The enzymatic hydrolysis of crystalline region of cellulose is one of the bottlenecks to produce bioenergy and bio-chemicals. To understand the interactions between the binding modules of cellulases and the surface of cellulose polymorphs is helpful to understand the mechanism of emzymatic hydrolysis of cellulose and therefore is helpful to enhance the efficiency of enzymatic hydrolysis, to reduce the loading of enzymes and to improve the recovery rate of enzymes. In this investigation, microcrystalline cellulose was initially treated with NaOH and then suffered to hydrolysis to obtain the cellulose crystals with polymorphs of Cellulose II and the intermediate polymorphs of cellulose I/II. Followed by modification QCM sensors with those produced crystals, the interactions between cellulose crystal surface and four cellulases from different origins of Trichoderma reesei ATCC 26921, Trichoderma viride, Aspergillus sp. and Aspergillus niger were monitored by Quartz Crystal Microbalance at 15 <sup>o</sup>C and then the corresponding hydrolysis was monitored was well at 45 <sup>o</sup>C. The results showed that cellulase from different origin have different affinity to cellulose surface due to their have different binding modules. And the polymorpths of cellulose crystals also have some impacts on the dynamics of adsorption and have significant influence on the hydrolysis. The results of this investigation will provide some theoratical evidences to the pretreatments of lignocellulosics, the oriented culture and the recovery of cellulases.

Interactions between cellulose surfaces and cellulases from different origins studied by QCM

251st National Meeting (2016)

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