Cutinase: characteristics, preparation, and application

Abstract

Cutinases (E.C. 3.1.1.74) belong to the α/β-hydrolase superfamily. They were initially discovered because they are secreted by fungi to hydrolyze the ester bonds of the plant polymer cutin. Since then, they have been shown to catalyze the hydrolysis of a variety of polymers, insoluble triacylglycerols, and low-molecular-weight soluble esters. Cutinases are also capable of catalyzing esterification and transesterification reactions. These relatively small, versatile, secreted catalysts have shown promise in a number of industrial applications. This review begins by describing the characteristics of cutinases, pointing out key differences among cutinases, esterases and lipases, and reviewing recent progress in engineering improved cutinases. It continues with a review of the methods used to produce cutinases, with the goal of obtaining sufficient quantities of material for use in industrial processes. Finally, the uses of cutinases in the textile industry are described. The studies presented here demonstrate that the cutinases are poised to become important industrial catalysts, replacing older technologies with more environmentally friendly processes.

Keywords: CBM; Crystal structure; Cutinase; DHA; EPA; Identification; Molecular modification; PBM; PET; Preparation; RBB; Remazol Brilliant Blue R; Textile industry; carbohydrate-binding module; docosahexanoic acid; eicosapentanoic acid; polyethylene terephthalate; polyhydroxyalkanoate-binding module.