Catalyzes the hydrolysis of complex carboxylic polyesters found in the cell wall of plants (PubMed:18658138, PubMed:8286366, PubMed:8555209, PubMed:19810726). Degrades cutin, a macromolecule that forms the structure of the plant cuticle (PubMed:18658138, PubMed:8286366, PubMed:8555209, PubMed:19810726). Allows pathogenic fungi to penetrate through the cuticular barrier into the host plant during the initial stage of fungal infection (Ref.4). cutin + H2O = cutin monomers. Inhibited by n-undecyl phosphonate (C11Y4) (PubMed:25219509). Inhibited by paraoxon (PubMed:8286366, PubMed:25219509). kcat is 1800 sec(-1) with p-nitrophenyl butyrate as substrate (at pH 9 and 30 degrees Celsius). Optimum pH is 8. Optimum temperature is below 30 degrees Celsius (PubMed:19810726). Optimum temperature is 30-40 degrees Celsius (PubMed:18658138). The 2 disulfide bonds play a critical role in holding the catalytic residues in juxta-position; reduction of the disulfide bridges results in the complete inactivation of the enzyme. O-glycosylated; contains one mole each of mannose, arabinose, N-acetylglucosamine, and glucuronic acid. May have promising applications in chemical and textile industries as it is capable of hydrolyzing a variety of substrates including soluble esters and insoluble triglycerides (PubMed:18658138, PubMed:25219509). Can hydrolyze and thus modulate the surface properties of synthetic fibers such as the plastic poly(ethylene terephthalate) (PET), or the textile fibers polyamide 6,6, polyester and acrylic (Ref.5, PubMed:17306400). Belongs to the cutinase family.