Benzaldehyde lyase (BAL)-catalyzed enantioselective C<ce:glyph name="sbnd"/>C bond formation in deep-eutectic-solvents-buffer mixtures.

Deep-eutectic-solvents (DES) have emerged in the last decades as promising bio-based and biodegradable neoteric solvents for biocatalysis, with examples covering different enzymes (mostly hydrolases) and whole-cells (baker's yeast). This paper explores for the first time the use of benzaldehyde lyase (BAL), a thiamine-diphosphate dependent lyase (ThDP-lyase) able to catalyze the carboligation of aldehydes (C<ce:glyph name="sbnd"/>C bond formation) in different DES-buffer mixtures. By using choline chloride-glycerol DES, BAL remains fully active with excellent enantioselectivity at 60:40 DES-buffer (v/v), whereby a significant denaturation is observed at 70:30 mixtures. Remarkably, the use of choline chloride-urea DES as reaction media leads to full conversions with BAL at such solvent-buffer proportions, suggesting that the design of both the biocatalyst and the neoteric solvent may provide useful novel reactive systems for biocatalysis in non-conventional media. [ABSTRACT FROM AUTHOR]