Biological valorization of lignin-derived vanillin to vanillylamine by recombinant E. coli expressing ω-transaminase and alanine dehydrogenase in a petroleum ether-water system

Vanillylamine, as an important drug precursor and fine chemical intermediate, has great economic value. By constructing a strategy of double enzyme co-expression, one newly constructed recombinant E. coli HNIQLE-AlaDH expressing ω-transaminase from Aspergillus terreus and alanine dehydrogenase from Bacillus subtilis was firstly used aminate lignin-derived vanillin to vanillylamine by using a relatively low dosage of amine donors (vanillin:L-alanine:isopropylamine = 1:1:1, mol/mol/mol). In addition, in a two-phase system (water:petroleum ether = 80:20 v/v), the bioconversion of vanillin to vanillylamine was catalyzed by HNIQLE-AlaDH cell under the ambient condition, and the vanillylamine yield was 71.5%, respectively. This double-enzyme HNIQLE-AlaDH catalytic strategy was applied to catalyze the bioamination of furfural and 5-hydroxymethylfurfural with high amination efficiency. It showed that the double-enzyme catalytic strategy in this study promoted L-alanine to replace D-alanine to participate in bioamination of vanillin and its derivatives, showing a great prospect in the green biosynthesis of biobased chemicals from biomass.