Biocatalytic

Biocatalytic refers to processes that use biological catalysts—primarily enzymes, but also whole cells or engineered microorganisms—to accelerate chemical transformations. Biocatalysis relies on the high specificity and activity of biological catalysts, often enabling highly selective transformations that are difficult to achieve with conventional chemical catalysts. Catalysts can be used in purified form or as part of living or non-living cells, and reactions may require cofactors such as NAD(P)H or ATP, which can be regenerated to improve efficiency. Immobilization on solid supports or within reactor systems is common to enable catalyst reuse and to improve stability.

Biocatalytic methods are applied across industries, including pharmaceutical, agrochemical, flavor and fragrance, and fine chemicals. Enantioselective oxidations, reductions, hydrolyses, amination, and carbon–carbon bond-forming reactions are achieved with enzymes such as lipases, transaminases, ketoreductases, and monooxygenases. Enzymes can operate under mild temperatures and pressures, often in aqueous media, and can tolerate renewable or waste streams, contributing to sustainable manufacturing and reduced byproducts.

Development of biocatalytic processes combines biochemistry with chemical engineering. Protein engineering and directed evolution expand substrate scope and stability, while immobilization and in situ cofactor recycling improve practicality for large-scale production. Whole-cell biocatalysis leverages cellular metabolism and can simplify cofactor management but may introduce side reactions or regulatory considerations.

Limitations include restricted substrate scope, enzyme stability, and high upfront development costs. Ongoing advances in computational design, high-throughput screening, and process intensification are expanding the range of feasible biocatalytic transformations.