Synthesis and characterization of Ogataea thermomethanolica alcohol oxidase immobilized on barium ferrite magnetic microparticles
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Author list: Mangkorn N., Kanokratana P., Roongsawang N., Laobuthee A., Laosiripojana N., Champreda V.
Publisher: Elsevier
Publication year: 2019
Journal: Journal of Bioscience and Bioengineering (1389-1723)
Volume number: 127
Issue number: 3
Start page: 265
End page: 272
Number of pages: 8
ISSN: 1389-1723
Languages: English-Great Britain (EN-GB)
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Abstract
Alcohol oxidase catalyzes the oxidation of primary alcohols into the corresponding aldehydes, making it a potential biocatalyst in the chemical industry. However, the high production cost and poor operational stability of this enzyme are limitations for industrial application. Immobilization of enzyme onto solid supports is a useful strategy for improving enzyme stability. In this work, alcohol oxidase from the thermotolerant methylotrophic yeast Ogataea thermomethanolica (OthAOX) was covalently immobilized onto barium ferrite (BaFe 12 O 19 ) magnetic microparticles. Among different conditions tested, the highest immobilization efficiency of 71.0 % and catalytic activity of 34.6 U/g was obtained. Immobilization of OthAOX onto magnetic support was shown by Fourier-Transformed infrared microscopy, scanning electron microscopy and X-ray diffraction. The immobilized OthAOX worked optimally at 55 ฐC and pH 8.0. Immobilization also improved thermostability, in which >65% of the initial immobilized enzyme activity was retained after 24 h pre-incubation at 45 ฐC. The immobilized enzyme showed a greater catalytic efficiency for oxidation of methanol and ethanol than free enzyme. The immobilized enzyme could be recovered by magnetization and recycled for at least three consecutive batches, after which 70% activity remained. The properties of the immobilized enzyme suggest its potential industrial application for synthesis of aldehyde. ฉ 2018 The Society for Biotechnology, Japan
Keywords
Aldehyde synthesis, Magnetic microparticles
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