Glycolaldehyde production from ethylene glycol with immobilized alcohol oxidase and catalase

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 m...

Full description

Saved in:
Bibliographic Details
Published in:Bioscience, biotechnology, and biochemistry biotechnology, and biochemistry, 1998, Vol.62 (8), p.1589-1591
Main Authors: Ukeda, H. (Kochi Univ., Nankoku (Japan). Faculty of Agriculture), Ishii, T, Sawamura, M, Isobe, K
Format: Article
Language:English
Subjects:
alcohol oxidase
ALDEHIDOS
ALDEHYDE
ALDEHYDES
Bioconversions. Hemisynthesis
Biological and medical sciences
Biotechnology
CATALASA
CATALASE
ENZIMAS INMOVILIZADAS
ENZYME IMMOBILISEE
ETHYLENE GLYCOL
ETHYLENEGLYCOL
ETILENOGLICOL
Fundamental and applied biological sciences. Psychology
glycolaldehyde
immobilized enzyme
IMMOBILIZED ENZYMES
Methods. Procedures. Technologies
OXIDOREDUCTASES
OXIDORREDUCTASAS
OXYDOREDUCTASE
Citations: Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary: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%
ISSN:0916-8451
1347-6947
DOI:10.1271/bbb.62.1589