Lipase-catalyzed ethanolysis of fish oils: multi-response kinetics
Related Experiment Video
Updated: Sep 25, 2026

Defining Substrate Specificities for Lipase and Phospholipase Candidates
Published on: November 23, 2016
Carlos F Torres1, Marlina Moeljadi, Charles G Hill
1Department of Chemical Engineering, University of Wisconsin-Madison, 1415 Engineering Drive, Madison, Wisconsin 53706, USA.
Abstract:
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.
More Related Videos
Related Concept Videos
Carboxylic Acids to Esters: Acid-Catalyzed (Fischer) Esterification Overview
Carboxylic Acids to Esters: Acid-Catalyzed (Fischer) Esterification Mechanism
Enzyme Kinetics
Scientists typically study enzyme kinetics with a fixed amount of enzyme in the controlled environment of a test tube. When more reactant, or substrate, is...
Esters to Carboxylic Acids: Acid-Catalyzed Hydrolysis
During hydrolysis, the ester is first activated towards nucleophilic attack through the protonation of the carboxyl oxygen atom by the acid catalyst. The protonation makes the ester carbonyl carbon more electrophilic. In the next step, water acts as a nucleophile and adds to the...
Biofuels

