Purification and Characterization of d -Aminoacylase from Alcaligenes faecalis DA1-Reference-Cited by-同舟云学术

Purification and Characterization of d -Aminoacylase from Alcaligenes faecalis DA1

Published:1991-04 Issue:4 Volume:57 Page:1259-1260
ISSN:0099-2240
Container-title:Applied and Environmental Microbiology
language:en
Short-container-title:Appl Environ Microbiol

Author:

Yang Yunn-Bor¹,Lin Chyuan-Sheng¹,Tseng Ching-Ping¹,Wang Yng-Jiin¹,Tsai Ying-Chieh¹

Affiliation:

1. Institute of Biochemistry, National Yang-Ming Medical College, Taipei 11221, Taiwan, Republic of China

Abstract

A d -aminoacylase from Alcaligenes faecalis DA1 has been purified to homogeneity by a simple purification procedure with two columns, Fractogel DEAE-650 and HW-50. The specific activity of the purified enzyme was found to be 580 U/mg of protein with N -acetyl- dl -methionine as the reaction substrate. The apparent molecular weight and isoelectric point of this enzyme were determined to be 55,000 and 5.4, respectively.

Publisher

American Society for Microbiology

Subject

Ecology,Applied Microbiology and Biotechnology,Food Science,Biotechnology

Link

https://journals.asm.org/doi/pdf/10.1128/aem.57.4.1259-1260.1991

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