Proceedings of the Korean Society for Applied Microbiology Conference (한국미생물생명공학회:학술대회논문집)
- 2000.04a
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- Pages.68-75
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- 2000
Enzymatic Production of D-Tagatose, a Sugar-substituting Sweetener, from D-Galactose
- Noh, Hoe-Jin (Basic Res. Team, R&D Center, Tongyang Confectionery Co.) ;
- Kim, Pil (Basic Res. Team, R&D Center, Tongyang Confectionery Co.)
- Published : 2000.04.01
Abstract
D-Tagatose is a potential bulking agent in food as a non-calorific sweetener. To produce D-tagatose from cheaper resources, plasmids harboring the L-arabinose isomerase gene (araA) from Escherichia coli was constructed because L-arabinose isomerase was previously suggested as an enzyme that mediates the bioconversion of galactose to tagatose as well as that of arabinose to ribulose. In the cultures of recombinant E.coli with pTC101, which harboring araA of E.coli, tagatose was produced from galactose in 9.9 % yield. The enzyme extract of E.coli containing pTC101 also converted galactose into tagatose in 96.4 % yield. For the economic production of D-tagatose, an L-arabinose isomerase of E.coli was immobilized using covalent binding on agarose. While the free L-arabinose isomerase produced tagatose with the rate of 0.48 mg/U
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