Catalyzes the hydrolysis of complex carboxylic polyesters found in the cell wall of plants (PubMed:19810726, PubMed:15968570). Degrades cutin, a macromolecule that forms the structure of the plant cuticle (PubMed:19810726, PubMed:15968570). cutin + H2O = cutin monomers. Competitively inhibited by the carboxylic acids butyric acid, valeric acid and hexanoic acid (PubMed:15968570). Competitively inhibited by the dicarboxylic acid succinic acid (PubMed:15968570). Competitively inhibited by the alcohols propan-1-ol, butan-1-ol, hexan-1-ol, octan-1-ol, and butane-1,4-diol (PubMed:15968570). kcat is 11 sec(-1) with p-nitrophenyl propionate as substrate (at pH 8.0 and 37 degrees Celsius) (PubMed:15968570). kcat is 18 sec(-1) with p-nitrophenyl butyrate as substrate (at pH 8.0 and 37 degrees Celsius) (PubMed:15968570). kcat is 14 sec(-1) with p-nitrophenyl valerate as substrate (at pH 8.0 and 37 degrees Celsius) (PubMed:15968570). Optimum pH is 9.0. Optimum temperature is 25-40 degrees Celsius (PubMed:19810726). Optimum temperature is 35-55 degrees Celsius (PubMed:15968570). This enzyme enables the fungus to utilize the biodegradable plastics poly(butylene succinate) (PBS) and poly(butylene succinate-co-butylene adipate) (PBSA) as sole carbon source and could therefore be used in plastic recycling. Belongs to the cutinase family.