Open AccessProcessing of extracellular lipase of Lactobacillus plantarum : involvement of a metalloprotease
Author(s) -
Fátima Silva Lopes Maria,
Leitão Ana Lúcia,
Figueiredo Marques J.J.,
Teixeira Carrondo Manuel José,
Barreto Crespo Maria Teresa
Publication year - 1999
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1999.tb13701.x
Subject(s) - pepstatin , proteases , lipase , biochemistry , extracellular , metalloproteinase , lactobacillus plantarum , protease , biology , chemistry , microbiology and biotechnology , enzyme , lactic acid , bacteria , genetics
The hypothesis of a proteolytic involvement in the extracellular lipase processing of a strain of Lactobacillus plantarum was considered and tested. in vitro assays with acid proteases, cathepsin D and renin revealed that both did affect lipolytic activity positively. In vivo assays with growth in the presence of the protease inhibitors pepstatin, phenylmethylsulfonyl fluoride, trans ‐epoxysuccinyl‐ l ‐leucylamido‐(4‐guanidino)butane and ethylenediaminetetraacetic acid showed that ethylenediaminetetraacetic acid did affect the pattern of the proteins that possess lipolytic activity. Therefore, it is suggested that a metalloprotease is involved in the processing of the extracellular lipases of L. plantarum , although other proteases can also be important.