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Purification and Characterization of a Dipeptidase from Lactobacillus casei ssp. casei IFPL 731 Isolated from Goat Cheese Made from Raw Milk

AutorFernandez-Espla, M. D; Martín-Hernández, M. C.
Fecha de publicación1997
EditorAmerican Dairy Science Association
CitaciónJournal of Dairy Science 80: 1497- 1504 (1997)
ResumenA dipeptidase was purified to homogeneity from the cell-free extract of Lactobacillus casei ssp. casei IFPL 731 by a combination of heat treatment, hydrophobic interaction chromatography, anion-exchange chromatography, and gel filtration. A purification factor of 395-fold was obtained, and yield was 20%. The dipeptidase was shown to be a metal-dependent enzyme; optimal activity was at pH 7.5 and 60 to 75°C, and the enzyme had a high degree of thermal stability. Molecular mass was estimated by SDS-PAGE and gel filtration to be 46 kDa, which suggested that the enzyme existed as a monomer. Enzyme activity was most effectively inhibited by metal-chelating agents, reducing agents, or sulfhydryl group reagents. After inhibition with phenanthroline, activity was partially restored by Co2+ and Mn2+. The kinetics of Phe-Ala and Leu-Leu did not follow Michaelis-Menten saturation kinetics but exhibited a mixture of positive and negative cooperativity for the successive binding of molecules of the same substrate.
Identificadoresdoi: 10.3168/jds.S0022-0302(97)76078-8
issn: 0022-0302
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