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. 1975 Mar 28;384(1):235-41.
doi: 10.1016/0005-2744(75)90112-6.

Isolation of an extracellular neutral proteinase from Pseudomonas fragi

M A Porzio, A M Pearson

Isolation of an extracellular neutral proteinase from Pseudomonas fragi

M A Porzio et al. Biochim Biophys Acta. .

Abstract

A single proteolytic enzyme (EC 3.4.4.-) was isolated from culture supernatants of Pseudomonas fragi with 20% yielded and 60-fold purification by means of stepwise DEAE-Sephadex batch adsorption, ammonium sulfate precipitation, gel filtration and DEAE-cellulose chromatography. The enzyme was Zn-2+ activated and Ca-2+ stabilized, had optimum activity at pH 6.5--8.0 and 40 degrees C. The molecular weight range was 40 000--50 000 as determined by dodecylsulfate gel electrophoresis, gel filtration and Zn assay. This proteinase has properties similar to other extracellular bacterial neutral proteinases.

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