详细信息
Biosynthesis of L-Erythrose by Assembly of Two Key Enzymes in Gluconobacter oxydans ( SCI-EXPANDED收录 EI收录)
文献类型:期刊文献
英文题名:Biosynthesis of L-Erythrose by Assembly of Two Key Enzymes in Gluconobacter oxydans
作者:Zou, Xingxing[1];Lin, Jinping[1];Mao, Xinlei[1];Zhao, Shengyun[2];Ren, Yuhong[1]
机构:[1]East China Univ Sci & Technol, New World Inst Biotechnol, State Key Lab Bioreactor Engn, Shanghai 200237, Peoples R China;[2]Wuyi Univ, Fujian Key Lab Ecoind Green Technol, Wuyishan 354300, Peoples R China
年份:2017
卷号:65
期号:35
起止页码:7721
外文期刊名:JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY
收录:;EI(收录号:20173704155616);WOS:【SCI-EXPANDED(收录号:WOS:000410255400015)】;
基金:This work was funded by the National Special Fund for the State Key Laboratory of Bioreactor Engineering (Grant 2060204), and The National Natural Foundation of China (Grant 21778018).
语种:英文
外文关键词:L-erythrose; self-assembly; G. oxydans; protein peptide interactions
摘要:L-erythrose, a rare aldotetrose, possesses various pharmacological activities. However, efficient L-erythrose production is challenging. Currently, L-erythrose is produced by a two-step fermentation process from erythritol. Here, we describe a novel strategy for the production of L-erythrose in Gluconobacter oxydans (G. oxydans) by localizing the assembly of L-ribose isomerase (L-RI) to membrane-bound sorbitol dehydrogenase (SDH) via the protein peptide interactions of the PDZ domain and PDZ ligand. To demonstrate this self-assembly, green fluorescent protein (GFP) replaced L-RI and its movement to membrane-bound SDH was observed by fluorescence microscopy. The final L-erythrose production was improved to 23.5 g/L with the stepwise metabolic engineering of G. oxydans, which was 1.4-fold higher than that obtained using coexpression of SDH and L-RI in G. oxydans. This self-assembly strategy shows remarkable potential for farther improvement of L-erythrose production.
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