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Enzymatic esterification of glycerol II. Lipase‐catalyzed synthesis of regioisomerically pure 1(3)‐ rac ‐monoacylglycerols
Author(s) -
Berger Matthias,
Schnelder Manfred P.
Publication year - 1992
Publication title -
journal of the american oil chemists' society
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.512
H-Index - 117
eISSN - 1558-9331
pISSN - 0003-021X
DOI - 10.1007/bf02541058
Subject(s) - rhizomucor miehei , chemistry , glycerol , lipase , monoacylglycerol lipase , organic chemistry , catalysis , solvent , rhizopus oryzae , fatty acid , diethyl ether , immobilized enzyme , triacylglycerol lipase , enzyme , biochemistry , fermentation , endocannabinoid system , receptor
Regioisomerically pure 1(3)‐ rac ‐monoacylglycerols are conveniently prepared in high yields (>75%) and in multigram quantities by enzymatic esterification of glycerol in the presence of various lipases (Chromobacterium viscosum, Rhizopus delemar, Rhizomucor miehei) with a variety of different acyl donors, such as free fatty acids, fatty acid alkyl esters, vinyl esters and triacylglycerols, as well as natural fats and oils. All reactions are carried out in aprotic organic solvents with low water content, namely n ‐hexane, diethyl ether, tBuOMe or mixtures of these solvents. Essential for the success of these transformations were the following two factors. First, the creation of an artificial interphase between the solvent‐immiscible hydrophilic glycerol and the hydrophobic reaction medium by its adsorption onto a solid support. Second, a facile system for the separation of the desired monoacylglycerol from the reaction mixture, coupled with the continuous recycling of acyl donor and undesirable by‐products.