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Purification and properties of endo-(1→4)-β-d-glucanase from Ruminococcus albus

✍ Scribed by Kunio Ohmiya; Keiko Maeda; Shoichi Shimizu

Publisher
Elsevier Science
Year
1987
Tongue
English
Weight
875 KB
Volume
166
Category
Article
ISSN
0008-6215

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✦ Synopsis

An enzyme active against 0-(carboxymethyl)cellulose (CMC) was purified from a synthetic medium containing ball-milled cellulose wherein Ruminococcus albus had been cultivated for 70 h. After 570-fold purification, a homogeneous enzyme was obtained in a yield of 3%. The enzyme degraded CMC (molecular weight, 180,000; degree of substitution, 0.6) to a smaller polymer having a molecular weight of -20,000, and generated a small proportion of glucose, but negligible proportions of such cello-saccharides as cellobiose, celiotriose, cellotetraose, or cellopentaose. The fact that the enzyme could produce water-in~luble fragments was discovered by dissolving substrate and products in Cadoxen solution.

No water-soluble cello-oligomers were detected by thin-layer chromatography after degradation of water-insoluble cellulose by the purified enzyme. Therefore, the enzyme was classified as an endo-( I-+4)-/3-D-giucanase,

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