Immobilization of yeast alcohol dehydrogenase on magnetic nanoparticles for improving its stability Article DOI:
Cite this article as: Liao, MH. & Chen, DH. Biotechnology Letters (2001) 23: 1723. doi:10.1023/A:1012485221802 Abstract
Yeast alcohol dehydrogenase (YADH) was immobilized covalently on Fe
3O 4 magnetic nanoparticles (10.6 nm) via carbodiimide activation. The immobilization process did not affect the size and structure of magnetic nanoparticles. The YADH-immobilized magnetic nanoparticles were superparamagnetic with a saturation magnetization of 61 emu g −1, only slightly lower than that of the naked ones (63 emu g −1). Compared to the free enzyme, the immobilized YADH retained 62% activity and showed a 10-fold increased stability and a 2.7-fold increased activity at pH 5. For the reduction of 2-butanone by immobilized YADH, the activation energies within 25–45 °C, the maximum specific activity, and the Michaelis constants for NADH and 2-butanone were 27 J mol −1, 0.23 mol min −1 mg −1, 0.62 mM, and 0.43 M, respectively. These results indicated a structural change of YADH with a decrease in affinity for NADH and 2-butanone after immobilization compared to the free enzyme. immobilization magnetic nanoparticles stability yeast alcohol dehydrogenase References
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