Comparative analysis of tagatose productivity of immobilized L-arabinose isomerase expressed in Escherichia coli and Bacillus subtilis
2008
Cheon, J.A. (Catholic University of Korea, Bucheon, Republic of Korea) | Kim, S.B. (CJ Foods RnD, CJ Corp., Seoul, Republic of Korea) | Park, S.W. (CJ Foods RnD, CJ Corp., Seoul, Republic of Korea) | Han, J.K. (CJ Foods RnD, CJ Corp., Seoul, Republic of Korea) | Kim, P. (Catholic University of Korea, Bucheon, Republic of Korea), E-mail: kimp@catholic.ac.kr
Although arabinose isomerase (E.C. 5.3.1.4), a commercial enzyme for edible tagatose bioconversion, call be expressed in ail Escherichia coli system, this expression system inight leave noxious by-products in food. To develop ail eligible tagatose bioconversion with food-safe system, we compared the tagatose production activity of immobilized arabinose isomerase expressed in Bacillus subtilis (a host generally recognized as safe) with that of the enzyme expressed in E. coli. A 48% increase in tagatose production (4.3 g tagatose/L at 69.4 mg/Lㆍhr) was found using the B. subtilis-expressed immobilized enzyme system, compared to the E. coli-expressed enzyme system (2.9 g tagatose/L). The increased productivity with safety of the B. subtilis-expressed arabinose isomerase suggests that it is a more eligible candidate for commercial tagatose production.
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