Engineering a Feruloyl–Coenzyme A Synthase for Bioconversion of Phenylpropanoid Acids into High-Value Aromatic Aldehydes

• DOI: 10.1021/acs.jafc.2c02980
• Publication Date: 2022-08-02T19:30:18Z
• Authors: Qihang Chen; Yaqin Jiang; Zhengzhong Kang; Jie Cheng; Xiaochao Xiong; Ching Yuan Hu; Yonghong Meng
• Keywords: Bioconversion; Phenylpropanoid; Decarboxylation; Hydroxycinnamic acid; Cinnamic acid; Biocatalysis

Aromatic aldehydes find extensive applications in food, perfume, pharmaceutical, and chemical industries. However, a limited natural enzyme selectivity has become the bottleneck of bioconversion aromatic from phenylpropanoid acids. Here, based on original structure feruloyl-coenzyme A (CoA) synthetase (FCS) Streptomyces sp. V-1, we engineered five substrate-binding domains to match specific FcsCIAE407A/K483L, FcsMAE407R/I481R/K483R, FcsHAE407K/I481K/K483I, FcsCAE407R/I481R/K483T, FcsFAE407R/I481K/K483R showed 9.96-, 10.58-, 4.25-, 6.49-, 8.71-fold enhanced catalytic efficiency for degrading CoA thioesters cinnamic acid, 4-methoxycinnamic 4-hydroxycinnamic caffeic ferulic respectively. Molecular dynamics simulation illustrated that novel formed strong interaction forces with substrates' methoxy/hydroxyl group provided hydrophobic/alkaline surfaces. Five recombinant E. coli FCS mutants were constructed maximum benzaldehyde, p-anisaldehyde, p-hydroxybenzaldehyde, protocatechualdehyde, vanillin productivity 6.2 ± 0.3, 5.1 0.23, 4.1 0.25, 7.1 8.7 0.2 mM/h, Hence, our study efficient enzymes acids into aldehydes.