Functional characterization and structural insights of three cutinases from the ascomycete Fusarium verticillioides

Caroline Torres de Oliveira, Michelle Alexandrino de Assis, João Paulo Lourenço Franco Cairo, André Damasio, Gonçalo Amarante Guimarães Pereira, Marcio Antonio Mazutti, Débora de Oliveira

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Cutinases are serine esterases that belong to the α/β hydrolases superfamily. The natural substrates for these enzymes are cutin and suberin, components of the plant cuticle, the first barrier in the defense system against pathogen invasion. It is well-reported that plant pathogens produce cutinases to facilitate infection. Fusarium verticillioides, one important corn pathogens, is an ascomycete upon which its cutinases are poorly explored. Consequently, the objective of this study was to perform the biochemical characterization of three precursor cutinases (FvCut1, FvCut2, and FvCut3) from F. verticillioides and to obtain structural insights about them. The cutinases were produced in Escherichia coli and purified. FvCut1, FvCut2, and FvCut3 presented optimal temperatures of 20, 40, and 35 °C, and optimal pH of 9, 7, and 8, respectively. Some chemicals stimulated the enzymatic activity. The kinetic parameters revealed that FvCut1 has higher catalytic efficiency (Kcat/Km) in the p-nitrophenyl-butyrate (p-NPB) substrate. Nevertheless, the enzymes were not able to hydrolyze polyethylene terephthalate (PET). Furthermore, the three-dimensional models of these enzymes showed structural differences among them, mainly FvCut1, which presented a narrower opening cleft to access the catalytic site. Therefore, our study contributes to exploring the diversity of fungal cutinases and their potential biotechnological applications.

Original languageEnglish
Article number106415
Number of pages10
Early online date15 Dec 2023
Publication statusPublished - Apr 2024

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  • Carboxylic Ester Hydrolases/genetics
  • Ascomycota
  • Fusarium/genetics

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