Cellulose Hydrolysis - The Role of Monocomponent Cellulases in Crystalline Cellulose Degradation

作者: Shawn D Mansfield , Roger Meder

DOI: 10.1023/A:1024022710366

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摘要: Changes in the molecular structure of cellulose during hydrolysis with four recombinant β-1,4-glycanases from cellulolytic bacterium Cellulomonas fimi were assessed and compared an attempt to elucidate mechanism crystalline degradation. It was apparent that two endoglucanases, Cel6A Cel5A, degraded sigmacell differently; Cel5A liberated more soluble sugars (cellobiose cellotriose) significantly altered weight distribution, while had a limited effect on polymer size primarily cellobiose glucose. Additionally, both endoglucanases slightly increased crystallinity cellulose. In contrast, cellobiohydrolases, Cel6B Cel48A, no only cellotriose. However, Cel48A shown be effective at reducing cellulosic substrate, index. Synergistic using combinations different enzymes showed that, although extensively hydrolysed, substrate similar original material. This phenomenon suggests actions individual monocomponent are offset by concurrent modification complementing synergistic hydrolysis.

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