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ISOLATION AND PROPERTIES OF PROTEASE FROM SACCHAROMYCES CARLSBERGENSIS
Author(s) -
WOODS FRONDA C.,
KINSELLA JOHN E.
Publication year - 1980
Publication title -
journal of food biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.507
H-Index - 47
eISSN - 1745-4514
pISSN - 0145-8884
DOI - 10.1111/j.1745-4514.1980.tb00647.x
Subject(s) - pmsf , chemistry , chromatography , protease , proteases , ammonium sulfate , ammonium sulfate precipitation , ammonium , phenylmethylsulfonyl fluoride , saccharomyces , urea , ammonium chloride , sodium , enzyme , saccharomyces cerevisiae , biochemistry , yeast , size exclusion chromatography , organic chemistry
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 +2 and Fe +3 , N‐ethylmaleimide (NEM), phenylmethanesulfonyl fluoride (PMSF), and sodium chloride (NaCl). It was activated by β‐mercaptoethanol and urea.