physicochemical properties: (1) Molecular mass: The protease has a molecular mass of from about 10,000 to 14,000 Daltons as measured by SDS-polyacrylamide gel electrophoresis; (2) Influence of inhibitors: The protease activity is inhibited by serine protease inhibitors; (3) Substrate specificity: A non-specific protease which can hydrolyze food proteins and bovine serum albumin at a rate of 50-100 nmoles peptide bonds/.mu.g enzyme/minute at 55.degree., pH 8.5 in 0.5 M Tris buffer without showing any substrate and/or product inhibition; (4) Reactivity: A broad spectrum serine type protease having activity at least 5 times greater than trypsin or chymotrypsin towards food grade proteins and bovine serum albumin; (5) Optimum activity temperature and temperature range: The optimum activity temperature is 80.degree. C. at pH of 8.0 in 0.05 M Tris buffer at an ionic strength of 0.2 M NaCl; The temperature range is 35.degree. to 95.degree. C. under the same pH, buffer, and ionic strength; (6) pH range and optimum pH value: The protease has a pH activity range of from about 7 to 11, and the optimum pH value is 9.0; (7) Tolerance to ionic strength conditions and optimum ionic strength: The protease is tolerant to ionic strengths of from 0.0 to about 1.0 M NaCl; Optimum ionic strength is 0.2 M NaCl; (8) Isoelectric point: The isoelectric point is at an alkaline pH; and (9) Structure: The protease is a monomer.

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Todd W Gusek