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Reshaping the substrate‐binding pocket of acyl‐ACP reductase to enhance the production of sustainable aviation fuel in Escherichia coli
Biotechnology and Bioengineering ( IF 3.5 ) Pub Date : 2024-10-16 , DOI: 10.1002/bit.28863 Jiahu Han, Takuya Matsumoto, Ryosuke Yamada, Hiroyasu Ogino
Biotechnology and Bioengineering ( IF 3.5 ) Pub Date : 2024-10-16 , DOI: 10.1002/bit.28863 Jiahu Han, Takuya Matsumoto, Ryosuke Yamada, Hiroyasu Ogino
To reduce carbon emissions and address environmental concerns, the aviation industry is exploring the use of sustainable aviation fuel (SAF) as an alternative to traditional fossil fuels. In this context, bio‐alkane is considered a potentially high‐value solution. The present study focuses on the enzymes acyl‐acyl carrier protein [ACP] reductase (AAR) and aldehyde‐deformylating oxygenase (ADO), which are crucial enzymes for alka(e)ne biosynthesis. By using protein engineering techniques, including semi‐rational design and site‐directed mutagenesis, we aimed to enhance the substrate specificity of AAR and improve alkane production efficiency. The co‐expression of a modified AAR (Y26G/Q40M mutant) with wild‐type ADO in Escherichia coli significantly increased alka(e)ne production from 28.92 mg/L to 167.30 mg/L, thus notably demonstrating a 36‐fold increase in alkane yield. This research highlights the potential of protein engineering in optimizing SAF production, thereby contributing to the development of more sustainable and efficient SAF production methods and promoting greener air travel.
更新日期：2024-10-16
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