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1‐Monoglyceride production from lipase‐catalyzed esterification of glycerol and fatty acid in reverse micelles
Author(s) -
Hayes Douglas G.,
Gulari Erdogan
Publication year - 1991
Publication title -
biotechnology and bioengineering
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.136
H-Index - 189
eISSN - 1097-0290
pISSN - 0006-3592
DOI - 10.1002/bit.260380509
Subject(s) - monoglyceride , glycerol , lipase , chemistry , micelle , fatty acid , candida antarctica , catalysis , glyceride , pulmonary surfactant , diglyceride , product inhibition , organic chemistry , chromatography , enzyme , biochemistry , aqueous solution , non competitive inhibition
Glycerol‐fatty acid esterification has been conducted with lipase from R. delemar in water/AOT/isooctane reverse micellar media, with the major product being 1‐monoglyceride, a useful food‐emulsifier. 1,3‐diglyceride was also synthesized, but to a much lesser extent. For a given set of initial conditions, the reaction productivity, measured in terms of the initial product formation rate, V 0 , and the final or equilibrium concentration of product, is optimal for a particular concentration of each surfactant, fatty acid, glycerol, and water. Many of these optimal values correlate well with a “critical” region on the phase diagram. Also, results indicate lipase‐catalyzed esterification stops due to the achievement of kinetic equilibrium expect for a few cases where enzyme deactivation is severe. Dynamic light scattering was employed to examine the influence of water, glycerol, and fatty acid on micellar and interfacial structure. Results from this technique indicate enzyme kinetic are linked to interfacial phenomena and the presence of substrates at the interfacial region.