Characterization of a highly thermostable extracellular lipase from Lactobacillus plantarum
2002
Lopes, M. de F.S. | Leitao, A.L. | Regalla, M. | Marques, J.J.F. | Carrondo, M.J.T. | Crespo, M.T.B.
After screening for the presence of lipase activity in lactobacilli isolated from "chourico", 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, Ca(2+), EDTA, BSA, glycerol, Mn(2+) and Mg(2+), only Mn(2+) and Mg(2+) 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.
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