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Nitrile hydratase of Brevibacterium R312 — purification and characterization —

✍ Scribed by Toru Nagasawa; Koichiro Ryuno; Hideaki Yamada

Book ID
117057125
Publisher
Elsevier Science
Year
1986
Tongue
English
Weight
817 KB
Volume
139
Category
Article
ISSN
0006-291X

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Purification and properties of the β-glu
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Besides its nitrile hydratase and wide spectrum amidase activities, the Brevibacterium sp. R312 strain also possesses a constitutive beta-glucosidase. Its optimum pH is 6. The enzyme was purified by fractionation precipitation with ammonium sulfate followed by chromatographic elutions on Q-Sepharose

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## Abstract Nitrile hydratase from __Brevibacterium__ sp. R312 was purified to homogeneity. The isoelectric point was 5.75. The two kinds of subunits were separated by reverse phase HPLC and their N‐terminal amino acid sequences were found to be identical to those of __Rhodococcus__ sp. N‐774 nitri

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## 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