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Lipase-catalyzed incorporation of conjugated linoleic acid into tricaprylin
Authors:In-Hwan Kim  Chil-Surk Yoon  Soo-Hee Cho  Kwang-Won Lee  Soo-Hyun Chung  Beom-Seok Tae
Affiliation:(1) Korea Food Research Institute, Sungnam, Korea;(2) Catholic Institute of Medical Science, Catholic University, Seoul, Korea;(3) Department of Chemical Engineering, Hankyong National University, Ansung, Korea;(4) Department of Food and Nutrition, College of Health Sciences, Korea University, Chungneung-Dong, Sungbuk-Gu, 136-703 Seoul, Korea
Abstract:Three commercially available immobilized lipases, Novozym 435 from Candida antarctica, Lipozyme IM from Rhizomucor miehei, and Lipase PS-C from Pseudomonas cepacia, were used as biocatalysts for the interesterification of conjugated linoleic acid (CLA) ethyl ester and tricaprylin. The reactions were carried out in hexane, and the products were analyzed by gas-liquid chromatography. The effects of molar ratio, enzyme load, incubation time, and temperature on CLA incorporation were investigated. Novozym 435, as compared to Lipozyme IM and Lipase PC-C, showed the highest degree of CLA incorporation into tricaprylin. By hydrolysis with pancreatic lipase, it was found that Lipozyme IM and Lipase PS-C exhibited high selectivity for the sn-1,3 position of the triacylglycerol early in the interesterification, with small extents of incorporation of CLA into the sn-2 position, probably due to acyl migration, at later reaction times. A small extent of sn-1,3 selectivity during interesterification by Novozym 435 was observed.
Keywords:Acyl migration  conjugated linoleic acid  immobilized lipase  interesterification  tricaprylin
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