バイオマス科学会議発表論文集
Online ISSN : 2423-8341
Print ISSN : 2423-8333
ISSN-L : 2423-8333
第11回バイオマス科学会議
セッションID: P-28
会議情報

P-28 結晶性セルロースの分解における溶解性多糖モノオキシゲナーゼとセロビオヒドロラーゼの相乗効果(糖化・発酵,ポスター発表)
石田 卓也中村 彰彦渡辺 大輝内橋 貴之安藤 敏夫和田 昌久五十嵐 圭日子鮫島 正浩
著者情報
会議録・要旨集 フリー

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抄録
Lytic Polysaccharide Monooxigenases (LPMOs) classified into Auxiliary Activity (AA) family 9 of Carbohydrate Active enZymes (CAZy) database degrade insoluble cellulose and release oxidized cello-oligosaccharides as reaction products. PcLPMO9D is a LPMO secreted by the basidiomycete Phanerochaete chrysosporium. As other LPMOs from wood-rotting fungi, the enzyme has catalytic activity that degrades insoluble cellulose and release C1-oxidized cello-oligosaccharides. LPMOs are generally known to show synergy effect with other hydrolytic cellulases and "boost" the cellulose degradation. However, the mechanism of this synergism between LPMO and cellulases has been unclear. In this study, High speed Atomic Force Microscopy (HsAFM) observation was conducted to visualize the effect of PcLPMO9D on the motion of a hydrolytic cellulase PcCe17D on the crystalline cellulose. When PcLPMO9D was added to the reaction solution, the number of PcCe17D observed on the crystalline cellulose significantly increased, indicating PcLPMO9D creates the chain end of cellulose molecules where PcCe17D can bind and start the reaction. Moreover, PcCe17D found on extended area of cellulose crystal after addition of PcLPMO9D, suggesting that PcLPMO9D may act on the crystalline surface which is not accessible for PcCe17D without LPMO activity.
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