ISOLATION AND PROPERTIES OF PROTEASE FROM SACCHAROMYCES CARLSBERGENSIS |
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| Authors: | FRONDA C WOODS JOHN E KINSELLA |
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| Affiliation: | Institute of Food Science Cornell University Ithaca, NY 14853 |
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| Abstract: | ABSTRACT Proteases from autolyzed Saccharomyces carlsbergensis were partially purified by ammonium sulfate precipitation and hydroxyapatite column chromatography. pH optima at pH 3.0 and 6.8 were observed. A 7.4-fold purification was achieved for the protease with neutral pH optimum. The general properties of this enzyme were studied. It displayed optimum activity and stability at 37°C and pH 6. It was inhibited by Fe+2and Fe+3, N-ethylmaleimide (NEM), phenylmethanesulfonyl fluoride (PMSF), and sodium chloride (NaCl). It was activated by β-mercaptoethanol and urea. |
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