Rational design of disulfide bonds increases thermostability of a mesophilic 1,3-1,4-β-glucanase from Bacillus terquilensis

PLoS ONE

Volumn 11, Issue 4, 2016, Pages

  Niu, Chengtuo ^a   Zhu, Linjiang ^a   Xu, Xin ^a   Li, Qi ^a  

^a JIANGNAN UNIVERSITY   (China)

Author keywords

[No Author keywords available]

Indexed keywords

1,3 1, 4 BETA GLUCANASE; BETA GLUCAN HYDROLASE; UNCLASSIFIED DRUG; DISULFIDE; GLYCOSIDASE; LICHENINASE;

ALPHA HELIX; AMINO ACID SUBSTITUTION; ARTICLE; BACILLUS; BACILLUS TERQUILENSIS; BETA SHEET; CATALYTIC EFFICIENCY; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; DISULFIDE BOND; ENTHALPY; ENTROPY; ENZYME ACTIVITY; ENZYME CONFORMATION; ENZYME INACTIVATION; ENZYME STABILITY; HYDROGEN BOND; NONHUMAN; PROTEIN EXPRESSION; PROTEIN SECONDARY STRUCTURE; CHEMISTRY; CIRCULAR DICHROISM; METABOLISM; MOLECULAR DYNAMICS; PH; TEMPERATURE;

CIRCULAR DICHROISM; DISULFIDES; ENZYME STABILITY; GLYCOSIDE HYDROLASES; HYDROGEN-ION CONCENTRATION; MOLECULAR DYNAMICS SIMULATION; TEMPERATURE;

EID: 84964589101     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0154036     Document Type: Article

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