Enzymatic synthesis of cocoa butter analog through interesterification of lard and tristearin in supercritical carbon dioxide by lipase

Abstract

Substrate oil composition, reaction time, acyl donor, temperature, and pressure affected the triacylglycerol (TG) content of cocoa butter analog during the interesterification reaction catalyzed by lipase in a supercritical carbon dioxide (SC-CO 2) system. Among oil sources used to interact with tristearin, the content of 1(3)-palmitoyl-3(1)-stearoyl-2-monoolein (POS) (P, palmitate; O, oleate; S, stearate) and 1-palmitoyl-2, 3-dioleoylglycerol (POO) in analog was most similar to the corresponding TG content of cocoa butter when analog was prepared with lard. The optimized interesterification reaction using lard and tristearin (at a mole ratio of 1.4) as substrates to produce cocoa butter analog in a SC-CO 2 system was at 17 MPa, 50 °C, pH 9, for 3 h with an immobilized lipase, Lipozyme IM-20, from Mucor miehei. The lyophilized enzyme facilitated the production of cocoa butter analog in anhydrous substrates ( a w 0.33). The yield and melting point of the purified cocoa butter analog by a silica column was 63% and 34.5 °C, respectively, when the analog was produced under optimal conditions.