KUAN-MIAO LIU2026-10-162026-10-162007-01-01Pure ID: 15457136Pure UUID: 7f4458c8-97e7-4e11-bc6c-361c28e13c5e10.1016/j.foodchem.2005.12.010https://www.scopus.com/pages/publications/33746524375https://scholars.csmu.edu.tw/handle/123456789/32419Substrate 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-CO2) 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-CO2 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 (aw 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.9enEnzymatic synthesis of cocoa butter analog through interesterification of lard and tristearin in supercritical carbon dioxide by lipasejournal article