EXTRACELLULAR PROTEINASE OF STREPTOCOCCUS LACTIS

Author:

Williamson W. T.1,Tove S. B.1,Speck M. L.1

Affiliation:

1. Departments of Food Science and Animal Science, North Carolina State of the University of North Carolina at Raleigh, North Carolina

Abstract

Williamson , W. T. (North Carolina State of the University of North Carolina, Raleigh), S. B. Tove, and M. L. Speck . Extracellular proteinase of Streptococcus lactis . J. Bacteriol. 87: 49–53. 1964.— Streptococcus lactis was shown to produce an extracellular proteolytic enzyme(s). A 120-fold purification of the proteinase was obtained from the cell-free culture medium by ammonium sulfate fractionation, calcium phosphate gel treatment, and chromatography on diethylaminoethyl cellulose. Only 32% of the activity was destroyed by heating at 98 C for 1 hr. The requirement of free sulfhydryl groups for enzyme activity was indicated by inhibition with p -chloromercuric benzoate. Diisopropyl fluorophosphate did not inhibit the proteinase.

Publisher

American Society for Microbiology

Subject

Molecular Biology,Microbiology

Reference13 articles.

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2. The intracellular proteinases of certain organisms from cheese and their relationship to the proteinases in cheese;BARIBO L. E.;J. Dairy Sci.,1952

3. On the mechanism of the decomposition of hydrogen peroxide by catalase;KEILIN D.;Proc. Roy. Soc. (London) Ser. B,1938

4. Protein measurement with the Folin phenol reagent;LOWRY H., N.;J. Biol. Chem.,1951

5. The distribution of certain amino acids in soluble fractions of milk cultures of Streptococcus lactis;MORGAN M. E.;J. Dairy Sci.,1951

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