ENZYMATIC PRODUCTION OF GLYOXAL FROM ETHYLENE-GLYCOL USING ALCOHOL OXIDASE FROM METHANOL YEAST

被引:28
作者
ISOBE, K [1 ]
NISHISE, H [1 ]
机构
[1] KOSHIEN UNIV, COLL NUTR, TAKARAZUKA, HYOGO 665, JAPAN
关键词
D O I
10.1271/bbb.58.170
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
A new oxidative reaction of ethylene glycol was found with two alcohol oxidases from methanol yeast, Candida sp. and Pichia pastoris. Both alcohol oxidases oxidized ethylene glycol to glyoxal via glycolaldehyde. The optimum pHs for the oxidation of ethylene glycol and glycolaldehyde by the Candida alcohol oxidase were around 8.5 and 5.5, respectively, and their apparent K(m)s were 2.96 M and 28.6 mM, respectively. The optimum temperature was 40 degrees C at pH 7.0. The optimum pHs for the oxidation of ethylene glycol and glycolaldehyde by the Pichia alcohol oxidase were around 8.0 and 6.0, respectively, and their optimum temperatures were 50 and 45 degrees C, respectively, at pH 7.0. The apparent K-m for glycolaldehyde was found to be 83.3 mM. For the accumulation of glyoxal, addition of catalase was effective, and a higher amount of glyoxal was obtained at a much lower temperature than the optimum for the alcohol oxidase. When 0.1M ethylene glycol and glycolaldehyde were incubated with 80 units of the Pichia enzyme at 10 degrees C, both substrates were almost completely converted to glyoxal after 10 and 3h of incubation, respectively.
引用
收藏
页码:170 / 173
页数:4
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