The temperature dependence of enzymatic kinetic resolutions reveals the relative contribution of enthalpy and entropy to enzymatic enantioselectivity

Biocatalysis and Biotransformation

Volumn 17, Issue 1, 1999, Pages 61-79

  Overbeeke, P L Antoine ^a   Ottosson, Jenny ^b   Hult, Karl ^b   Jongejan, Jaap A ^a   Duine, Johannis A ^a  

^a DELFT UNIVERSITY OF TECHNOLOGY   (Netherlands)

^b ROYAL INSTITUTE OF TECHNOLOGY   (Sweden)

Author keywords

Enantioselectivity; Enthalpy entropy compensation; Enzymes; Kinetic resolution; Organic media; Temperature dependence

Indexed keywords

ACTIVATION ENERGY; ACYLATION; ALCOHOLS; CATALYSIS; CATALYST SELECTIVITY; ENTHALPY; ENTROPY; ESTERS; HYDROLYSIS; ORGANIC SOLVENTS; THERMAL EFFECTS;

ENZYMATIC ENANTIOSELECTIVITY;

ENZYME KINETICS;

ALCOHOL DERIVATIVE; ENZYME; ESTER; SOLVENT; TRIACYLGLYCEROL LIPASE;

ACYLATION; ARTICLE; CATALYSIS; CORRELATION FUNCTION; ENANTIOMER; ENTHALPY; ENTROPY; ENVIRONMENTAL TEMPERATURE; ENZYME ACTIVATION; ENZYME KINETICS; ENZYME SUBSTRATE COMPLEX; HYDROLYSIS; MATHEMATICAL ANALYSIS; TEMPERATURE DEPENDENCE;

EID: 0032894468     PISSN: 10242422     EISSN: None     Source Type: Journal    
DOI: 10.3109/10242429909003207     Document Type: Article

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