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Molecular and biochemical characterizations of a new cold-active and mildly alkaline beta-Mannanase from Verrucomicrobiae DG1235

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成果类型:
期刊论文
作者:
Xie, Huifang;Poon, Chun Kin Kingsley;Liu, Hanyan;Wang, Dan;Yang, Jiangke*;...
通讯作者:
Yang, Jiangke;Han, Zhenggang
作者机构:
[Liu, Hanyan; Yang, JK; Han, ZG; Wang, Dan; Xie, Huifang; Yang, Jiangke; Han, Zhenggang] Wuhan Polytech Univ, Coll Biol & Pharmaceut Engn, Wuhan 430023, Peoples R China.
[Poon, Chun Kin Kingsley] Shanghai Xuhui Siqiao Sci & Technol Res Ctr, Shanghai, Peoples R China.
[Poon, Chun Kin Kingsley] Shanghai High Sch, Int Div, Shanghai, Peoples R China.
通讯机构:
[Yang, JK; Han, ZG] W
Wuhan Polytech Univ, Coll Biol & Pharmaceut Engn, Wuhan 430023, Peoples R China.
语种:
英文
关键词:
Alkaline;cold-active;mannanase;mannans;Verrucomicrobiae
期刊:
Preparative Biochemistry & Biotechnology
ISSN:
1082-6068
年:
2021
卷:
51
期:
9
页码:
881-891
基金类别:
Hubei Provincial Natural Science Foundation of ChinaNational Natural Science Foundation of China (NSFC) [2020CFB803]; China Ocean Mineral Resources Research and Development Association [DY135-B2-06]
机构署名:
本校为第一且通讯机构
院系归属:
生命科学与技术学院
摘要:
Mannanases catalyze the cleavage of β-1,4-mannosidic linkages in mannans and have various applications in different biotechnological industries. In this study, a new β-mannanase from Verrucomicrobiae DG1235 (ManDG1235) was biochemically characterized and its enzymatic properties were revealed. Amino acid alignment indicated that ManDG1235 belonged to glycoside hydrolase family 26 and shared a low amino acid sequence identity to reported β-mannanases (up to 50% for CjMan26C from Cellvibrio japonicus). ManDG1235 was expressed in Escherichia co...

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