Computational design-based molecular engineering of the glycosyl hydrolase family i I B. subtilis XynA endoxylanase improves its acid stability

Protein Engineering, Design and Selection

Volumn 22, Issue 10, 2009, Pages 587-596

  Beliën, Tim ^a,b   Joye, Iris J ^a   Delcour, Jan A ^a   Courtin, Christophe M ^a  

^a LEUVEN FOOD SCIENCE AND NUTRITION RESEARCH CENTRE LFORCE   (Belgium)

^b PCFruit Vzw ^*  (Belgium)

Author keywords

4 xylanase; Endo 1; In silico protein design; Mutagenesis; PH stability

Indexed keywords

ACID STABILITY; ACIDIC CONDITIONS; AMINO ACID RESIDUES; BACILLUS SUBTILIS; CATALYTIC ACTIVITY; COMPUTATIONAL DESIGN; COMPUTATIONAL PREDICTIONS; ENDOXYLANASE; EXPERIMENTAL CONDITIONS; GLYCOSYL HYDROLASES; IN-SILICO; IONISATION; MOLECULAR ENGINEERING; MOLECULAR MECHANISM; MOLECULAR MODELLING; PH DEPENDENCE; PH LEVELS; PH-DEPENDENT; PH-STABILITY; POINT MUTATIONS; PROTEIN ENGINEERING; PROTEIN STABILITY; SIDE CHAINS; STRENGTH CONDITION; SUBTILIS; WILD-TYPE ENZYMES; XYLANASES;

AMINO ACIDS; BACTERIOLOGY; BIOCHEMICAL ENGINEERING; CATALYST ACTIVITY; CYTOLOGY; DESIGN; ELECTROCHEMICAL SENSORS; ESCHERICHIA COLI; GENETIC ENGINEERING; IONIC STRENGTH; MUTAGENESIS; PROTEINS;

STABILITY;

AMINO ACID; ENDO 1,4 BETA XYLANASE; GLYCOSIDASE; HISTIDINE; PROTEIN; UNCLASSIFIED DRUG; XYNA PROTEIN;

AMINO ACID METABOLISM; ARTICLE; BACILLUS SUBTILIS; CYTOPLASM; ENZYME ACTIVITY; ESCHERICHIA COLI; GENETIC ENGINEERING AND GENE TECHNOLOGY; INCUBATION TIME; MOLECULAR MECHANICS; NONHUMAN; NUCLEOTIDE SEQUENCE; PH; POINT MUTATION; PRIORITY JOURNAL; PROTEIN ENGINEERING; PROTEIN STABILITY; WILD TYPE;

BACILLUS SUBTILIS; BACTERIAL PROTEINS; COMPUTER SIMULATION; ELECTROPHORESIS, POLYACRYLAMIDE GEL; ENDO-1,4-BETA XYLANASES; ENZYME STABILITY; ESCHERICHIA COLI; HYDROGEN-ION CONCENTRATION; KINETICS; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; OSMOLAR CONCENTRATION; PROTEIN ENGINEERING; RECOMBINANT PROTEINS; TEMPERATURE;

BACILLUS SUBTILIS; ESCHERICHIA COLI;

EID: 76849098696     PISSN: 17410126     EISSN: 17410134     Source Type: Journal    
DOI: 10.1093/protein/gzp024     Document Type: Article

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