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Enzymatic Esterification of Diols in Reverse Micellar Media
Author(s) -
Yang ChingLun,
Gulari Erdogan
Publication year - 1994
Publication title -
biotechnology progress
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 129
eISSN - 1520-6033
pISSN - 8756-7938
DOI - 10.1021/bp00027a006
Subject(s) - candida rugosa , lauric acid , lipase , chemistry , substrate (aquarium) , hydrolysis , catalysis , micelle , chromatography , reaction rate , enzyme catalysis , organic chemistry , enzyme , fatty acid , oceanography , aqueous solution , geology
With the help of highly dynamic reverse micellar media, lipase‐catalyzed esterification reactions can be carried out at ambient conditions without any agitation. Having low water contents in reverse micellar media, these reversible reactions favor the esterification direction instead of the normal hydrolysis catalyzed by lipases. A proposed enzyme kinetic model has successfully predicted the reaction mechanism of lauric acid with 1,3‐propanediol in reverse micellar media. However, experiments conducted showed a likelihood of substrate inhibition at higher lauric acid concentrations (>70 mM) and a strong bonding effect among 1,3‐propanediol, water, and AOT head groups. The effect of water concentration in the reaction media was shown to be important. The optimal W o 's for achieving the greatest initial reaction rate and final conversion were 9 and 4 for Candida rugosa and Rhizopus delemar , respectively. For both lipases, reverse micellar media experiments showed a lipase localization possibility.