Membrane-bound glycerol dehydrogenase catalyzes oxidation of D-pentonates to 4-keto-D-pentonates, D-fructose to 5-keto-D-fructose, and D-psicose to 5-keto-D-psicose

被引:22
作者
Ano, Yoshitaka [1 ]
Hours, Roque A. [2 ]
Akakabe, Yoshihiko [3 ]
Kataoka, Naoya [3 ]
Yakushi, Toshiharu [3 ]
Matsushita, Kazunobu [3 ]
Adachi, Osao [3 ]
机构
[1] Ehime Univ, Grad Sch Agr, Dept Biosci, Matsuyama, Ehime, Japan
[2] Natl Univ La Plata, Sch Sci, CINDEFI, La Plata, Buenos Aires, Argentina
[3] Yamaguchi Univ, Dept Biol Chem, Fac Agr, Yamaguchi, Japan
基金
日本学术振兴会;
关键词
acetic acid bacteria; glycerol dehydrogenase; 4-keto-D-arabonate production; 4-keto-D-pentonate; oxidative fermentation; D-GLUCONATE DEHYDROGENASE; D-GLUCOSE DEHYDROGENASE; ACETIC-ACID BACTERIA; GLUCONOBACTER-SUBOXYDANS; SORBITOL DEHYDROGENASE; PURIFICATION; FERMENTATION; 2-KETO-D-GLUCONATE; SOLUBILIZATION; INDUSTRIUS;
D O I
10.1080/09168451.2016.1254535
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 novel oxidation of D-pentonates to 4-keto-D-pentonates was analyzed with Gluconobacter thailandicus NBRC 3258. D-Pentonate 4-dehydrogenase activity in the membrane fraction was readily inactivated by EDTA and it was reactivated by the addition of PQQ and Ca2+. D-Pentonate 4-dehydrogenase was purified to two different subunits, 80 and 14 kDa. The absorption spectrum of the purified enzyme showed no typical absorbance over the visible regions. The enzyme oxidized D-pentonates to 4-keto-D-pentonates at the optimum pH of 4.0. In addition, the enzyme oxidized D-fructose to 5-keto-D-fructose, D-psicose to 5-keto-D-psicose, including the other polyols such as, glycerol, D-ribitol, D-arabitol, and D-sorbitol. Thus, D-pentonate 4-dehydrogenase was found to be identical with glycerol dehydrogenase (GLDH), a major polyol dehydrogenase in Gluconobacter species. The reaction versatility of quinoprotein GLDH was notified in this study.
引用
收藏
页码:411 / 418
页数:8
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