Glycolaldehyde Production from Ethylene Glycol with Immobilized Alcohol Oxidase and Catalase

Article abstract of DOI:10.1271/bbb.62.1589

An enzymatic method for glycolaldehyde production from ethylene glycol was investigated using immobilized alcohol oxidase and catalase. Those enzymes were immobilized onto Chitopearl BCW 3501. When only alcohol oxidase was immobilized onto it, the apparent activity was 190 units/g in wet gel using methanol as the substrate. Tris-HCl buffer (1.5 M; pH 9.0) was selected based on a high stability of glycolaldehyde and a low production of glyoxal as a by-product. Under the optimum conditions, 0.97 M glycolaldehyde was formed from 1.0 M ethylene glycol and the ratio of glyoxal to glycolaldehyde was less than 1%.

Full text of DOI:10.1271/bbb.62.1589

Bioscience, Biotechnology, and Biochemistry
ISSN: 0916-8451 (Print) 1347-6947 (Online) Journal homepage: http://www.tandfonline.com/loi/tbbb20
Glycolaldehyde Production from Ethylene Glycol
with Immobilized Alcohol Oxidase and Catalase
Hiroyuki UKEDA, Tohru ISHII, Masayoshi SAWAMURA & Kimiyasu ISOBE
To cite this article: Hiroyuki UKEDA, Tohru ISHII, Masayoshi SAWAMURA & Kimiyasu ISOBE
(1998) Glycolaldehyde Production from Ethylene Glycol with Immobilized Alcohol Oxidase
and Catalase, Bioscience, Biotechnology, and Biochemistry, 62:8, 1589-1591, DOI: 10.1271/
bbb.62.1589
To link to this article: http://dx.doi.org/10.1271/bbb.62.1589
Published online: 22 May 2014.
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Date: 15 June 2016, At: 08:12