Biokatalyysiin

Biokatalyysiin refers to biocatalysis, the use of natural catalysts—principally enzymes—to accelerate chemical reactions. In practice, biocatalysis encompasses enzymatic transformations performed in vitro and, in whole-cell approaches, by living microorganisms. Biocatalysts offer high chemo-, regio-, and enantioselectivity under mild conditions, often enabling routes that are difficult for traditional catalysis.

Enzymes such as hydrolases, oxidoreductases, transferases, lyases, and isomerases are commonly employed. Lipases enable esterifications and transesterifications; dehydrogenases and reductases effect redox steps; aminotransferases and deaminases handle amination and related reactions. Whole cells can perform multi-step transformations and cofactor-dependent processes. Advances in enzyme engineering and directed evolution expand substrate scope and robustness. Immobilization and flow reactors improve stability, allow reuse, and facilitate scale-up. Cofactor recycling systems reduce costs.

Applications span pharmaceutical manufacturing, fine-chemical production, agrochemicals, food and flavor industries, and environmental remediation. Biocatalysis is valued for producing optically active compounds with high enantioselectivity, reducing chemical waste, and enabling greener processes.

Challenges include limited natural substrate range for some enzymes, sensitivity to process conditions, enzyme stability, and higher upfront development cost. Ongoing research aims to broaden enzyme libraries, create robust cell-free systems, and integrate biocatalysis with chemical steps in one-pot cascades and continuous production.

Biokatalyysiin thus represents a central approach in sustainable synthesis, linking biochemistry, molecular biology, and chemical engineering to enable efficient, selective, and eco-friendly manufacturing.