hydrolyzing

Hydrolyzing, or hydrolysis, is the chemical process by which a molecule is cleaved into two parts through the addition of water. In a hydrolysis reaction, a water molecule donates a hydrogen to one fragment and a hydroxyl group to the other, effectively breaking a bond that was previously stable in the absence of water. The reaction can occur spontaneously under certain conditions or be catalyzed by acids, bases, or specific enzymes. Enzymatic hydrolysis is a central mechanism in biology, enabling digestion and metabolism.

Common targets of hydrolysis include ester bonds (as in fats and esters), amide bonds (as in proteins and some polymers), glycosidic bonds (in carbohydrates), and phosphodiester bonds (in nucleic acids). Lipases catalyze fat hydrolysis into fatty acids and glycerol; proteases cleave proteins; glycosidases break down carbohydrates; nucleases hydrolyze nucleic acids. ATP hydrolysis is a key energy-releasing process in cells, where the bond linking the terminal phosphate group is cleaved.

Hydrolysis is important in many contexts beyond biology. In industry, ester hydrolysis under basic conditions (saponification) yields carboxylate salts and alcohols, while acid-catalyzed hydrolysis of acetals and other polymers is used in chemical processing. Environmental hydrolysis affects the fate of pesticides and synthetic polymers, and naturally occurring hydrolysis reactions contribute to the degradation of biomolecules after death.

Overall, hydrolyzing expands molecular diversity by converting larger compounds into smaller, more soluble, or more reactive fragments, often enabling further biochemical steps.