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Partial Purification of Cellulase from Clostridium thermocellum

✍ Scribed by AIT, N.; CREUZET, N.; FORGET, P.


Book ID
121812258
Publisher
Microbiology Society
Year
1979
Tongue
English
Weight
521 KB
Volume
113
Category
Article
ISSN
0022-1287

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Crystallization of a family 8 cellulase
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The catalytic domain of cellulase CelA, a family 8 glycohydrolase from C. thennocellurn, h a s been crystallized in the orthorhombic space group P212121 with unit cell dimensions a = 50.12 A, b = 63.52 A, c = 104.97 A. The diffraction pattern extends beyond 1.5 A resolution.

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Acetate kinase (EC 2.7.2.1), an enzyme involved in the wasteful production of acetate during conversion of cellulose to ethanol by Clostridlum thermocellum, was purified 144-fold. The enzyme has an Mr of 84 kD by non-denaturing gradient gel electrophoresis, and an Mr of 46 kD when estimated with a d