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Lytic polysaccharide monooxygenases from Myceliophthora thermophila C1 differ in substrate preference and reducing agent specificity

机译:嗜热毁丝霉C1的溶菌多糖单加氧酶在底物偏好和还原剂特异性上不同

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摘要

BackgroundLytic polysaccharide monooxgygenases (LPMOs) are known to boost the hydrolytic breakdown of lignocellulosic biomass, especially cellulose, due to their oxidative mechanism. For their activity, LPMOs require an electron donor for reducing the divalent copper cofactor. LPMO activities are mainly investigated with ascorbic acid as a reducing agent, but little is known about the effect of plant-derived reducing agents on LPMOs activity.
机译:背景技术已知溶质多糖单加氧合酶(LPMO)由于其氧化机理而促进木质纤维素生物质尤其是纤维素的水解分解。对于其活性,LPMO需要电子供体来还原二价铜辅助因子。 LPMO活性主要以抗坏血酸作为还原剂进行研究,但对于植物衍生的还原剂对LPMO活性的影响知之甚少。

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