한빛사 논문
Jing-Jing Liu1, Guo-Chang Zhang1,2, Suryang Kwak1,2, Eun Joong Oh1,2, Eun Ju Yun1,3, Kulika Chomvong4, Jamie H.D. Cate5 & Yong-Su Jin1,2,*
1 Carl R. Woese Institute for Genomic Biology, University of Illinois at Urbana-Champaign, Urbana, IL 61801, USA. 2 Department of Food Science and Human Nutrition, University of Illinois at Urbana-Champaign, Urbana, IL 61801, USA. 3 Department of Biotechnology, Graduate School, Korea University, Seoul 02841, South Korea. 4 National Center for Genetic Engineering and Biotechnology (BIOTEC), 113 Thailand Science Park, Phahonyothin Road, Pathum Thani 12120, Thailand. 5 Department of Molecular and Cell Biology, University of California, Berkeley, CA 94720, USA.
*Correspondence and requests for materials should be addressed to Y.-S.J.
Abstract
Isomerases perform biotransformations without cofactors but often cause an undesirable mixture of substrate and product due to unfavorable thermodynamic equilibria. We demonstrate the feasibility of using an engineered yeast strain harboring oxidoreductase reactions to overcome the thermodynamic limit of an isomerization reaction. Specifically, a yeast strain capable of consuming lactose intracellularly is engineered to produce tagatose from lactose through three layers of manipulations. First, GAL1 coding for galactose kinase is deleted to eliminate galactose utilization. Second, heterologous xylose reductase (XR) and galactitol dehydrogenase (GDH) are introduced into the ∆gal1 strain. Third, the expression levels of XR and GDH are adjusted to maximize tagatose production. The resulting engineered yeast produces 37.69 g/L of tagatose from lactose with a tagatose and galactose ratio of 9:1 in the reaction broth. These results suggest that in vivo oxidoreaductase reactions can be employed to replace isomerases in vitro for biotransformation.
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