Biotechnological Application of Cutinase: A Powerful Tool in Synthetic Biology

Abstract

Cutinases (EC 3.1.1.74) are widely distributed in fungi, bacteria and plants with diversified structures and properties. Besides acting on the natural substrate cutin, cutinases are the first line of natural biocatalysts to hydrolyze artificial polyesters and toxic xenobiotics such as polyethylene terephthalate (PET), polycaprolactone (PCL), polylactic acid (PLA), polyhydroxybutyl succinate (PBS), phthalate and malathion esters. Moreover, cutinases can act as promising stereoselective catalysts in esterification and transesterification reactions and present better selectivities than lipases. These pioneering studies indicate that the biotechnological application of cutinase as a powerful tool in synthetic biology deserves further investigation, for both degradation and biosynthesis towards a broader range of ester bond-containing substrates. This review summarizes the classifications and properties of cutinases from different sources and insights into the structure–function relationship of different cutinases. It also highlights the uniqueness and advantages of representative cutinases in biodegradation and biosynthesis, and then prospects the future application of natural and engineered cutinases in synthetic biology.

Eight Up-Coming Biotech Tools to Combat Climate Crisis

“…To invade plants, pathogens produce cutinases, which are enzymes capable of breaking down cutin through the hydrolysis of its polymeric network. Cutinases are primarily produced by plant pathogenic fungi, but also by some bacteria and plants [ 87 ]. As serine hydrolases, cutinases cleave ester bonds such as esterases and lipases.…”

ANCUT1, a novel thermoalkaline cutinase from Aspergillus nidulans and its application on hydroxycinnamic acids lipophilization

“…Cutinases are named for their hydrolytic action on the ester bonds linking the fatty acids that make up cutin, a structural component of the cuticle that covers the aerial parts of plants and whose primary function is to serve as a protective barrier against physical, chemical, and biological environmental factors, including pathogens (Kolattukudy et al 1981 ; Arya and Cohen 2022 ). The production of natural cutinases is mainly related to phytopathogenic fungi; however, they are also found in other microorganisms such as bacteria and in plants that can degrade the cutin barrier of the stigma to promote the fertilization process (Liang and Zou 2023 ).…”

“…In addition to natural polyesters, cutinases hydrolyze other related substrates such as lipids, waxes and various synthetic esters. They can also catalyze biosynthesis reactions such as esterification and transesterification (Liang and Zou 2023 ). Due to their versatility, cutinases have been proposed for a wide range of applications in industrial processes, including food, textile, detergent, agricultural, chemical and environmental industries (Chen et al 2013 ; Dutta et al 2009 ).…”

Natural deep eutectic solvents as thermostabilizer for Humicola insolens cutinase

“…Cutinases (EC 3.1.1.74) are small extracellular serine hydrolases produced by bacteria and fungi generally catalyzing the hydrolysis of the cutin, an insoluble lipid polyester which acts as structural component of plant cuticles [1]. Compared to other hydrolase family members such as lipases and esterases, cutinases have the smallest molecular weight (20-30 kDa) with a three-dimensional structure characterized by a central parallel β-sheet and surrounding α-helices.…”

“…Recently, cutinases from several fungal sources have been applied as natural biocatalysts on different synthetic aliphatic polyesters such as polybutylene succinate (PBS), polycaprolactone (PCL), polylactic acid (PLA), poly(butylene succinate-co-adipate) (PBSA) polyethylene terephthalate (PET) [1,4,5], and polyurethanes [6]. Cutinase from Fusarium sp.…”