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纤维素酶解速度的可视化表征与限制因素分析
引用本文:孟凡辉,蒋绪恺,刘琳,张怀强,高培基,王禄山.纤维素酶解速度的可视化表征与限制因素分析[J].生物化学与生物物理进展,2015,42(3):201-210.
作者姓名:孟凡辉  蒋绪恺  刘琳  张怀强  高培基  王禄山
作者单位:山东大学微生物技术国家重点实验室,济南 250100,山东大学微生物技术国家重点实验室,济南 250100,山东大学微生物技术国家重点实验室,济南 250100,山东大学微生物技术国家重点实验室,济南 250100,山东大学微生物技术国家重点实验室,济南 250100,山东大学微生物技术国家重点实验室,济南 250100
基金项目:国家自然科学基金(31370111,31070063)和山东省国际科技合作项目计划(鲁科合字[2011]176号第6项)资助项目
摘    要:纤维素酶解效率是木质纤维素高效生物转化的限制瓶颈,利用原子力显微镜(atomic force microscope,AFM)可以在水相中原位可视化表征纤维素酶分子运动行为,分析单个酶分子的运动速度及其影响因素.研究发现,高效降解结晶纤维素酶分子仅结合于特定结晶表面上的特定位点上,通过单方向运动完成逐层降解,过量酶分子结合于特定表面上会导致持续性运动"塞车"现象.结晶微纤丝的降解不仅取决于酶分子运动速度及其糖苷键断裂效率,更取决于酶分子可及底物的晶面大小及其晶面氢键解聚程度.以新结合模式、新运动模式或新组织模式的纤维素酶系或复合体应是纤维素酶研究的重点方向.

关 键 词:木质纤维素  纤维素酶  原子力显微镜  降解效率  限制因素
收稿时间:8/4/2014 12:00:00 AM
修稿时间:1/4/2015 12:00:00 AM

The Visual Representation for Cellulase Degradation Velocity and The Analysis for Limiting Factor
MENG Fan-Hui,JIANG Xu-Kai,LIU Lin,ZHANG Huai-Qiang,GAO Pei-Ji and WANG Lu-Shan.The Visual Representation for Cellulase Degradation Velocity and The Analysis for Limiting Factor[J].Progress In Biochemistry and Biophysics,2015,42(3):201-210.
Authors:MENG Fan-Hui  JIANG Xu-Kai  LIU Lin  ZHANG Huai-Qiang  GAO Pei-Ji and WANG Lu-Shan
Institution:The State Key Laboratory of Microbial Technology, Shandong University, Jinan 250100, China,The State Key Laboratory of Microbial Technology, Shandong University, Jinan 250100, China,The State Key Laboratory of Microbial Technology, Shandong University, Jinan 250100, China,The State Key Laboratory of Microbial Technology, Shandong University, Jinan 250100, China,The State Key Laboratory of Microbial Technology, Shandong University, Jinan 250100, China and The State Key Laboratory of Microbial Technology, Shandong University, Jinan 250100, China
Abstract:The efficient bioconversion of lignocelluloses is limited by the enzymatic hydrolysis efficiency, atomic force microscope (AFM) enables us to represent the Real-time motion behavior of the cellulase in the aqueous solution, to analysis the moving velocity and limiting factors. Cellobiohydrolase (CBH) is demonstrated to combine to specific site of the crystal face, to move unidirectionally and accomplish the degradation layer by layer. Over-dose cellobiohydrolase which combine to special face results in the "traffic jam" phenomenon. The degradation efficiency of crystal cellulose not only depends on the moving velocity of the enzyme molecule and the cleavage of glycosidic bond, but also lies on the crystal surface area of accessible substrate and the breakdown of hydrogen bonds on the crystal face. The novel cellulase complex or system with different combining mode, different movement mode or composition mode should be an important research aspect in the future.
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