Pio_2009_Adv.Appl.Microbiol_66_77

Cutinases, also known as cutin hydrolases (EC 3.1.1.74) are enzymes first discovered from phytopathogenic fungi that grow on cutin as the sole carbon source. Cutin is a complex biopolymer composed of epoxy and hydroxy fatty acids, and forms the structural component of higher plants cuticle. These enzymes share catalytic properties of lipases and esterases, presenting a unique feature of being active regardless the presence of an oil-water interface, making them interesting as biocatalysts in several industrial processes involving hydrolysis, esterification, and trans-esterification reactions. Cutinases present high stability in organic solvents and ionic liquids, both free and microencapsulated in reverse micelles. These characteristics allow the enzyme application in different areas such as food industry, cosmetics, fine chemicals, pesticide and insecticide degradation, treatment and laundry of fiber textiles, and polymer chemistry. The present chapter describes the characteristics, potential applications, and new perspectives for these enzymes.