Bulletin of the Korean Chemical Society

Korean Chemical Society (대한화학회)
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Immobilization of Lipase using Alginate Hydrogel Beads and Enzymatic Evaluation in Hydrolysis of p-Nitrophenol Butyrate

  • Zhang, Shuang (Department of Chemistry, Renmin University of China) ;
  • Shang, Wenting (Department of Chemistry, Renmin University of China) ;
  • Yang, Xiaoxi (Department of Chemistry, Renmin University of China) ;
  • Zhang, Shujuan (Department of Chemistry, Renmin University of China) ;
  • Zhang, Xiaogang (Department of Chemistry, Renmin University of China) ;
  • Chen, Jiawei (State Key Laboratory of Geological Processes and Mineral Resources, China University of Geosciences)
  • Received : 2013.04.01
  • Accepted : 2013.06.25
  • Published : 2013.09.20
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Abstract

The immobilization of enzyme is one of the key issues both in the field of enzymatic research and industrialization. In this work, we reported a facile method to immobilize Candida Antarctica lipase B (CALB) in alginate carrier. In the presence of calcium cation, the enzyme-alginate suspension could be cross-linked to form beads with porous structure at room temperature, and the enzyme CALB was dispersed in the beads. Activity of the enzyme-alginate composite was verified by enzymatic hydrolysis reaction of p-nitrophenol butyrate in aqueous phase. The effects of reaction parameters such as temperature, pH, embedding and lyophilized time on the reactive behavior were discussed. Reuse cycle experiments for the hydrolysis of p-nitrophenol butyrate demonstrated that activity of the enzyme-alginate composite was maintained without marked deactivation up to 6 repeated cycles.

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