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Molecular cloning and characterisation of a novel xanthine oxidase from Cellulosimicrobium cellulans ATCC21606

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成果类型:
期刊论文
作者:
Chen, Yuanyuan;Li, Yan;Chao, Hongjun;Wu, Jing;Zhu, Wenjun;...
通讯作者:
Yan, Dazhong
作者机构:
[Wu, Jing; Yan, Dazhong; Li, Yan; Chen, Yuanyuan; Zhu, Wenjun; Chao, Hongjun] Wuhan Polytech Univ, Sch Biol & Pharmaceut Engn, 68 Xuefu South Rd, Wuhan 430023, Peoples R China.
[Fang, Ti] Chinese Acad Sci, Wuhan Inst Virol, State Key Lab Virol, 44 Xiaohongshan, Wuhan 430071, Peoples R China.
[Gao, Xuewang] Chinese Acad Sci, Tech Inst Phys & Chem, Beijing 100190, Peoples R China.
通讯机构:
[Yan, Dazhong] W
Wuhan Polytech Univ, Sch Biol & Pharmaceut Engn, 68 Xuefu South Rd, Wuhan 430023, Peoples R China.
语种:
英文
关键词:
Cellulosimicrobium cellulans ATCC21606;Pseudomonas putida PaW340;Recombinant expression;Thermostability;Xanthine oxidase
期刊:
Process Biochemistry
ISSN:
1359-5113
年:
2020
卷:
91
页码:
65-72
基金类别:
National Natural Science Foundation of ChinaNational Natural Science Foundation of China [31770119, 31400114]
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:
Xanthine oxidase (XOD) catalyses the oxidation of hypoxanthine into xanthine and xanthine into uric acid. The enzyme plays a key role in the purine metabolic pathway. Despite the presence of different XODs in prokaryotes, the functional and structural knowledge of prokaryotic XODs remain limited (compared with their well-known eukaryotic counterparts), thereby hindering their biochemical analysis and industrial application. Using genetic and biochemical analyses, we identified and characterised recombinant XOD (CcXODAB) from Cellulosimicrobium ...

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