Enhanced (S)-linalool production by fusion expression of farnesyl diphosphate synthase and linalool synthase in Saccharomyces cerevisiae

被引:55
|
作者
Deng, Yu [1 ]
Sun, Mingxue [2 ,3 ]
Xu, Sha [2 ,3 ]
Zhou, Jingwen [2 ,3 ,4 ]
机构
[1] Jiangnan Univ, Natl Engn Lab Cereal Fermentat Technol NELCF, Wuxi, Jiangsu, Peoples R China
[2] Jiangnan Univ, Key Lab Ind Biotechnol, Minist Educ, Wuxi, Jiangsu, Peoples R China
[3] Jiangnan Univ, Sch Biotechnol, 1800 Lihu Rd, Wuxi 214122, Jiangsu, Peoples R China
[4] Synerget Innovat Ctr Food Safety & Nutr, Wuxi, Jiangsu, Peoples R China
基金
中国国家自然科学基金;
关键词
biotechnology; enzymes; fermentation biotechnology; gene expression; BIFUNCTIONAL ENZYME; BIOSYNTHESIS; ISOPRENOIDS; CONSTRUCTION; MONOTERPENE; STRATEGIES; LINKERS; DOMAIN; YEAST;
D O I
10.1111/jam.13105
中图分类号
Q81 [生物工程学(生物技术)]; Q93 [微生物学];
学科分类号
071005 ; 0836 ; 090102 ; 100705 ;
摘要
AimsIn order to improve the availability of geranyl diphosphate (GPP) in the mevalonate pathway for enhancing (S)-linalool production in Saccharomyces cerevisiae. Methods and ResultsA (S)-linalool synthase (LIS): AaLS1 from Actinidia arguta was coexpressed with FPPS with different peptide linkers to redirect the flux from geranyl diphosphate (GPP) to (S)-linalool production in S.cerevisiae. The strain with the best peptide linker ((GGGGS)(3)), produced 10155297gl(-1) (S)-linalool, a 697% increase compared to those with two independent LIS and FPPS expressed. In a 3-l fermenter, the (S)-linalool titre was further improved to 24064531gl(-1). ConclusionsThe results demonstrate that the fusion proteins catalysing consecutive steps in a metabolic pathway significantly improved the (S)-linalool production with GPP as precursor. Significance and Impact of the StudyThe fusion protein strategy co-expressing AaLS1 and FPPS, assembled with a long peptide linker made S.cerevisiae produced the highest reported (S)-Linalool titre to date.
引用
收藏
页码:187 / 195
页数:9
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