Rationally selected single-site mutants of the Thermoascus aurantiacus endoglucanase increase hydrolytic activity on cellulosic substrates

Biotechnology and Bioengineering

Volumn 109, Issue 6, 2012, Pages 1595-1599

  Srikrishnan, Sneha ^a   Randall, Arlo ^b   Baldi, Pierre ^b   Da Silva, Nancy A ^a,b  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

Cellulase; Endo 1,4 glucanase; Hydrolysis; Mutagenesis; Pichia pastoris; Thermoascus aurantiacus

Indexed keywords

AMINO ACID RESIDUES; CATALYTIC EFFICIENCIES; CELLULASE; CELLULOSIC SUBSTRATES; ENDOGLUCANASES; HYDROLYTIC ACTIVITIES; INITIAL ACTIVITY; NON-CATALYTIC; OPTIMAL ACTIVITY; PICHIA PASTORIS; PRE-TREATMENT; PURIFIED ENZYME; SINGLE MUTATION; SINGLE SITES; SITE DIRECTED MUTAGENESIS; STRUCTURAL BIOINFORMATICS; THERMOASCUS AURANTIACUS; WILD TYPES;

AMINO ACIDS; BIOINFORMATICS; ENZYME ACTIVITY; HYDROLYSIS; MUTAGENESIS; YEAST;

EFFICIENCY;

GLUCAN SYNTHASE;

ARTICLE; BIOINFORMATICS; CATALYSIS; ENZYME ACTIVITY; ENZYME PURIFICATION; EVOLUTION; HYDROLYSIS; MUTATION; NONHUMAN; PH; PICHIA PASTORIS; PREMEDICATION; PROTEIN EXPRESSION; SITE DIRECTED MUTAGENESIS; TEMPERATURE; THERMOASCUS; THERMOSTABILITY;

AMINO ACID SUBSTITUTION; CELLULASE; CELLULOSE; CLONING, MOLECULAR; ENZYME STABILITY; GENE EXPRESSION; HYDROGEN-ION CONCENTRATION; HYDROLYSIS; KINETICS; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; MUTANT PROTEINS; MUTATION, MISSENSE; PICHIA; PROTEIN CONFORMATION; TEMPERATURE; THERMOASCUS;

PICHIA PASTORIS; THERMOASCUS AURANTIACUS;

EID: 84859922225     PISSN: 00063592     EISSN: 10970290     Source Type: Journal    
DOI: 10.1002/bit.24414     Document Type: Article

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