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Characterization of ribose-5-phosphate isomerase of Clostridium thermocellum producing D-allose from D-psicose
- Authors
- Park, Chang-Su; Yeom, Soo-Jin; Kim, Hye-Jung; Lee, Sook-Hee; Lee, Jung-Kul; Kim, Seon-Won; Oh, Deok-Kun
- Issue Date
- Sep-2007
- Publisher
- Kluwer Academic Publishers
- Keywords
- D-allose; Clostridium thermocellum; isomerization; D-psicose; ribose-5-phospate isomerase
- Citation
- Biotechnology Letters, v.29, no.9, pp 1387 - 1391
- Pages
- 5
- Indexed
- SCIE
SCOPUS
- Journal Title
- Biotechnology Letters
- Volume
- 29
- Number
- 9
- Start Page
- 1387
- End Page
- 1391
- ISSN
- 0141-5492
1573-6776
- Abstract
- 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.
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