Characterization of the Pro-aminopeptidase from Aeromonas caviae T-64

Zhen-Zhong ZHANG; Satoru NIRASAWA; Yoshiaki NAKAJIMA; Michiteru YOSHIDA; Isao KUSAKABE; Kiyoshi HAYASHI

doi:10.1271/bbb.65.420

Bioscience, Biotechnology, and Biochemistry

Online ISSN : 1347-6947
Print ISSN : 0916-8451

Biochemistry & Molecular Biology

Characterization of the Pro-aminopeptidase from Aeromonas caviae T-64

Zhen-Zhong ZHANG, Satoru NIRASAWA, Yoshiaki NAKAJIMA, Michiteru YOSHIDA, Isao KUSAKABE, Kiyoshi HAYASHI

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Keywords: Aeromonas caviae, aminopeptidase, enzyme stability, pro-enzyme, substrate specificity

JOURNAL FREE ACCESS

2001 Volume 65 Issue 2 Pages 420-423

DOI https://doi.org/10.1271/bbb.65.420

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Abstract

The pro-aminopeptidase from Aeromonas caviae T-64 (pro-apAC) had maximal activity at 60°C and was more stable than mature apAC at temperature up to 65°C for 1 hour. The pH stability of pro-apAC ranged from 4.0 to 8.0, which is broader than the range for the mature apAC. The k_cat/K_m of pro-apAC was 1.4% to 24% of that of mature apAC.

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