THE ASPARAGINE DEAMIDASE OF BACILLUS COAGULANS AND BACILLUS STEAROTHERMOPHILUS
- 1 December 1957
- journal article
- research article
- Published by Canadian Science Publishing in Canadian Journal of Microbiology
- Vol. 3 (7), 1001-1009
- https://doi.org/10.1139/m57-111
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.Keywords
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