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Reductant-independent oxidative cleavage of cellulose by a novel marine fungal lytic polysaccharide monooxygenase.
Hoang, Honghanh; Liu, Wenxian; Zhan, Wenhao; Zou, Sini; Xu, Liting; Zhan, Yuran; Cheng, Haina; Chen, Zhu; Zhou, Hongbo; Wang, Yuguang.
Affiliation
  • Hoang H; School of Minerals Processing and Bioengineering, Central South University, Changsha 410083, China.
  • Liu W; School of Minerals Processing and Bioengineering, Central South University, Changsha 410083, China.
  • Zhan W; National Key Laboratory of Human Factors Engineering, China Astronauts Research and Training Center, Beijing 100094, China.
  • Zou S; School of Minerals Processing and Bioengineering, Central South University, Changsha 410083, China.
  • Xu L; School of Minerals Processing and Bioengineering, Central South University, Changsha 410083, China.
  • Zhan Y; School of Minerals Processing and Bioengineering, Central South University, Changsha 410083, China.
  • Cheng H; School of Minerals Processing and Bioengineering, Central South University, Changsha 410083, China; Key Laboratory of Biometallurgy of Ministry of Education, Central South University, Changsha 410083, China.
  • Chen Z; School of Minerals Processing and Bioengineering, Central South University, Changsha 410083, China.
  • Zhou H; School of Minerals Processing and Bioengineering, Central South University, Changsha 410083, China; Key Laboratory of Biometallurgy of Ministry of Education, Central South University, Changsha 410083, China.
  • Wang Y; School of Minerals Processing and Bioengineering, Central South University, Changsha 410083, China; Key Laboratory of Biometallurgy of Ministry of Education, Central South University, Changsha 410083, China. Electronic address: ygwang@csu.edu.cn.
Int J Biol Macromol ; 276(Pt 2): 133929, 2024 Sep.
Article in En | MEDLINE | ID: mdl-39025178
ABSTRACT
Among the enzymes derived from fungus that act on polysaccharides, lytic polysaccharide monooxygenase (LPMOs) has emerged as a new member with complex reaction mechanisms and high efficiency in dealing with recalcitrant crystalline polysaccharides. This study reported the characteristics, structure, and biochemical properties of a novel LPMO from Talaromyces sedimenticola (namely MaLPMO9K) obtained from the Mariana Trench. MaLPMO9K was a multi-domain protein combined with main body and a carbohydrate-binding module. It was heterologously expressed in E. coli for analyzing peroxidase activity in reactions with the substrate 2,6-DMP, where H2O2 serves as a co-substrate. Optimal peroxidase activity for MaLPMO9K was observed at pH 8 and 25 °C, achieving the best Vmax value of 265.2 U·g-1. In addition, MaLPMO9K also demonstrated the ability to treat cellulose derivatives, and cellobiose substrates without the presence of reducing agents.
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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Oxidation-Reduction / Cellulose / Mixed Function Oxygenases Language: En Journal: Int J Biol Macromol Year: 2024 Document type: Article Affiliation country:
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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Oxidation-Reduction / Cellulose / Mixed Function Oxygenases Language: En Journal: Int J Biol Macromol Year: 2024 Document type: Article Affiliation country: