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Partial purification and characterization of phospholipase C from Yersinia enterocolitica
Author(s) -
TOORA S.,
SINGH GAGANDEEP,
DHAR S.,
SINGH A.D.,
TIWARI R.P.,
SINGH G.
Publication year - 1989
Publication title -
journal of applied bacteriology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.889
H-Index - 156
eISSN - 1365-2672
pISSN - 0021-8847
DOI - 10.1111/j.1365-2672.1989.tb02483.x
Subject(s) - lecithinase , yersinia enterocolitica , sephadex , chromatography , phospholipase c , chemistry , ammonium sulfate precipitation , enzyme , phospholipase , column chromatography , ammonium , size exclusion chromatography , biochemistry , biology , bacteria , organic chemistry , genetics
About 34% of the strains of Yersinia enterocolitica isolated from raw milk were found to produce lecithinase. A selected strain produced phospholipase C at 22°C and 37°C; production was optimum at 37°C in the stationary phase (14–16 h). A decrease in phospholipase C activity at various storage temperatures (—5°C, 4°C, 37°C) was also observed, although the enzyme was active over a wide range of temperature (5–65°C) and pH (3mD5–7mD5). The phospholipase C was partially purified by ammonium sulphate precipitation and Sephadex column chromatography, and characterized.