A combination of weakly stabilizing mutations with a disulfide bridge in the α-helix region of Trichoderma reesei endo-1,4-β-xylanase II increases the thermal stability through synergism

Journal of Biotechnology

Volumn 88, Issue 1, 2001, Pages 37-46

  Turunen, Ossi ^a   Etuaho, Kirsikka ^a   Fenel, Fred ^a   Vehmaanperä, Jari ^b   Wu, Xiaoyan ^a   Rouvinen, Juha ^c   Leisola, Matti ^a  

^a AALTO UNIVERSITY   (Finland)

^b Roal Oy   (Finland)

^c UNIVERSITY OF EASTERN FINLAND   (Finland)

Author keywords

Designed mutations; Endo 1,4 xylanase; Family 11; PH activity; Thermal stability; Trichoderma reesei

Indexed keywords

GENETIC ENGINEERING; PH EFFECTS; SULFUR COMPOUNDS; THERMODYNAMIC STABILITY;

MUTATIONS;

BIOTECHNOLOGY;

AMINO ACID; DISULFIDE; ENDO 1,4 BETA XYLANASE II; MUTANT PROTEIN; UNCLASSIFIED DRUG;

ALPHA HELIX; ARTICLE; CARBOXY TERMINAL SEQUENCE; CHROMATOGRAPHY; CLONE; ENZYME ACTIVITY; ENZYME ASSAY; ENZYME STABILITY; GENE STRUCTURE; HALF LIFE TIME; KINETICS; MUTATION; NONHUMAN; PH; PRIORITY JOURNAL; TEMPERATURE; THERMOSTABILITY; TRICHODERMA REESEI;

CATALYTIC DOMAIN; DISULFIDES; ENDO-1,4-BETA XYLANASES; ENZYME STABILITY; HYDROGEN-ION CONCENTRATION; KINETICS; MUTATION; PROTEIN CONFORMATION; PROTEIN ENGINEERING; TEMPERATURE; TRICHODERMA; XYLOSIDASES;

HYPOCREA JECORINA; TRICHODERMA;

EID: 0035370202     PISSN: 01681656     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0168-1656(01)00253-X     Document Type: Article

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