Lipase-catalyzed ethanolysis of fish oils: multi-response kinetics.
The kinetics of the lipase-catalyzed (Pseudomonas cepacia) ethanolysis of fish oil has been studied in a batch reactor using menhaden oil, tuna oil, and acylglycerol mixtures derived from menhaden oil. Multi-response models derived from a generalized Michaelis-Menten mechanism were developed to describe the rates of formation of ethyl esters of the primary fatty acids present in the precursor oil. A first-order model for deactivation of the lipase was fit simultaneously to one of the data sets.
Torres
Carlos F
CF
Department of Chemical Engineering, University of Wisconsin-Madison, 1415 Engineering Drive, Madison, Wisconsin 53706, USA.
Moeljadi
Marlina
M
Hill
Charles G
CG
D000818:Animals; D016956:Burkholderia cepacia / Q000737:chemistry / Q000201:enzymology; D003198:Computer Simulation; D004281:Docosahexaenoic Acids / Q000138:chemical synthesis*; D015118:Eicosapentaenoic Acid / Q000138:chemical synthesis*; D004789:Enzyme Activation; D004795:Enzyme Stability; D004951:Esterification; D000431:Ethanol / Q000737:chemistry*; D005231:Fatty Acids, Unsaturated / Q000138:chemical synthesis; D005395:Fish Oils / Q000737:chemistry*; D007700:Kinetics; D008049:Lipase / Q000737:chemistry*; D008956:Models, Chemical; D014413:Tuna / Q000378:metabolism
D005231:Fatty Acids, Unsaturated; D005395:Fish Oils; C033266:Menhaden oil; D004281:Docosahexaenoic Acids; D000431:Ethanol; D015118:Eicosapentaenoic Acid; D008049:Lipase