期刊
JOURNAL OF BIOTECHNOLOGY
卷 142, 期 3-4, 页码 233-241出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.jbiotec.2009.05.008
关键词
Phlorizin; Naringenin glycoside; UDP-glucose; Galactose inducible promoter; Glyceraldehyde-3-phosphate dehydrogenase promoter
资金
- School of Chemical Engineering, Purdue University [NIH 5 R33 DK070290-03]
Glycosyltransferases are promising biocatalysts for the synthesis of small molecule glycosides. In this study. Saccharomyces cerevisiae expressing a flavonoid glucosyltransferase (GT) front Dianthus caryophyllus (carnation) was investigated as a whole-cell biocatalyst. Two yeast expression systems were compared using the navonoid naringenin as a model substrate. Under in vitro conditions, naringenin-7-O-glucoside was formed and a higher specific glucosyl transfer activity was found using a galactose inducible expression system compared to a constitutive expression system. However, S. cerevisiae expressing the GT constitutively was significantly more productive than the galactose inducible system under in vivo conditions. Interestingly, the glycosides were recovered directly from the Culture broth and did not accumulate intracellularly. A previously uncharacterized naringenin glycoside formed using the D. caryophyllus GT was identified as naringenin-4'-O-glucoside. It was found that S. cerevisiae cells hydrolyze naringenin-7-O-glucoside during whole-cell biocatalysis. resulting in a low final glycoside titer. When phloretin was added as a substrate to the yeast strain expressing the GT constitutively, the natural product phlorizin was formed. This study demonstrates S. cerevisiae is a promising whole-cell biocatalyst host for the production of valuable glycosides. (C) 2009 Elsevier B.V. All rights reserved.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据