Catalyzes the hydrolysis of complex carboxylic polyesters found in the cell wall of plants (PubMed:16844780, PubMed:22238011, PubMed:28124733). Degrades cutin, a macromolecule that forms the structure of the plant cuticle (PubMed:22238011, PubMed:28124733). Also degrades suberin, a specialized macromolecule found in the cell wall of various plant tissues (By similarity). cutin + H2O = cutin monomers. Partially inhibited by the serine protease inhibitor phenylmethanesulfonyl fluoride (PubMed:28124733). Inhibited by various ions, including copper, iron, sodium, potassium, magnesium and calcium (PubMed:28124733). Inhibited by the chelating agent EDTA (ethylenediaminetetraacetic acid) (PubMed:28124733). Inhibited by the surfactants sodium dodecyl sulfate and polysorbate 80 (PubMed:28124733). kcat is 242 sec(-1) with p-nitrophenyl acetate as substrate (at pH 9 and 37 degrees Celsius). Optimum pH is 9-10. Optimum temperature is 60 degrees Celsius. Induced during growth on cutin, in a manner dependent on transcription factors FarA and FARB (PubMed:30863878). Induced during growth on olive oil (PubMed:30863878, PubMed:22238011). Not induced during growth on the lipidic carbon sources 16-hydroxyhexadecanoic acid and propyl ricinoleate (synthetic cutin monomers), or triacetin and triesterate (triglycerides) (PubMed:30863878). Repressed during growth on glucose and on starch (PubMed:30863878, PubMed:22238011). May be exploited in the production of biodiesel. Belongs to the cutinase family.