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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Bibliographic Details
Main Authors: Khalid, Noraini M., Marth, Elmer H.
Format: Artigo
Language:Inglês
Published: 1990
Subjects:
Enzymology and Protein Engineering
Online Access:https://ncbi.nlm.nih.gov/pmc/articles/PMC183349/
https://ncbi.nlm.nih.gov/pubmed/16348113
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