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

• DOI: 10.1007/s10529-024-03467-2
• Publication Date: 2024-02-28T07:02:32Z
• Authors: Carolina Peña-Montes; Eva Bermúdez-García; Denise Castro-Ochoa; Fernanda Vega-Pérez; Katia Esqueda-Dom...; José Augusto Cast...; Augusto González-...; Laura Segoviano-R...; Arturo Navarro-Ocaña; Amelia Farrés
• Keywords: Cutin; Cutinase; Aspergillus nidulans; Acyltransferases; Hydroxycinnamic acid; Aspergillus oryzae

Abstract One of the four cutinases encoded in Aspergillus nidulans genome, ANCUT1, is described here. Culture conditions were evaluated, and it was found that this enzyme produced only when cutin present culture medium, unlike previously ANCUT2, with which shares 62% amino acid identity. The differences between them include fact ANCUT1 a smaller enzyme, experimental molecular weight pI values 22 kDa 6, respectively. It shows maximum activity at pH 9 60 °C under assayed retains more than 60% after incubation for 1 h wide range (6–10) incubations or 3 h. has higher towards medium-chain esters can modify long-chain length hydroxylated fatty acids constituting cutin. Its substrate specificity properties allow lipophilization alkyl coumarates, valuable antioxidants its thermoalkaline behavior, competes favorably other fungal cutinases, suggests may be useful many applications.