Improved thermostability of esterase from Aspergillus fumigatus by site-directed mutagenesis

Enzyme and Microbial Technology

Volumn 64-65, Issue , 2014, Pages 11-16

  Zhang, Shanshan ^a   Wu, Gaobing ^a   Feng, Shiyu ^a   Liu, Ziduo ^a  

^a HUAZHONG AGRICULTURAL UNIVERSITY   (China)

Author keywords

Esterase; Half life; Site directed mutagenesis; Thermostability

Indexed keywords

AMINO ACIDS; ASPERGILLUS; CLONING; ESCHERICHIA COLI; ESTERS; GENE ENCODING; HYDROGEN BONDS; STABILITY;

CATALYTIC EFFICIENCIES; ESTERASE; FAVORABLE INTERACTIONS; HALF-LIFE; SITE DIRECTED MUTAGENESIS; STRUCTURE-FUNCTION RELATIONSHIP; THERMOSTABILITY; THERMOSTABLE ESTERASE;

ENZYMES;

ESTERASE; RESTRICTION ENDONUCLEASE; FUNGAL PROTEIN; RECOMBINANT PROTEIN;

ARTICLE; ASPERGILLUS CLAVATUS; ASPERGILLUS FUMIGATUS; ASPERGILLUS ORYZAE; CATALYSIS; CONTROLLED STUDY; DNA BASE COMPOSITION; EMERICELLA NIDULANS; ENZYME ACTIVITY; ENZYME STABILITY; ESCHERICHIA COLI; FUNGAL STRAIN; HYDROGEN BOND; HYDROPHILICITY; HYDROPHOBICITY; IN VITRO STUDY; MOLECULAR CLONING; NEOSARTORYA; NONHUMAN; NUCLEOTIDE SEQUENCE; PENICILLIUM DIGITATUM; PROTEIN EXPRESSION; PROTEIN PURIFICATION; SITE DIRECTED MUTAGENESIS; STRUCTURE ACTIVITY RELATION; AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; CHEMICAL STRUCTURE; CHEMISTRY; ENZYMOLOGY; FUNGAL GENE; GENETICS; IDEOMOTOR APRAXIA; METABOLISM; MOLECULAR GENETICS; PH; PROTEIN CONFORMATION; SEQUENCE HOMOLOGY; TEMPERATURE;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; APRAXIA, IDEOMOTOR; ASPERGILLUS FUMIGATUS; CLONING, MOLECULAR; ENZYME STABILITY; ESTERASES; FUNGAL PROTEINS; GENES, FUNGAL; HYDROGEN BONDING; HYDROGEN-ION CONCENTRATION; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; PROTEIN CONFORMATION; RECOMBINANT PROTEINS; SEQUENCE HOMOLOGY, AMINO ACID; TEMPERATURE;

EID: 84904306074     PISSN: 01410229     EISSN: 18790909     Source Type: Journal    
DOI: 10.1016/j.enzmictec.2014.06.003     Document Type: Article

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