@article{Zhou2026, 
author = {Jieyu Zhou and Xiangyuan Gu and Siyi Chen and Yichun Zhu and Ye Ni},
title = {Biooxidation of aromatic aldehydes by aldehyde dehydrogenase from Sphingobium sp. using synthetic nicotinamide cofactor biomimetics},
year = {2026},
journal = {Green Chemical Engineering},
volume = {7},
number = {3},
pages = {245-250},
keywords = {Aldehyde dehydrogenase, Nicotinamide cofactor biomimetic, Biocatalysis},
url = {https://www.sciopen.com/article/10.1016/j.gce.2025.05.005},
doi = {10.1016/j.gce.2025.05.005},
abstract = {An aldehyde dehydrogenase SpALDH2 from Sphingobium sp. has been discovered with the unprecedented ability to utilize oxidized nicotinamide cofactor biomimetics (NCBsox). Among eight NCBsox tested, 3-carbamoyl-1-(4-carboxybenzyl) pyridin-1-ium (p-BANA+) enabled 96.8% conversion of syringaldehyde, comparable to NAD+. SpALDH2 exhibited a kcat/KM of 21.418 mM−1 min−1 with p-BANA+, nearly 500-fold higher than with other NCBsox. Molecular docking and interaction analyses suggested that hydrogen bonding and pi–pi stacking between the para-carboxyl group of p-BANA+ and key active-site residues contribute to its superior compatibility. These results support SpALDH2 as a promising catalyst for NCBsox-mediated oxidation.}
}