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Immobilization of α-amylase from Exiguobacterium sp. DAU5 on Chitosan and Chitosan-carbon Bead: Its Properties
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 Title & Authors
Immobilization of α-amylase from Exiguobacterium sp. DAU5 on Chitosan and Chitosan-carbon Bead: Its Properties
Fang, Shujun; Chang, Jie; Lee, Yong-Suk; Hwang, Eun-Jung; Heo, Jae Bok; Choi, Yong-Lark;
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 Abstract
Glutaraldehyde was used as a cross-linking agent for immobilization of purified -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 -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 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 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 -amylase possessed high hydrolyzing activity. These results indicate that chitosan is good support and has broad application prospects of enzyme immobilization.
 Keywords
-amylase;chitosan bead;chitosan-carbon bead;
 Language
English
 Cited by
1.
Chitosan hydrogel microspheres: an effective covalent matrix for crosslinking of soluble dextranase to increase stability and recycling efficiency, Bioprocess and Biosystems Engineering, 2017, 40, 3, 451  crossref(new windwow)
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