Purification and Properties ofd-Aminoacylase ofStreptomyces olivaceus
- 1 January 1978
- journal article
- research article
- Published by Oxford University Press (OUP) in Agricultural and Biological Chemistry
- Vol. 42 (1) , 107-113
- https://doi.org/10.1080/00021369.1978.10862932
Abstract
D-Aminoacylase for enzymatic resolution of dl-amino acids was produced in the presence of inducer by Streptomyces olivaceus and almost all the activity was found in cell fraction. The partial purification and properties of this induced enzyme were studied. The enzyme had a molecular weight of about 45,000 and was specific for the hydrolysis of N-acetyl d-amino acids. The optimum pH was found to be at pH 7.0 and the activity was remarkably inhibited by the presence of Hg2+ or Ag2+. Enzyme stability was increased by the addition of Co2+. Michaelis constants (Km) for several preferred substrates were between 1.13 × 10−3 and 2.95 × 10−3 m.This publication has 4 references indexed in Scilit:
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