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Partial purification and characterization of an X-prolyl dipeptidyl aminopeptidase from Lactobacillus sanfranciscensis CB1

2005-07-01

Abstract excerpt

An X-prolyl dipeptidyl aminopeptidase (PepX) from Lactobacillus sanfranciscensis CB1, a key sourdough lactic acid bacterium, was partially purified by five chromatographic steps. As estimated by sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE) and gel filtration, the enzyme appeared to be a 49.2-56 kDa monomer. Optimal activity occurred at pH 6.0 and 30 degrees C, with K(m) of 0.6 mM and V(max...

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Literature Corpus work
1194c5c5-df5a-553c-abf8-c04ffafcd7ca
DOI
10.1016/j.foodchem.2004.08.047
Open publication

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