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Catalytic Mechanism Steps The lipase-catalyzed hydrolysis process involves a series of precisely coordinated steps: Substrate binding: Triglyceride substrate approaches the enzyme active site at the lipid-water interface Formation of acyl-enzyme intermediate: Nucleophilic attack by the serine residue creates a covalent intermediate Release of alcohol product: First product (glycerol or partial glyceride) is released from the enzyme Hydrolysis of intermediate: Water molecule attacks the acyl-enzyme complex Release of fatty acid product: Final product (fatty acid) is released, regenerating the free enzyme Interfacial Activation Phenomenon A unique characteristic of lipases is their interfacial activation, where enzyme activity dramatically increases in the presence of lipid-water interfaces