Carlos M. Verdasco-Martína, Eduardo Garcia-Verdugob, Raul Porcarb,
Roberto Fernandez-Lafuentea, Cristina Oteroa,⁎
a Department of Biocatalysis, Institute of Catalysis and Petroleochemistry, CSIC, C/ Marie Curie 2 L10, Madrid 28049, Spain
b Department of Inorganic and Organic Chemistry, University Jaume I, Avda. Sos Baynat s/n, 12071 Castellón, Spain
Lipases B from Candida antarctica (CALB), Rhizomucor miehei (RML) and Thermomyces lanuginosus (TLL) were immobilized on octadecyl methacylate (OM) or octadecyl methacrylate (OMC) beads. Their specific activity and regioselectivity were studied in the synthesis of conjugated linoleic acid (CLA) partial glycerides, which presented nutraceutical properties.
TLL derivatives were poor catalysts. Novozym® 435 was much better than Lipozyme® RM IM. RML activity (a GRAS enzyme) was modulated via immobilization. After only 3 h, OM−RML gave the highest CLA conversion (54% at 40 °C with 1:3M ratio of glycerol to CLA). OM-RML reduced by a factor of 3.12 and 1.16 the activation energy of the reaction with Lipozyme® RM IM and Novozym® 435, respectively. The new GRAS preparation OM-RML brings forth an optimal regioselective preparation of sn-1 mono and sn-1,3 diacylglycerols rich in CLA, with a ratio of sn-1,3/sn-1,2 regioisomers of 21.8, compared to 2.3 for Novozym®435.
