Fusion of an oligopeptide to the N terminus of an alkaline α-amylase from Alkalimonas amylolytica simultaneously improves the enzyme's catalytic efficiency, thermal stability, and resistance to oxidation

Applied and Environmental Microbiology

Volumn 79, Issue 9, 2013, Pages 3049-3058

  Yang, Haiquan ^a   Lu, Xinyao ^a   Liu, Long ^a   Li, Jianghua ^a   Shin, Hyun Dong ^b   Chen, Rachel R ^b   Du, Guocheng ^a   Chen, Jian ^a  

^a JIANGNAN UNIVERSITY   (China)

^b Georgia Institute of Technology   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CATALYTIC CONSTANTS; CATALYTIC EFFICIENCIES; DETERGENT INGREDIENTS; INDUSTRIAL ENZYMES; OPTIMAL TEMPERATURE; OXIDATIVE STABILITY; STRUCTURAL CHARACTERISTICS; THREEDIMENSIONAL (3-D);

CATALYST ACTIVITY; CATALYTIC OXIDATION; EFFICIENCY; MODEL STRUCTURES; PEPTIDES; SOAPS (DETERGENTS); THERMODYNAMIC STABILITY;

AMYLASES;

ALKALINITY; BACTERIOLOGY; BACTERIUM; CATALYSIS; DETERGENT; ENZYME ACTIVITY; HYDROGEN PEROXIDE; NITROGEN; OXIDATION; PEPTIDE; PH; PROTEIN; TEMPERATURE TOLERANCE;

ALKALIMONAS AMYLOLYTICA;

AMYLASE; BACTERIAL PROTEIN; DETERGENT; HYBRID PROTEIN; HYDROGEN PEROXIDE; OLIGOPEPTIDE;

AMINO ACID SEQUENCE; AUDIOVISUAL EQUIPMENT; BIOCATALYSIS; ENZYME STABILITY; ENZYMOLOGY; GAMMAPROTEOBACTERIA; GENE EXPRESSION; GENETICS; HALF LIFE TIME; HEAT; ISOLATION AND PURIFICATION; KINETICS; METABOLISM; MOLECULAR DYNAMICS; MOLECULAR GENETICS; OXIDATION REDUCTION REACTION; PH; PROTEIN CONFORMATION; PROTEIN ENGINEERING;

ALPHA-AMYLASES; AMINO ACID SEQUENCE; BACTERIAL PROTEINS; BIOCATALYSIS; DETERGENTS; ENZYME STABILITY; GAMMAPROTEOBACTERIA; GENE EXPRESSION; HALF-LIFE; HOT TEMPERATURE; HYDROGEN PEROXIDE; HYDROGEN-ION CONCENTRATION; KINETICS; MODELS, STRUCTURAL; MOLECULAR DYNAMICS SIMULATION; MOLECULAR SEQUENCE DATA; OLIGOPEPTIDES; OXIDATION-REDUCTION; PROTEIN CONFORMATION; PROTEIN ENGINEERING; RECOMBINANT FUSION PROTEINS;

EID: 84876303319     PISSN: 00992240     EISSN: 10985336     Source Type: Journal    
DOI: 10.1128/AEM.03785-12     Document Type: Article

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