Site-directed mutagenesis of an alkaline phytase: Influencing specificity, activity and stability in acidic milieu

Enzyme and Microbial Technology

Volumn 49, Issue 2, 2011, Pages 177-182

  Tran, Thuy T ^a,b   Mamo, Gashaw ^a   Búxo, Laura ^a   Le, Nhi N ^a   Gaber, Yasser ^a,c   Mattiasson, Bo ^a   Hatti Kaul, Rajni ^a  

^a LUND UNIVERSITY   (Sweden)

^b Department of Biotechnology and Microbiology   (United States)

^c Beni Suef University   (Egypt)

Author keywords

Bacillus sp.; Phytase; Site directed mutagenesis; Substrate specificity

Indexed keywords

ACIDIC CONDITIONS; ACIDIC ENVIRONMENT; ACTIVE SITE; ACTIVE SITE RESIDUES; BACILLUS SP; CALCIUM PHYTATE; CATALYTIC SURFACES; CHARGED RESIDUES; DOUBLE MUTANTS; INITIAL ACTIVITY; MUTANT PHYTASE; MUTATION SITES; OPTIMUM PH; PHYTASES; POSITIVE CHARGES; POSITIVELY CHARGED; RELATIVE ACTIVITIES; SITE DIRECTED MUTAGENESIS; SODIUM PYROPHOSPHATE; SPECIFIC ACTIVITY; SUBSTRATE SPECIFICITY; SUBSTRATE-BINDING; WILD TYPES; WILD-TYPE ENZYMES;

ALKALINITY; BACILLI; BACTERIOLOGY; HYDROGEN BONDS; HYDROLYSIS; MUTAGENESIS; SODIUM; STABILITY; SUBSTRATES;

ENZYME ACTIVITY;

ALKALINE PHYTASE; BACTERIAL ENZYME; CALCIUM PHYTATE; PARAOXON; PHYTASE; PHYTATE; PYROPHOSPHATE; UNCLASSIFIED DRUG;

ACIDITY; ARTICLE; BACILLUS AMYLOLIQUEFACIENS; BACILLUS LICHENIFORMIS; BACTERIAL STRAIN; CATALYSIS; CONTROLLED STUDY; ENVIRONMENT; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME BINDING; ENZYME SPECIFICITY; ENZYME STABILITY; ENZYME SUBSTRATE; HYDROGEN BOND; MOLECULAR DOCKING; MUTANT; MUTATIONAL ANALYSIS; NONHUMAN; NUCLEOTIDE SEQUENCE; PROTEIN HYDROLYSIS; RECOMBINANT PLASMID; SITE DIRECTED MUTAGENESIS; STRUCTURE ANALYSIS; SURFACE CHARGE; WILD TYPE;

6-PHYTASE; AMINO ACID SUBSTITUTION; BACILLUS; BACTERIAL PROTEINS; BASE SEQUENCE; CATALYTIC DOMAIN; DNA PRIMERS; ENZYME STABILITY; HYDROGEN-ION CONCENTRATION; KINETICS; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; MUTANT PROTEINS; PROTEIN CONFORMATION; RECOMBINANT PROTEINS; SUBSTRATE SPECIFICITY;

BACILLUS SP.;

EID: 79959881355     PISSN: 01410229     EISSN: 18790909     Source Type: Journal    
DOI: 10.1016/j.enzmictec.2011.05.012     Document Type: Article

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