Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10870586 | FEBS Letters | 2014 | 5 Pages |
Abstract
To understand the lignocellulose degradation activity of the Clostridium josui cellulosome, a carbohydrate-binding module of the scaffoldin CjCBM3 was characterized. CjCBM3 shows binding to crystalline cellulose, non-crystalline cellulose and soluble polysaccharides. The binding isotherm of CjCBM3 to acid-swollen cellulose is best fitted by the Langmuir two-site model, suggesting that there are two CjCBM3 binding sites on acid-swollen cellulose with different affinities. The second site shows lower affinity and larger binding capacity, suggesting that the cellulosome is directly targeted to the cellulose surface with high affinity, where larger amounts of the cellulosome bind to cellulose with low affinity.
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Authors
Shunsuke Ichikawa, Shuichi Karita, Makoto Kondo, Masakazu Goto,