1C1522 Contribution of Trp273 in the a-repeat of the carbohydrate-binding module of endo-1,3-β-glucanase to laminarin binding(Proteins: Measurement, Analysis, Engineering,Oral Presentation,The 50th Annual Meeting of the Biophysical Society of Japan)

Abstract

Ishida2, Akinori Ikeuchi2, lzumi Kurnagaii. Mit$uo Umetsui (i7bhoku univ. tech., 2Tbyota Central RdiD tab) Cellulose is naturally occuning plant cell wall constituent and most abundant po]ysaccharides on earth. An economically viable process for converting this biomass to fermentable sugar is a prerequisite for the development ofcellulosic biomass-based bio-refineries for the production of food, feed, chemieals and fuels. Cel]ulDse can be converted to fermentable sugar by microbial cellulose degrading enzyrnes, so ca]]ed ce]lulase. Ce]]u]ases are general]y modular proteins with an independent catalytic domain (CD) and a caTbohydrate-binding module (CBM) and in some bacteria, CDs with different functions are clustered onagiantscaffoldproteincontainingCBM,viacoheisin-dockerininteractionto eencient degradation, so called cellulosome. Recently, we proposcd a new design of artificial cellulosome to enhance ce]]ulase activity with streptavidin or streptavidin modified CdSe quantum dot as a scaffold via biotin-avidin interaction.Activity of the cluster enzyme with two kind of CBD indicated that depend on combination of scafTbld and CBD,