Simultaneously Enhanced Thermostability and Catalytic Activity of Xylanase from <i>Streptomyces rameus</i> L2001 by Rigidifying Flexible Regions in Loop Regions of the N-Terminus-Reference-Cited by-同舟云学术

Simultaneously Enhanced Thermostability and Catalytic Activity of Xylanase from Streptomyces rameus L2001 by Rigidifying Flexible Regions in Loop Regions of the N-Terminus

Published:2023-08-17 Issue:34 Volume:71 Page:12785-12796
ISSN:0021-8561
Container-title:Journal of Agricultural and Food Chemistry
language:en
Short-container-title:J. Agric. Food Chem.

Author:

Wu Qiuhua¹²³,Zhang Chengnan¹⁴⁵³,Dong Wenqi¹²³,Lu Hongyun¹⁴³,Yang Yue¹²³,Li Weiwei¹⁴⁵³,Xu Youqiang¹²⁵³,Li Xiuting¹²⁴⁵³^ORCID

Affiliation:

1. Ministry of Education, Key Laboratory of Geriatric Nutrition and Health (Beijing Technology and Business University), Beijing 100048, China

2. China General Chamber of Commerce, Key Laboratory of Brewing Microbiome and Enzymatic Molecular Engineering, Beijing 100048, China

3. School of Food and Health, Beijing Technology and Business University (BTBU), Beijing 100048, China

4. Beijing Advanced Innovation Center for Food Nutrition and Human Health, Beijing Technology and Business University (BTBU), Beijing 100048, China

5. Beijing Association for Science and Technology-Food Nutrition and Safety Professional Think Tank Base, Beijing 100048, China

Funder

Beijing Municipal Commission of Education

National Key Research and Development Program of China

Beijing Municipal Natural Science Foundation

National Natural Science Foundation of China

Publisher

American Chemical Society (ACS)

Subject

General Agricultural and Biological Sciences,General Chemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/acs.jafc.3c03871

Reference48 articles.

1. Thermostable xylanases from thermophilic fungi and bacteria: Current perspective

2. xln23 from Streptomyces chattanoogensis UAH23 Encodes a Putative Enzyme with Separate Xylanase and Arabinofuranosidase Catalytic Domains

3. A classification of glycosyl hydrolases based on amino acid sequence similarities

4. Sequence- and structure-guided improvement of the catalytic performance of a GH11 family xylanase from Bacillus subtilis

5. Improved thermostability, acid tolerance as well as catalytic efficiency of Streptomyces rameus L2001 GH11 xylanase by N-terminal replacement

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