Depolymerization of a hydroxy fatty acid biopolymer, cutin, by an extracellular enzyme from Fusarium solani f. pisi: Isolation and some properties of the enzyme

摘要: Abstract Fusarium solani f. pisi was shown to grow on the hydroxy fatty acid biopolymer cutin as sole carbon source. Such growth conditions induced production of an extracellular depolymerising enzyme. Analysis products enzymatically derived from labeled by thin-layer chromatography and radio gas-liquid showed that enzyme released all classes monomers. This preparation also catalyzed hydrolysis several model ester substrates. It did not hydrolyze triacyl glycerol pancreatic lipase cutin, indicating is a nonspecific lipase. With p-nitrophenyl palmitate substrate broad pH optimum near 8.5 it stimulated Triton X-100. Maximal stimulation obtained at 3.7 mg/ ml detergent. Apparent Km for 1.6 × 10−4 m . p-Nitrophenyl esters C2–C18 acids gave comparable values V revealing no striking specificity. Treatment with diisopropyl fluorophosphate severely inhibited while iodoacetamide p-chloromercuric benzoate affect enzymatic activity, suggesting serine hydrolase.