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KMID : 0380620140460030315
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Korean Journal of Food Science and Technology
2014 Volume.46 No. 3 p.315 ~ p.322
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Immobilization of Lipases on Amberlite and Their Interesterification Reaction Characteristics
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Park So-Ra
Lee Ki-Teak
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Abstract
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Immobilized lipases were prepared by physical adsorption using lipase AK, AY, AH, PS and R on Amberlite®XAD®7 HP resin. With the immobilized lipases (10%), structured lipid was synthesized by enzymatic interesterification of canola oil, palmitic ethyl ester, and stearic ethyl ester in order to study the reaction characteristics. Among the lipase, the highest protein content was obtained from lipase AH (11.41%) before immobilization, while the highest levels of bound protein was observed from immobilized lipase AK (63.91%). Immobilized lipase AK had the highest interesterification activity (38.3% of total saturated fatty acid). Lipase AK was also used for a continuous reaction in which the slow flow of reactant resulted in increased reaction rate. Reusability of immobilized AK, AH and PS increased at the second reaction (120-196.5%). However, the activity of immobilized AK, which had the highest bound protein content (63.91%) decreased after the third reaction, while the activity of immobilized AH and PS was maintained until the sixth reaction.
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KEYWORD
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immobilized lipase, adsorption, support, continuous reactor, enzymatic interesterification
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