Enzymatic Resolution of Racemic Amino Acids

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  • MICHI Kimiyo
    Laboratory of Food and Nutrition of Japan Women's University
  • NONAKA Harumi
    Laboratory of Food and Nutrition of Japan Women's University

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Other Title
  • DL-アミノ酸の酵素による光学的分割
  • Part 2. Resolution of DL-Glutamic Acid and DL-Valine
  • (第2報) DL-Glutamic acid及びDL-Valineの光学的分割

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Description

The acetyl-DL-glutamic acid and the chloroacetyl-DL-valine were prepared and asymmetrically hydrolyzed by the acylase obtained from several strains of mold which were known to pro-duce sufficient activity in the preceding study, and by the enzyme prepared from the Taka-dias-tase.<br> The effect of pH on the enzyme activity and the hydrolytic rates of acetyl-DL-glutanmic acid with the enzyme of A. tamarii, A. oryzae, A. flavus, P. vinaceous, P. oxalicum var. pectinoporum nov. and P. viridicatum were measured.<br> A. tamarii and P. vinaceous produced the greatest yields of the acylase.<br> An, active acylase was prepared by fractionation of water extract of culture medium with (NH4)2SO4 and acetone.<br> The active enzyme of 0.11_??_0.2g of solid matter were sufficient to hydrolyze 10g of acetyl-DL-glutamic acid.<br> The research was partly studied by one of the authors (K. MICHI) under Dr. WILLIUM C. ROSE of the University of Illinois U.S. A. during the session 1951_??_1952 under a grant from the American Association of University Women.<br> The author wishes to thank Dr. ROSE for his kind suggestions and fbr his generousity in making the facilities of his laboratory available.

Journal

  • Nippon Nōgeikagaku Kaishi

    Nippon Nōgeikagaku Kaishi 28 (5), 346-349, 1954

    Japan Society for Bioscience, Biotechnology, and Agrochemistry

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