How do lipases and esterases work: The electrostatic contribution

Journal of Biotechnology

Volumn 85, Issue 2, 2001, Pages 115-147

  Neves Petersen, Maria Teresa ^a   Fojan, Peter ^a   Petersen, Steffen B ^a  

^a AALBORG UNIVERSITY   (Denmark)

Author keywords

Electrostatic catapult; pH dependent electrostatics; pH activity profile; Phospholipase; Product release; Triglyceride lipase

Indexed keywords

ELECTROCHEMISTRY; ELECTROSTATICS; PH EFFECTS; PHOSPHOLIPIDS;

ESTERASES; LIPASES;

ENZYME KINETICS;

ESTER; ESTERASE; PHOSPHATIDYLCHOLINE; PHOSPHATIDYLETHANOLAMINE; PHOSPHATIDYLSERINE; PHOSPHOLIPASE; PHOSPHOLIPID; TRIACYLGLYCEROL; TRIACYLGLYCEROL LIPASE;

ALKALINITY; ARTICLE; BACTERIUM; CHEMICAL BOND; CONFORMATION; CONTROLLED STUDY; ELECTRIC POTENTIAL; ELECTRICITY; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME STRUCTURE; ENZYME SUBSTRATE; GUINEA PIG; HUMAN; LIPOLYSIS; NONHUMAN; PH; PRIORITY JOURNAL; SPECIES DIFFERENCE; TITRIMETRY;

AMINO ACID SEQUENCE; ANIMALS; BIOTECHNOLOGY; CATALYTIC DOMAIN; ELECTROSTATICS; ESTERASES; HUMANS; HYDROGEN-ION CONCENTRATION; LIPASE; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN CONFORMATION;

CAVIA PORCELLUS; SUS SCROFA;

EID: 0035852885     PISSN: 01681656     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0168-1656(00)00360-6     Document Type: Article

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