Comparative fatty acid selectivity of lipases in esterification reactions with glycerol and diol analogues in organic media.
Reaction selectivity of Pseudomonas cepacia, Rhizomucor miehei, and Candida antarctica B lipases was assessed in multicompetitive esterification reaction mixtures containing an homologous series of n-chain even carbon number fatty acid (FA; C4-C18) substrates and a single alcohol cosubstrate (glycerol, 1,2-propanediol (1,2-PD), or 1, 3-propanediol (1,3-PD)) in tert-butyl methyl ether at water activity of 0.69 or 0.90 and a reaction temperature of 35 degrees C. For P. cepacia lipase, the ordinal patterns of FA selectivities observed were, with glycerol, C8 > C10, C6, C16 > other FA; with 1,2-PD and 1, 3-PD, C16 > C8 > C14 > other FA. For R. miehei lipase, the ordinal patterns of FA selectivities observed were, with glycerol, C8 > C12 > C10, C14 > other FA; with 1,2-PD and 1,3-PD, C8 > C12 > other FA. For C. antarctica B lipase, the ordinal patterns of FA selectivities observed were, with glycerol, C8 > C10, C6, C12 > other FA; with 1, 2-PD, C8 > C10, C6 > other FA; and with 1,3-PD, C8 > C10 > C6 > other FA. The differences in selectivity among FA ranged up to 16-fold, depending upon the lipase and alcohol cosubstrate used. These findings represent intrinsic and substrate-modulated features of FA selectivities that are of particular relevance to the use of lipases for acylglycerol synthesis reactions.
Lee
C H
CH
Department of Food Science, University of Wisconsin, 1605 Linden Drive, Madison, Wisconsin 53706, USA.
Parkin
K L
KL
D016956:Burkholderia cepacia / Q000201:enzymology; D002175:Candida / Q000201:enzymology; D004951:Esterification; D005227:Fatty Acids / Q000378:metabolism*; D005990:Glycerol / Q000737:chemistry / Q000378:metabolism*; D007700:Kinetics; D008049:Lipase / Q000378:metabolism*; D009930:Organic Chemicals; D020103:Rhizomucor / Q000201:enzymology; D013379:Substrate Specificity
D005227:Fatty Acids; D009930:Organic Chemicals; D008049:Lipase; D005990:Glycerol