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Immobilization of Lipases on Amberlite and Their Interesterification Reaction Characteristics

Amberlite에 고정화된 Lipase 제조 및 효소적 Interesterification을 이용한 반응 특성 연구

  • Park, So Ra (Department of Food Science and Technology, Chungnam National University) ;
  • Lee, Ki Teak (Department of Food Science and Technology, Chungnam National University)
  • Received : 2013.08.08
  • Accepted : 2014.02.23
  • Published : 2014.06.30

Abstract

Immobilized lipases were prepared by physical adsorption using lipase AK, AY, AH, PS and R on Amberlite$^{(R)}$XAD$^{(R)}$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.

Keywords

immobilized lipase;adsorption;support;continuous reactor;enzymatic interesterification

Acknowledgement

Supported by : 한국원자력연구원

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