Characterization of a highly thermostable extracellular lipase from Lactobacillus plantarum

Int J Food Microbiol. 2002 Jun 5;76(1-2):107-15. doi: 10.1016/s0168-1605(02)00013-2.

Abstract

After screening for the presence of lipase activity in lactobacilli isolated from "chouriço", a traditional Portuguese dry fermented sausage, a strain of Lactobacillus plantarum (DSMZ 12028) was chosen for extracellular lipase characterisation and purification. Proteinase K did not significantly affect lipolytic activity, as opposed to trypsin, which completely eliminated this activity. Among NaCl, Ca2+, EDTA, BSA, glycerol, Mn2+ and Mg2+, only Mn2+ and Mg2+ stimulated the lipase. Purification by gel filtration chromatography and gel electrophoresis revealed four bands, between 98 and 45 kDa, all with lipolytic activity against olive oil.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Chromatography, Gel
  • Electrophoresis, Agar Gel
  • Endopeptidase K
  • Fermentation
  • Food Microbiology
  • Lactobacillus / enzymology*
  • Lipase / isolation & purification
  • Lipase / metabolism*
  • Meat Products / microbiology*
  • Swine
  • Temperature
  • Trypsin

Substances

  • Lipase
  • Trypsin
  • Endopeptidase K