biokatalízist

Biocatalysis (biokatalysis) is the use of natural catalysts—primarily enzymes and microorganisms—to accelerate chemical transformations. These catalysts typically enable reactions under mild temperatures and pressures, in aqueous media, and with high selectivity for particular substrates or stereoisomers.

Enzymes can be used as isolated biocatalysts or as whole cells. Reactions may be performed in free solution or with immobilized enzymes to allow reuse and continuous processing. Cofactor requirements, such as NAD(P)H, are often necessary, and various regeneration strategies exist to reduce costs and improve practicality for industrial use.

The field arose from classic studies of fermentation enzymes and expanded through advances in protein engineering, directed evolution, and synthetic biology. These developments have improved enzyme activity, stability, and substrate scope, broadening the range of feasible transformations and enabling more complex reaction sequences.

Applications span pharmaceutical and agrochemical synthesis, flavor and fragrance production, and the manufacture of enantioenriched building blocks. Biocatalysis is central to green chemistry because it can reduce waste, lower energy consumption, and minimize the use of heavy metals and harsh reagents. It also enables high regio- and enantioselectivity that is difficult to achieve with conventional chemical catalysts.

Advantages include high selectivity, mild operating conditions, and the potential for one-pot cascade reactions. Limitations involve incomplete substrate scope for some enzymes, stability under process conditions, upfront development costs, and reliance on efficient cofactor recycling or alternative cofactor-free designs.

Future directions include expanding enzyme repertoires, engineering for non-natural substrates, integration with flow chemistry, and computational design to enable broader industrial deployment.