Adopting selected hydrogen bonding and ionic interactions from Aspergillus fumigatus phytase structure improves the thermostability of Aspergillus niger PhyA phytase

Applied and Environmental Microbiology

Volumn 73, Issue 9, 2007, Pages 3069-3076

  Zhang, Wanming ^a   Mullaney, Edward J ^b   Xin, Gen Lei ^a  

^a Department of Obstetrics Gynecology   (United States)

^b SOUTHERN REGIONAL RESEARCH CENTER   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CRYSTAL STRUCTURE; HYDROGEN BONDS; MELTING POINT; PHOSPHORUS COMPOUNDS;

ASPERGILLUS FUMIGATUS PHYTASE STRUCTURE; ASPERGILLUS NIGER PHYA PHYTASE; IONIC INTERACTIONS; MANURE PHOSPHORUS POLLUTION;

ENZYME KINETICS;

PHYTASE;

CHEMICAL BONDING; CRYSTAL STRUCTURE; ENZYME; HYDROGEN; MANURE; MUTATION; PHOSPHORUS; POULTRY; WADER;

ARTICLE; ASPERGILLUS FUMIGATUS; ASPERGILLUS NIGER; CRYSTAL STRUCTURE; HYDROGEN BOND; ION TRANSPORT; NONHUMAN; SEQUENCE HOMOLOGY; SUBSTITUTION REACTION; THERMOSTABILITY;

6-PHYTASE; ASPERGILLUS FUMIGATUS; ASPERGILLUS NIGER; CALORIMETRY, DIFFERENTIAL SCANNING; DNA PRIMERS; ENZYME STABILITY; HEAT; HYDROGEN BONDING; IONS; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; PROTEIN CONFORMATION; SPECIES SPECIFICITY; THERMODYNAMICS;

ASPERGILLUS FUMIGATUS; ASPERGILLUS NIGER; SUIDAE;

EID: 34248192717     PISSN: 00992240     EISSN: None     Source Type: Journal    
DOI: 10.1128/AEM.02970-06     Document Type: Article

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