Journal
FOOD SCIENCE AND BIOTECHNOLOGY
Volume -, Issue -, Pages -Publisher
KOREAN SOCIETY FOOD SCIENCE & TECHNOLOGY-KOSFOST
DOI: 10.1007/s10068-023-01337-7
Keywords
Candida antarctica Lipase B; Lipozyme 435; Sn-1; 3 specificity; Immobilization; Interesterification
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This study aimed to investigate the regiospecificity of immobilized CALB in the solvent-free interesterification of triacylglycerol with fatty acid ethyl esters. The results showed that immobilized CALB exhibited distinct sn-1,3 regiospecificity.
Candida antarctica lipase B (CALB) is regarded as non-regiospecific. This study aimed to investigate the regiospecificity of CALB in the solvent-free interesterification of high-oleic sunflower oil with stearic acid ethyl ester for 1,3-distearoyl-2-oleoylglycerol (SOS)-rich fat preparation using a packed bed reactor. The content ratio of 1,2-distearoyl-3-oleoylglycerol (SSO) to SOS (denoted by SSO/SOS content) obtained using Lipozyme 435 (a commercially immobilized CALB; 0-4.1%), at residence times (1-32 min) was similar to that obtained using Lipozyme RM IM (0-3.0%), but lower than that obtained using Lipozyme TL IM (6.0-39.4%). When immobilized on Lewatit VP OC 1600, Lipozyme CALB had an SSO/SOS content of 0-10.4%, which was greater than that of Palatase 20,000 L (0-1.1%) but was lower than that of Lipozyme TL 100 L (8.8-97.7%). Our findings suggest that immobilized CALB shows distinct sn-1,3 regiospecificity in the interesterification of triacylglycerol with fatty acid ethyl esters.
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