Structural and functional study of a novel lytic polysaccharide monooxygenase cPMO2 from compost sample in the oxidative degradation of cellulose
CHEMICAL ENGINEERING JOURNAL(2022)
摘要
Lytic polysaccharide monooxygenases (LPMOs) are the major groups of oxidizing the recalcitrant polysaccharides. Here, a novel AA9 family protein cPMO2 originated from composting was characterized, and it had a better binding capacity to phosphoric acid swollen cellulose (PASC) and Avicel, as well the isothermal titration calorimetry (ITC) analysis showed that it owned a considerable capacity of binding Cu2+ with the K-d value of 1.58 & PLUSMN; 0.78 mu M. Interestingly, the kinetics of cPMO2 by using 2, 6-dimethoxyphenol (2, 6-DMP) as substrate indicated that cPMO2 was a novel member of LPMOs family, with the V-max of 21.30 & PLUSMN; 0.83 U.g(-1) at pH 7.5. In addition, cPMO2 owned a broad substrate specificity, which could act on PASC and xylan at the C1 site based on the MALDI-TOF-MS analysis results. Simultaneously, cPMO2 could also act on Avicel directly resulting the decrease of crystallinity by 4% and further to synergistic degradation of corncob and rice straw with glycoside hydrolases. The structure of the functional region of cPMO2 was obtained by using single-crystal X-ray diffraction, and the enzymatic properties and molecular docking analysis results showed that His1 and Tyr175 were the critical active sites of the cPMO2. Altogether, this study will be a supplement for the AA9 LPMOs in cellulose degradation.
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关键词
Lytic polysaccharide monooxygenases,Composting,Cellulose,Synergistic activity,Dynamic characteristics
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