Purification and Characterization of an l -Aminopeptidase from Pseudomonas putida ATCC 12633-Reference-Cited by-同舟云学术

Purification and Characterization of an l -Aminopeptidase from Pseudomonas putida ATCC 12633

Published:1993-12 Issue:12 Volume:59 Page:4330-4334
ISSN:0099-2240
Container-title:Applied and Environmental Microbiology
language:en
Short-container-title:Appl Environ Microbiol

Author:

Hermes H. F. M.¹,Sonke T.¹,Peters P. J. H.¹,van Balken J. A. M.¹,Kamphuis J.¹,Dijkhuizen L.¹,Meijer E. M.¹

Affiliation:

1. DSM Research, Bio-organic Chemistry section, P.O. Box 18, 6160 MD Geleen, and Department of Microbiology, University of Groningen, Kerklaan 30, 9571 NN Haren, 2 The Netherlands

Abstract

An l -aminopeptidase of Pseudomonas putida , used in an industrial process for the hydrolysis of d,l -amino acid amide racemates, was purified to homogeneity. The highly l -enantioselective enzyme resembled thiol reagent-sensitive alkaline serine proteinases and was strongly activated by divalent cations. It possessed a high substrate specificity for dipeptides and α-H amino acid amides, e.g., l -phenylglycine amide.

Publisher

American Society for Microbiology

Subject

Ecology,Applied Microbiology and Biotechnology,Food Science,Biotechnology

Link

https://journals.asm.org/doi/pdf/10.1128/aem.59.12.4330-4334.1993

Reference16 articles.

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