Author:
Manning Gilbert B.,Campbell Jr. L. Leon
Abstract
The purification and certain properties of L-asparagine deamidase of Bacillus coagulans and Bacillus stearothermophilus are described. Maximum enzyme activity was obtained at 55 °C. over a pH range of 7.5 to 8.5. The purified deamidase hyclrolyzed the L-isomer of asparagine quantitatively to aspartic acid and ammonia and did not attack the D-isomer. D-Asparagine inhibited the hydrolysis of the L-isomer. The Kmfor the inhibition reaction was found to be 1.87 × 10−2 M. The enzyme did not catalyze transamidation or hydroxylamine transfer reactions. Enzyme activity was inhibited by N-ethylmaleimide and p-chloromercuribenzoate. The inhibition by these agents was reversed by glutathione. In the absence of substrate the deamidase of both organisms was relatively heat labile at 55 °C. The heat lability of this enzyme is discussed in relation to the heat stability of other enzyme systems of thermophilic microorganisms.
Publisher
Canadian Science Publishing
Subject
Genetics,Molecular Biology,Applied Microbiology and Biotechnology,General Medicine,Immunology,Microbiology
Cited by
26 articles.
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