Characterization of ribose-5-phosphate isomerase of Clostridium thermocellum producing D-allose from D-psicose

被引：48

作者：

Park, Chang-Su

Yeom, Soo-Jin

Kim, Hye-Jung

Lee, Sook-Hee

Lee, Jung-Kul

Kim, Seon-Won

Oh, Deok-Kun

机构：

[1] Konkuk Univ, Dept Biosci & Biotechnol, Seoul 143701, South Korea

[2] Konkuk Univ, Dept Chem & Biomol Engn, Seoul 143701, South Korea

[3] Gyeongsang Natl Univ, EB NCRC, Div Appl Life Sci, Jinju 660701, South Korea

来源：

BIOTECHNOLOGY LETTERS | 2007年 / 29卷 / 09期

关键词：

D-allose; Clostridium thermocellum; isomerization; D-psicose; ribose-5-phospate isomerase;

D O I：

10.1007/s10529-007-9393-7

中图分类号：

Q81 [生物工程学（生物技术）]; Q93 [微生物学];

学科分类号：

071005 ; 0836 ; 090102 ; 100705 ;

摘要：

The rpiB gene, encoding ribose-5-phosphate isomerase (RpiB) from Clostridium thermocellum, was cloned and expressed in Escherichia coli. RpiB converted D-psicose into D-allose but it did not convert D-xylose, L-rhamnose, D-altrose or D-galactose. The production of D-allose by RpiB was maximal at pH 7.5 and 65 degrees C for 30 min. The half-lives of the enzyme at 50 degrees C and 65 degrees C were 96 h and 4.7 h, respectively. Under stable conditions of pH 7.5 and 50 degrees C, 165 g D-allose l(-1) was produced without by-products from 500 g D-psicose l(-1) after 6 h.

引用

页码：1387 / 1391

页数：5

共 15 条

[1]

Bhuiyan SH, 1997, J FERMENT BIOENG, V84, P319

[2] D-allose production from D-psicose using immobilized L-rhamnose isomerase [J].