Biocatalyse

Biocatalysis, or biocatalyse, is the use of natural catalysts—primarily enzymes, and sometimes whole cells—to accelerate chemical transformations. Enzymes confer high chemo-, regio-, and enantioselectivity under mild conditions, often in aqueous solution at ambient temperature and pressure. Biocatalysts can be isolated enzymes, whole-cell catalysts, or engineered variants designed to enhance activity, stability, or substrate scope.

The field encompasses a range of reaction types, including hydrolysis and condensation by hydrolases, redox transformations by oxidoreductases, carbon–carbon and carbon–nitrogen bond modifications by lyases and transferases, and C–H functionalization by oxidases or monooxygenases. Many processes exploit enzyme specificity to produce chiral building blocks, vitamins, fragrances, and pharmaceutical intermediates. Cofactor-dependent reactions are common, with strategies such as cofactor recycling enabling economical processes.

Industrial use is driven by advantages over traditional chemistry: high selectivity reduces purification burdens, reactions often proceed under mild, aqueous conditions, and the processes can be more sustainable with lower waste. Biocatalysis is widely applied in pharmaceutical manufacturing, agrochemicals, food and feed, and fine chemicals, and is increasingly integrated with chemical steps in chemoenzymatic cascades and flow processes.

Optimization methods include protein engineering (directed evolution and rational design) to improve stability or broaden substrate scope, and enzyme immobilization or reactor design to enable reuse and continuous operation. Limitations include substrate range, enzyme stability under process conditions, scale-up challenges, and cofactor requirements for certain enzymes. Advances in genomics, structural biology, and computational design continue to expand its capabilities.