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Volumn 87, Issue 3, 2001, Pages 225-254
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Engineering the pH-optimum of a triglyceride lipase: From predictions based on electrostatic computations to experimental results
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Author keywords
Electrostatic interactions; Electrostatic potential; Engineering pH optimum; Lipase esterase pH activity profile; pH optimum shift
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Indexed keywords
CALCULATIONS;
ENZYMES;
PH;
TITRATION;
ELECTROSTATIC COMPUTATIONS;
BIOTECHNOLOGY;
ALANINE;
ALKALINE EARTH METAL;
CUTINASE;
ESTER;
ESTERASE;
GLUTAMINE;
LYSINE;
PROLINE;
THREONINE;
TRIACYLGLYCEROL LIPASE;
ARTICLE;
ELECTRIC POTENTIAL;
ELECTRICITY;
ENERGY;
ENZYME ACTIVE SITE;
ENZYME ACTIVITY;
FUSARIUM SOLANI;
GENE MUTATION;
GENETIC ENGINEERING;
MELTING POINT;
PH MEASUREMENT;
PRIORITY JOURNAL;
TEMPERATURE DEPENDENCE;
TITRIMETRY;
AMINO ACID SEQUENCE;
AMINO ACID SUBSTITUTION;
BASE SEQUENCE;
CARBOXYLIC ESTER HYDROLASES;
CIRCULAR DICHROISM;
COMPUTER SIMULATION;
ELECTROSTATICS;
ENZYME STABILITY;
FUSARIUM;
HYDROGEN-ION CONCENTRATION;
LIPASE;
MODELS, CHEMICAL;
MODELS, MOLECULAR;
MOLECULAR SEQUENCE DATA;
MUTAGENESIS, SITE-DIRECTED;
PROTEIN CONFORMATION;
PROTEIN ENGINEERING;
RECOMBINANT PROTEINS;
SEQUENCE HOMOLOGY, AMINO ACID;
FUSARIUM;
FUSARIUM SOLANI;
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EID: 0035907145
PISSN: 01681656
EISSN: None
Source Type: Journal
DOI: 10.1016/S0168-1656(01)00240-1 Document Type: Article |
Times cited : (27)
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References (97)
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