Biocatalysis

Biocatalysis refers to the use of natural catalysts, typically enzymes, to speed chemical transformations. Enzymes enable a wide range of reactions under mild conditions, often in aqueous solution, and can provide high regio- and enantioselectivity. These features make biocatalysis attractive for producing pharmaceuticals, agrochemicals, and food ingredients with reduced environmental impact.

Enzymes are organized into classes such as hydrolases, oxidoreductases, transferases, lyases, isomerases, and ligases, each catalyzing different reaction types. Common biocatalytic processes include hydrolysis, redox reactions, group transfers, and stereoselective isomerizations. Many enzymes require cofactors, such as NADH or NADPH, or ATP; industrial processes often employ cofactor recycling to reduce costs.

Industrial biocatalysis uses isolated enzymes or whole cells. Techniques such as enzyme immobilization enhance stability and allow reuse, while whole-cell biocatalysis can simplify cofactor recycling. The modern field increasingly relies on protein engineering and directed evolution to improve activity, selectivity, or stability, and on recombinant expression, computational design, and high-throughput screening to expand substrate scope and tailor enzymes for specific processes.

Applications span pharmaceutical synthesis, fine chemicals, flavor and fragrance production, and environmentally sensitive processes. Biocatalysis is a key element of green chemistry due to high selectivity, lower energy demands, and reduced waste. Challenges include limited substrate compatibility for some enzymes, stability under process conditions, enzyme and cofactor costs, and regulatory considerations for large-scale use.