lhydrolyse

lhydrolyse is commonly written as hydrolysis and refers to the chemical process in which a molecule is cleaved into two parts by reaction with water. In a hydrolysis reaction, water supplies a proton to one fragment and a hydroxyl group to the other, enabling the breaking of bonds such as esters, amides, glycosidic linkages, or phosphoesters.

Hydrolysis can be catalyzed by acids, bases, or enzymes. Acid hydrolysis uses protonation to activate the leaving group and is often applied to esters and glycosides; it can be reversible and typically requires elevated temperatures. Base-catalyzed hydrolysis, or saponification, involves hydroxide attack on an acyl carbon, yielding a carboxylate salt and an alcohol; this process is usually irreversible under workup conditions. Enzymatic hydrolysis is highly specific and occurs under mild conditions in biological systems, driven by enzymes such as proteases, amylases, lipases, nucleases, and hydrolases, each targeting particular bond types.

Common examples include the hydrolysis of esters to carboxylic acids (or carboxylates) and alcohols, the hydrolysis of amides to carboxylic acids and amines, and the cleavage of glycosidic bonds in carbohydrates. In biology, hydrolysis is essential for digestion, metabolism, and macromolecule turnover, with lysosomal hydrolases playing key roles. In industry, hydrolysis is used to convert polymers and once-esterified products into more usable components, to break down biomolecules, and to prepare monomers for synthesis.

Key factors influencing hydrolysis include pH, temperature, solvent, and the nature of the leaving group, all of which determine rate and outcome.