Bioscience, Biotechnology and Biochemistry p. 1589 - 1591 (1998)
Update date:2022-07-29
Topics: Catalase Experimental Production Immobilized Ethylene Glycol
Ukeda, Hiroyuki
Ishii, Tohru
Sawamura, Masayoshi
Isobe, Kimiyasu
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%.
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