Sunday, July 29, 2007
P7
Investigation of galactose 6-phosphate isomerase and ribose 5-phosphate isomerase for production of D-allose from D-psicose
Sook-Hee Lee1, Sang-Hwal Yoon1, Eun-Gyeong Lee1, Hee-Kyoung Ryu1, Chong-Long Wang1, Hee-Jung Jang1, Ji-Seon Park1, Pil Kim2, Deok-Kun Oh3, and Seon-Won Kim1. (1) Division of Applied Life Science, Gyeongsang National University, 900 Gajwadong, Jinju, 660-701, South Korea, (2) College of Humanities and Sciences, The Catholic University, Gyeonggi, 420-743, South Korea, (3) Department of Bioscience and Biotechnology, Konkuk University, Seoul, 143-503, South Korea
D-Psicose and D-allose, a rare keto and aldo-hexose, are not abundant in nature and are difficult to prepare by chemical methods. For the production of D-allose in E. coli, we used galactose 6-phosphate isomerase coding lacAB of Staphylococcus aureus, Lactococcus lactis, and ribose 5-phosphate isomerase coding rpiB of Clostridium thermocellum, Thermotoga maritima, Corynebacterium glutamicum. Through the whole cell reaction using recombinant E. coli harboring lacAB or rpiB, psicose was not converted to allose, but conversion of allose to psicose was observed. The enzymes used here were shown to have the biased isomerization activity from allose to psicose. In the enzyme reaction using ribose 5-phosphate isomerase of C. thermocellum, which had the highest isomerization activity among the tested enzymes, isomerization of allose to psicose was only occurred.
This work was supported by the Basic Research program of the KOSEF (Grant No. R01-2004-000-10012-0) , EB-NCRC (Grant No. R15-2003-012-02001-0) and BK21 program of
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