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자료유형
학술저널
저자정보
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)
저널정보
한국응용생명화학회 Journal of applied biological chemistry Journal of applied biological chemistry 제59권 제1호
발행연도
2016.1
수록면
75 - 81 (7page)

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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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