Characterization of a thermostable glucose dehydrogenase with strict substrate specificity from a hyperthermophilic archaeon Thermoproteus sp. GDH-1

被引：6

作者：

Aiba, Hiroshi ^{[1
,2
]}

Nishiya, Yoshiaki ^{[3
]}

Azuma, Masayuki ^{[2
]}

Yokooji, Yuusuke ^{[4
]}

Atomi, Haruyuki ^{[4
]}

Imanaka, Tadayuki ^{[5
]}

机构：

[1] TOYOBO CO LTD, Inst Biotechnol, Tsuruga, Fukui, Japan

[2] Osaka City Univ, Grad Sch Engn, Dept Appl Chem & Bioengn, Osaka 558, Japan

[3] Setsunan Univ, Dept Life Sci, Neyagawa, Osaka, Japan

[4] Kyoto Univ, Grad Sch Engn, Dept Synthet Chem & Biol Chem, Kyoto, Japan

[5] Ritsumeikan Univ, Dept Biotechnol, Coll Life Sci, Kusatsu, Japan

来源：

BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY | 2015年 / 79卷 / 07期

关键词：

thermostability; glucose dehydrogenase (GDH); archaea; hyperthermophile; ENTNER-DOUDOROFF PATHWAY; ASPERGILLUS-ORYZAE; COENZYME SPECIFICITY; ESCHERICHIA-COLI; PURIFICATION; METABOLISM; ENZYME;

D O I：

10.1080/09168451.2015.1018120

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 hyperthermophilic archaeon was isolated from a terrestrial hot spring on Kodakara Island, Japan and designated as Thermoproteus sp. glucose dehydrogenase (GDH-1). Cell extracts from cells grown in medium supplemented with glucose exhibited NAD(P)-dependent glucose dehydrogenase activity. The enzyme (TgGDH) was purified and found to display a strict preference for d-glucose. The gene was cloned and expressed in Escherichia coli, resulting in the production of a soluble and active protein. Recombinant TgGDH displayed extremely high thermostability and an optimal temperature higher than 85 degrees C, in addition to its strict specificity for d-glucose. Despite its thermophilic nature, TgGDH still exhibited activity at 25 degrees C. We confirmed that the enzyme could be applied for glucose measurements at ambient temperatures, suggesting a potential of the enzyme for use in measurements in blood samples.

引用

页码：1094 / 1102

页数：9

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