Lipase-catalyzed incorporation of conjugated linoleic acid into tricaprylin |
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| Authors: | In-Hwan Kim Chil-Surk Yoon Soo-Hee Cho Kwang-Won Lee Soo-Hyun Chung Beom-Seok Tae |
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| 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 |
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| 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. |
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| Keywords: | Acyl migration conjugated linoleic acid immobilized lipase interesterification tricaprylin |
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