ArticleBiotechnology letters2024
ANCUT1, a novel thermoalkaline cutinase from Aspergillus nidulans and its application on hydroxycinnamic acids lipophilization.
Article in Biotechnology letters, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed, 8 citations in OpenAlex.
- Molecular Dynamics Insights into the Biodegradation of Synthetic Polymers byJournal of chemical information and modeling · 2026Article
- Fatty acids in filamentous pathogenic fungi: Multidimensional regulation and pathogenic mechanisms.Virulence · 2025Review
- Biochemical Characterization and Polyester-Binding/Degrading Capability of Two Cutinases fromMicroorganisms · 2025Article
- Exploring biodegradable alternatives: microorganism-mediated plastic degradation and environmental policies for sustainable plastic management.Archives of microbiology · 2024Review
- Poly(lactic acid) Degradation by Recombinant Cutinases fromPolymers · 2024Article
Corrections and comments
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Authors and funding
10 authors at 3 institutions in 1 country.
Funding
Abstract
One of the four cutinases encoded in the Aspergillus nidulans genome, ANCUT1, is described here. Culture conditions were evaluated, and it was found that this enzyme is produced only when cutin is present in the culture medium, unlike the previously described ANCUT2, with which it shares 62% amino acid identity. The differences between them include the fact that ANCUT1 is a smaller enzyme, with experimental molecular weight and pI values of 22 kDa and 6, respectively. It shows maximum activity at pH 9 and 60 °C under assayed conditions and retains more than 60% of activity after incubation for 1 h at 60 °C in a wide range of pH values (6-10) after incubations of 1 or 3 h. It has a higher activity towards medium-chain esters and can modify long-chain length hydroxylated fatty acids constituting cutin. Its substrate specificity properties allow the lipophilization of alkyl coumarates, valuable antioxidants and its thermoalkaline behavior, which competes favorably with other fungal cutinases, suggests it may be useful in many more applications.
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Registered trials
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