Kinetics of the lipase-catalyzed synthesis of glucose esters in acetone.
A simple kinetic model derived from a ping-pong bi-bi mechanism is proposed to describe the lipase-catalyzed esterification of glucose with fatty acids. The mathematical expressions derived from this model have been tested using several sets of data obtained from reactions carried out under different reaction conditions. The predicted values provide very good fits of the experimental data for temperatures from 30 to 60 degrees C, enzyme loadings from 90 to 180 mg, and fatty acid concentrations from 0.33M to 1M. Experiments conducted at different temperatures permit one to estimate an activation energy of approximately 12 kcal/mol for the rate-limiting step of the reaction (formation of the acyl-enzyme complex). The model also considers the kinetics of inactivation of the biocatalyst during the reaction.
Instituto de Catalisis y Petroleoquimica, CSIC, Cantoblanco, 28049, Madrid, Spain.
J A
JA
Arcos
C G
CG
Hill
C
C
Otero
D000096:Acetone / Q000737:chemistry; D002384:Catalysis; D004789:Enzyme Activation; D004800:Enzymes, Immobilized; D004951:Esterification; D004952:Esters / Q000138:chemical synthesis*; D005656:Fungal Proteins; D005947:Glucose / Q000737:chemistry*; D007700:Kinetics; D007850:Lauric Acids / Q000737:chemistry; D008049:Lipase / Q000737:chemistry*; D008433:Mathematics; D008956:Models, Chemical; D019308:Palmitic Acid / Q000737:chemistry; D013229:Stearic Acids / Q000737:chemistry; D013696:Temperature
D004800:Enzymes, Immobilized; D004952:Esters; D005656:Fungal Proteins; D007850:Lauric Acids; D013229:Stearic Acids; D000096:Acetone; D019308:Palmitic Acid; C093667:Novozyme 435; D008049:Lipase; D005947:Glucose