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Título

Purification and Characterization of a Novel Serine Aminopeptidase from Lactobacillus casei Ssp. casei IFPL 731

Autor Fernandez-Espla, M. D; Fox, P. F.; Martín-Hernández, M. C
Palabras clave Mesophilic lactic acid bacteria
Lactobacillus casei
Enzyme purification
Aminopeptidase
Fecha de publicación 1997
EditorAmerican Chemical Society
Citación Journal of Agricultural and Food Chemistry 45: 1624- 1628 (1997)
ResumenAn aminopeptidase showing broad specificity has been purified to homogeneity from the cell-free extract of Lactobacillus casei ssp. casei IFPL 731. Enzyme activity was inhibited by the serine protease inhibitor, phenylmethanesulfonyl fluoride, and reducing agents such as dithiothreitol and β-mercaptoethanol. The metal chelating agent, ethylenediamintetraacetic acid, also reduced enzyme activity. The molecular mass of the purified enzyme was estimated to be 67 kDa by gel filtration and sodium dodecyl sulfate-polyacrylamide gel electrophoresis, indicating that the enzyme exits as a monomer. The purified enzyme hydrolyzed p-nitroanilides of several amino acids and peptides as well as di- and tripeptides. The best substrates were Arg-Pro-p-nitroanilide, Ala-Pro-p-nitroanilide, Phe-Met, Leu-Gly, Phe-Ala, and Leu-Gly-Phe. Km values for Arg-Pro-p-nitroanilide and Leu-Gly were 4.8 and 1.1 mM, respectively. The properties of the enzyme are compared with those of other aminopeptidases isolated from lactic acid bacteria.
URI http://hdl.handle.net/10261/115608
DOI10.1021/jf960889w
Identificadoresdoi: 10.1021/jf960889w
issn: 0021-8561
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