Heterologous expression and characterization of a novel lytic polysaccharide monooxygenase from Natrialbaceae archaeon and its application for chitin biodegradation
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Li, Fei
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Huazhong Univ Sci & Technol, Coll Life Sci & Technol, Dept Biotechnol, Wuhan 430074, Peoples R ChinaHuazhong Univ Sci & Technol, Coll Life Sci & Technol, Dept Biotechnol, Wuhan 430074, Peoples R China
Li, Fei
[1
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Liu, Yuxin
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Huazhong Univ Sci & Technol, Coll Life Sci & Technol, Dept Biotechnol, Wuhan 430074, Peoples R ChinaHuazhong Univ Sci & Technol, Coll Life Sci & Technol, Dept Biotechnol, Wuhan 430074, Peoples R China
Liu, Yuxin
[1
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Liu, Yang
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Huazhong Univ Sci & Technol, Coll Life Sci & Technol, Dept Biotechnol, Wuhan 430074, Peoples R ChinaHuazhong Univ Sci & Technol, Coll Life Sci & Technol, Dept Biotechnol, Wuhan 430074, Peoples R China
Liu, Yang
[1
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Li, Yanjun
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Huazhong Univ Sci & Technol, Coll Life Sci & Technol, Dept Biotechnol, Wuhan 430074, Peoples R ChinaHuazhong Univ Sci & Technol, Coll Life Sci & Technol, Dept Biotechnol, Wuhan 430074, Peoples R China
Li, Yanjun
[1
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Yu, Hongbo
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Huazhong Univ Sci & Technol, Coll Life Sci & Technol, Dept Biotechnol, Wuhan 430074, Peoples R ChinaHuazhong Univ Sci & Technol, Coll Life Sci & Technol, Dept Biotechnol, Wuhan 430074, Peoples R China
Yu, Hongbo
[1
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[1] Huazhong Univ Sci & Technol, Coll Life Sci & Technol, Dept Biotechnol, Wuhan 430074, Peoples R China
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.
机构:
Shandong Agr Univ, Dept Mycol, Tai An 271018, Shandong, Peoples R ChinaShandong Agr Univ, Dept Mycol, Tai An 271018, Shandong, Peoples R China
Yu, Weishuai
Mohsin, Imran
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Univ Turku, Turku Biosci Ctr, Turku 20521, Finland
Abo Akad Univ, Turku Biosci Ctr, Turku 20521, FinlandShandong Agr Univ, Dept Mycol, Tai An 271018, Shandong, Peoples R China
Mohsin, Imran
Papageorgiou, Anastassios C.
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Univ Turku, Turku Biosci Ctr, Turku 20521, Finland
Abo Akad Univ, Turku Biosci Ctr, Turku 20521, FinlandShandong Agr Univ, Dept Mycol, Tai An 271018, Shandong, Peoples R China
Papageorgiou, Anastassios C.
Li, Duochuan
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Shandong Agr Univ, Dept Mycol, Tai An 271018, Shandong, Peoples R ChinaShandong Agr Univ, Dept Mycol, Tai An 271018, Shandong, Peoples R China