Partial purification and characterization of phospholipase C from Yersinia enterocolitica

J Appl Bacteriol. 1989 Apr;66(4):303-9. doi: 10.1111/j.1365-2672.1989.tb02483.x.

Abstract

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 degrees C and 37 degrees C; production was optimum at 37 degrees C in the stationary phase (14-16 h). A decrease in phospholipase C activity at various storage temperatures (-5 degrees C, 4 degrees C, 37 degrees C) was also observed, although the enzyme was active over a wide range of temperature (5-65 degrees C) and pH (3.5-7.5). The phospholipase C was partially purified by ammonium sulphate precipitation and Sephadex column chromatography, and characterized.

MeSH terms

  • Animals
  • Bacterial Typing Techniques
  • Buffaloes
  • Electrophoresis, Polyacrylamide Gel
  • Food Microbiology
  • Milk / microbiology*
  • Type C Phospholipases / analysis
  • Type C Phospholipases / isolation & purification*
  • Yersinia enterocolitica / enzymology*

Substances

  • Type C Phospholipases