Advances in benzaldehyde lyase-catalyzed biotransformations: From enzyme engineering to industrial applications

Abstract

Benzaldehyde lyase (BAL), a thiamine diphosphate (ThDP)-dependent enzyme requiring divalent cations ( e.g. , Mg 2+ ), mediates enantioselective C-C bond formation and cleavage to exclusively produce ( R )-configured α -hydroxy ketones. Recent integration of rational enzyme design, materials science, and green chemistry innovations has significantly broadened BAL's catalytic versatility. These advances establish BAL as a pivotal tool in sustainable chiral synthesis, enabling efficient construction of high-value molecules for medicinal chemistry, agrochemicals, and advanced materials. This review highlights BAL's emerging applications in biotransformation over the last fifteen years (2010–2025), including multi-enzyme combinations and multidisciplinary collaborations. It presents groundbreaking results that provide both theoretical foundations and scalable solutions for pharmaceutical and industrial processes.