enzymatichydrolysis

Enzymatic hydrolysis is a biochemical process in which water is added across chemical bonds under the catalysis of enzymes, resulting in bond cleavage. It contrasts with non-enzymatic or chemical hydrolysis, which often requires harsher conditions.

In enzymatic hydrolysis, an enzyme binds its substrate at the active site to form the enzyme–substrate complex. A catalytic water molecule is positioned and activated, enabling bond scission and release of product molecules. The enzyme may be regenerated to catalyze additional cycles.

Substrates include proteins (proteolysis), carbohydrates (amylolysis, cellulolysis), lipids (lipolysis), and esters. Enzymes such as proteases, amylases, cellulases, and lipases catalyze these reactions under mild conditions of temperature and pH.

Applications span biology and industry: digestion and nutrient release in animals; production of glucose, maltose, and amino acids from biomass and foods; hydrolysis of fats in detergents; and conversion of plant matter to fermentable sugars for biofuels. Enzymatic hydrolysis is also employed in textile processing, paper production, and food technology to modify texture and flavor.

Advantages include high specificity, fewer side reactions, and operation under mild conditions. Limitations include enzyme cost, stability and sensitivity to inhibitors, and substrate accessibility. Industrial use often relies on strategies such as enzyme immobilization and protein engineering to improve stability, reusability, and activity under process conditions.