Structural perspectives of an engineered β-1,4-xylanase with enhanced thermostability

Journal of Biotechnology

Volumn 189, Issue , 2014, Pages 175-182

  Chen, Chun Chi ^a   Luo, Huiying ^b   Han, Xu ^a   Lv, Pin ^a   Ko, Tzu Ping ^c   Peng, Wei ^a,d   Huang, Chun Hsiang ^a   Wang, Kun ^b   Gao, Jian ^a   Zheng, Yingying ^a   Yang, Yunyun ^a,d   Zhang, Jianyu ^e   Yao, Bin ^b   Guo, Rey Ting ^a  

^a INSTITUTE OF GEOLOGY AND GEOPHYSICS   (China)

^b INSTITUTE OF PLANT PROTECTION   (China)

^c INSTITUTE OF BIOLOGICAL CHEMISTRY   (Taiwan)

^d TIANJIN UNIVERSITY OF SCIENCE AND TECHNOLOGY   (China)

^e Jilin University   (China)

Author keywords

Crystal structure; Protein engineering; Protein rigidity; Thermozyme; 1,4 Xylanase

Indexed keywords

PROTEIN ENGINEERING; PROTEIN RIGIDITIES; THERMOZYMES;

CRYSTAL STRUCTURE;

XYLAN ENDO 1,3 BETA XYLOSIDASE; ENDO-1,4-BETA XYLANASES;

ARTICLE; CONSENSUS SEQUENCE; CRYSTAL STRUCTURE; CRYSTALLIZATION; ENZYME ACTIVE SITE; ENZYME ENGINEERING; ENZYME STABILITY; ENZYME STRUCTURE; ENZYME SUBSTRATE COMPLEX; HEAT TOLERANCE; HYDROGEN BOND; MOLECULAR INTERACTION; NONHUMAN; NUCLEOTIDE SEQUENCE; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN MOTIF; THERMOPHILE; CHEMISTRY; GENETICS; METABOLISM; METHODS; PROTEIN ENGINEERING; PROTEIN STABILITY; TEMPERATURE;

ENDO-1,4-BETA XYLANASES; PROTEIN ENGINEERING; PROTEIN STABILITY; TEMPERATURE;

EID: 84908465238     PISSN: 01681656     EISSN: 18734863     Source Type: Journal    
DOI: 10.1016/j.jbiotec.2014.08.030     Document Type: Article

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