Journal
FOOD CHEMISTRY
Volume 100, Issue 4, Pages 1303-1311Publisher
ELSEVIER SCI LTD
DOI: 10.1016/j.foodchem.2005.12.010
Keywords
lipase; cocoa butter analog; lard; interesterification reaction; supercritical carbon dioxide
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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-CO2) system. Among oil sources used to interact with tristearin, the content of 1(3)-palmitoyl-3(1)-stearoyl-2-monoolein (POS) (P, palmitate; 0, 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 degrees C, pH 9, for 3 It 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 degrees C, respectively, when the analog was produced under optimal conditions. (c) 2005 Elsevier Ltd. All rights reserved.
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