Heterologous expression and characterization of a novel lytic polysaccharide monooxygenase from Natrialbaceae archaeon and its application for chitin biodegradation

Heterologous expression and characterization of a novel lytic polysaccharide monooxygenase from Natrialbaceae archaeon and its application for chitin biodegradation
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钠藻科古菌新型裂解性多糖单加氧酶的异源表达和表征及其在几丁质生物降解中的应用

DOI:
10.1016/j.biortech.2022.127174
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发表时间:
2022-04-20
影响因子:
11.4
通讯作者:
Yu, Hongbo
Yu, Hongbo
中科院分区:
工程技术1区
文献类型:
--
作者:
Li, Fei;Liu, Yuxin;Yu, Hongbo

文献摘要

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裂解多糖单加氧酶能促进糖苷水解酶对柠檬酸多糖的酶促转化。本研究报道了一种新的来源于Natrialbaceae古菌的AA 10 LPMO的表达和鉴定,命名为NaLPMO 10A,作为几丁质的C1氧化剂。NaLPMO10A的最适温度和pH分别为40 ℃和9.0,在碱性条件下,NaLPMO10A表现出较高的热稳定性和pH稳定性。NaLPMO10A在高浓度金属离子(1M)处理下也具有很高的耐受性和稳定性。金属离子(Na+、K+、Ca2+和Mg2+)对NaLPMO10A酶活有显著的促进作用,使几丁质的糖化效率分别提高了22.6%、45.9%、36.7%和53.9%。总之,这项研究的发现填补了古细菌LPMO研究的空白,并首次证明古细菌NaLPMO10A可能是一种有前途的酶,用于改善极端条件下的糖化,并在生物精炼中具有潜在的应用。
Lytic polysaccharide monooxygenases could enhance the enzymatic conversion of recalcitrant polysaccharides by glycoside hydrolases. This study reports the expression and identification of a novel AA10 LPMO from Natrialbaceae archaeon, named NaLPMO10A, as a C1 oxidizer of chitin. The optimal temperature and pH for NaLPMO10A activity were 40 degrees C and 9.0, respectively, and NaLPMO10A exhibited high thermostability and pH stability under alkaline conditions. NaLPMO10A was also highly tolerant and stable when treated with high concentration of metal ions (1 M). Moreover, metal ions (Na+, K+, Ca2+ and Mg2+) significantly promoted NaLPMO10A activity and improved the saccharification efficiency of chitin by 22.6%, 45.9%, 36.7% and 53.9%, respectively, compared to commercial chitinase alone. Together, the findings of this study fill a gap in archaeal LPMO research, and for the first time demonstrate that archaeal NaLPMO10A could be a promising enzyme for improving saccharification under extreme condition, with potential applications in biorefineries.