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Purification and characterization of nitrile hydratase of a mutant strain of Brevibacterium sp.

✍ Scribed by J. L. Moreau; S. Azza; Prof. Dr. A. Arnaud; P. Galzy

Publisher
John Wiley and Sons
Year
1993
Tongue
English
Weight
429 KB
Volume
33
Category
Article
ISSN
0233-111X

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✦ Synopsis

Abstract

The nitrile hydratase from the mutant strain of Brevibacterium sp. ACV2 was purified and compared to that from the wild type R312. Its molecular weight was estimated at 80000. This enzyme is composed of 2 sub‐units with 26000 and 27500 molecular weights. The nitrile hydratase of the mutant strain is different from that of the wild type by its pHi, optimum activity pH, and its rates of hydrolysis of cyanovaleramide and cyanovaleric acid which were 30 and 15 folds greater.

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