Purification and partial characterization of a prolyl-dipeptidyl aminopeptidase from Lactobacillus helveticus CNRZ 32

X-prolyl-dipeptidyl aminopeptidase, which hydrolyzed Gly-Pro-p-nitroanilide (relative activity [RA] = 100%) and Arg-Pro-p-nitroanilide (RA, 130%), was purified to homogeneity from the cell extract of Lactobacillus helveticus CNRZ 32. The enzyme also hydrolyzed Ala-Pro-Gly (RA, 11%) and Ala-Ala-p-nit...

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Veröffentlicht in:	Applied and Environmental Microbiology 1990-02, Vol.56 (2), p.381-388
Hauptverfasser:	Khalid, N.M. (University of Wisconsin, Madison, WI), Marth, E.H
Format:	Artikel
Sprache:	eng
Schlagworte:	ACTIVIDAD ENZIMATICA ACTIVITE ENZYMATIQUE Bacteriology Biological and medical sciences dipeptidyl dipeptidase IV Enzymology and Protein Engineering EPURATION FABRICACION DEL QUESO Fundamental and applied biological sciences. Psychology HIDROLASAS HYDROLASE LACTOBACILLUS Lactobacillus helveticus Metabolism. Enzymes Microbiology PURIFICACION TECHNOLOGIE FROMAGERE
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