Purification and Some Properties of a Cellulase Active on Crystalline Cellulose from Cellulomonas uda
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概要
- 論文の詳細を見る
A cellulase was purified by ammonium sulfate precipitation, DEAE-Sepharose chromatography and Toyopearl HW-55F gel filtration from the culture filtrate of Cellulomonas uda CB4. The purified enzyme appeared homogeneous on disc-electrophoresis.Its isoelectric point was 4.4 and its molecular weight was estimated to be 66,000 by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The enzyme repidly hydrolyzed crystalline cellulose and produced cellobiose, but showed little activity on CM-cellulose or filter paper. It hydrolyzed cellotetraose to cellobiose but did not hydrolyze cellotriose.
- 公益社団法人日本生物工学会の論文
- 1983-08-25
著者
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Kitamura Kumpei
Applied Bioscience Laboratory Kirin Brewery Co. Ltd.
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Nakamura Katsumi
Applied Bioscience Laboratory Kirin Brewery Co. Ltd.