Biocatalytic valorization of lignin subunit: Screening a carboxylic acid reductase with high substrate preference to syringyl functional group

Lignin is inexpensive and the most abundant source of biological aromatics. It can be decomposed to three types of subunits, 4-hydroxybenzoic, vanillic and syringic acids, each of which can be valorized to value added compounds. Syringaldehyde is a versatile phenolic aldehyde implicated with multiple bioactive properties as well as intermediates for biofuels. Herein, fourteen microbial carboxylic acid reductases (CARs) were screened for the biocatalysis of the energetically unfavorable reduction of syringic acid to syringaldehyde. Nine CARs were positive to syringic acid reduction, among which Mycobacterium abscessus CAR exhibited the highest analytical yield of the product. By the optimization of the reaction condition, the whole-cell biocatalyst (i.e., recombinant Escherichia coli expressing the gene) successfully converted syringic acid to syringaldehyde with a yield of 90%. Furthermore, structural features of the screened CAR responsible for the specificity toward the syringyl subunit were analyzed that helps to further engineer the biocatalyst for improved performances.