Characterization of a highly thermostable extracellular lipase from Lactobacillus plantarum

Maria de Fátima Silva Lopes, Ana Lúcia Leitão, Manuela Regalla, J. J. Figueiredo Marques, Manuel José Teixeira Carrondo, Maria Teresa Barreto Crespo

Research output: Contribution to journalArticlepeer-review

44 Citations (Scopus)


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.

Original languageEnglish
Pages (from-to)107-15
Number of pages9
JournalInternational Journal of Food Microbiology
Issue number1-2
Publication statusPublished - 5 Jun 2002


  • Animals
  • Chromatography, Gel
  • Electrophoresis, Agar Gel
  • Endopeptidase K
  • Fermentation
  • Food Microbiology
  • Lactobacillus
  • Lipase
  • Meat Products
  • Swine
  • Temperature
  • Trypsin
  • Journal Article
  • Research Support, Non-U.S. Gov't


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