文献类型：期刊文献

英文题名：Metabolic Checkpoint Aldehyde Dehydrogenases Are Important for Diverting β-Oxidation into 1-Butanol Biosynthesis from Kitchen Waste Oil in Pseudomonas aeruginosa

作者：Li, Ying[1]; Liu, Zheng[1]; Ge, Xizhen[1]

第一作者：李映

通讯作者：Ge, Xizhen

机构：[1] Beijing Key Laboratory of Biomass Waste Resource Utilization, College of Biochemical Engineering, Beijing Union University, Beijing, 100023, China

第一机构：北京联合大学生物化学工程学院生物医药系

年份：2021

卷号：193

期号：3

起止页码：730-742

外文期刊名：Applied Biochemistry and Biotechnology

收录：EI(收录号：20204609489240);Scopus(收录号：2-s2.0-85095867133)

基金：This work was financially supported by Beijing Municipal Education Commission Technology Plan (KM202011417006), Project of Beijing Municipal Commission of Education (KZ201911417049), Premium Funding Project for Academic Human Resources Development in Beijing Union University (BPHR2018BZ01), and China Scholarship Council Project (201908110070).

语种：英文

外文关键词：Aldehydes - Bacteria - Binding energy - Biochemistry - Biosynthesis - Fuel additives - Metabolism - Oils and fats - Transcription

摘要：1-Butanol (1-BD) is a promising fuel additive which can be biosynthesized via reversed β-oxidation pathway in bacteria. However, heterologous reversed β-oxidation pathway is a carbon chain prolongation process with several genes overexpressed in most of bacterial hosts, leading to low titer of 1-BD and high cost for production. Here we displayed a forward β-oxidation pathway for 1-BD production in a kitchen waste oil (KWO) degrading Pseudomonas aeruginosa PA-3, and we proved that aldehyde dehydrogenase (ALDH) is a checkpoint for diverting metabolic flux into 1-BD biosynthesis. With nitrogen source supplied, titer of 1-BD was increased accompanied with 12 ALDH coding genes transcriptionally promoted to different degrees. At the same time, binding energies of these ALDHs with different length of acyl-CoAs in β-oxidation were calculated to identify their specificities. Based on the above information, ALDH deletions were conducted. We certified that deletion of ALDH8 and ALDH9 led to significant decreased titers of 1-BD. Finally, these two ALDHs were separately overexpressed in PA-3, and titer of 1-BD was promoted to 1.36?g/L at 72?h in shake flask. Totally in this work, we provided a forward β-oxidation pathway for 1-BD production from KWO, and the roles of ALDHs were confirmed. ? 2020, Springer Science+Business Media, LLC, part of Springer Nature.