Lipases hydrolyze which bonds?

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Lipases hydrolyze ester bonds in lipids. They catalyze the cleavage of the ester linkage that connects fatty acids to the glycerol backbone in triglycerides (and other lipids), releasing free fatty acids and glycerol or mono- and di-glycerides. This specificity explains why lipases act on lipid substrates while other enzyme classes target different bond types: glycosidic bonds in carbohydrates are broken by carbohydrases, peptide bonds in proteins by proteases, and phosphodiester bonds in nucleic acids by nucleases. In digestion, lipases often work at the lipid–water interface, aided by emulsification to increase accessibility to the hydrophobic lipid substrates.