Journal of Applied Biological Chemistry

The Korean Society for Applied Biological Chemistry (한국응용생명화학회)
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Immobilization of α-amylase from Exiguobacterium sp. DAU5 on Chitosan and Chitosan-carbon Bead: Its Properties

  • Fang, Shujun (Department of Biotechnology, Dong-A University) ;
  • Chang, Jie (Department of Biotechnology, Dong-A University) ;
  • Lee, Yong-Suk (Department of Biotechnology, Dong-A University) ;
  • Hwang, Eun-Jung (Department of Biotechnology, Dong-A University) ;
  • Heo, Jae Bok (Department of Molecular Biotechnology, Dong-A University) ;
  • Choi, Yong-Lark (Department of Biotechnology, Dong-A University)
  • Received : 2015.11.25
  • Accepted : 2016.01.15
  • Published : 2016.03.31
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Abstract

Glutaraldehyde was used as a cross-linking agent for immobilization of purified ${\alpha}$-amylase from Exiguobacterium sp. DAU5. Befitting concentration of glutaradehyde and cross-linking time is the key to preparation of cross-linking chitosan beads. Based on optimized immobilization condition for ${\alpha}$-amylase, an overall yield of 56% with specific activity of 2,240 U/g on chitosan beads and 58% with specific activity of 2,320 U/g on chitosan-carbon beads was obtained. The optimal temperature and pH of each immobilized enzyme activity were $50^{\circ}C$ and 50 mM glycine-NaOH buffer pH 8.5, respectively. Those retained more than 75 and 90% of its maximal enzyme activity at pH 7.0-9.5 and after incubation at $50^{\circ}C$ for 1 h, respectively. In addition, the immobilization product showed higher organic-solvent tolerance than free enzymes. The mode of hydrolyzing soluble starch revealed that the ${\alpha}$-amylase possessed high hydrolyzing activity. These results indicate that chitosan is good support and has broad application prospects of enzyme immobilization.

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References

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