Regulation of the cutinases expressed by Aspergillus nidulans and evaluation of their role in cutin degradation

Bermúdez-García, Eva; Peña-Montes, Carolina; Martins, Isabel; Pais, Joana; Pereira, Cristina Silva; Sánchez, Sergio; Farrés, Amelia

doi:10.1007/s00253-019-09712-3

Cited by 15 publications

(17 citation statements)

References 37 publications

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“…Microorganism and maintenance . A. nidulans PW1 ( biA1, argB2, methG1, veA1 ), a nonpathogenic arginine auxotroph, can be obtained from FGSC as described (Bermúdez-García et al 2019 ). It was maintained in silica gel stocks.…”

Section: Methodsmentioning

confidence: 99%

“…We have reported the purification and characterization of the cutinase ANCUT2 produced by A. nidulans induced by olive oil, some triacylglycerides and fatty acids (Bermúdez-García et al 2017 ; Castro-Ochoa et al 2012 ). Additionally, we have characterized the cutinolytic system and its regulation in A. nidulans (Bermúdez-García et al 2019 ).…”

Section: Introductionmentioning

confidence: 99%

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

Peña-Montes,

Bermúdez-García,

Castro-Ochoa

et al. 2024

Biotechnol Lett

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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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Section: Methodsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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

Peña-Montes,

Bermúdez-García,

Castro-Ochoa

et al. 2024

Biotechnol Lett

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“…AnRodA, Cut1, and Cut2 are the orthologues of RolA, CutL1, and CutB of A. oryzae , respectively [ 8 , 28 ]. Expression of the cut1 and cut2 genes is induced by lipidic carbon sources such as suberin, cutin, or olive oil [ 163 , 164 , 165 ]. Expression of the AnrodA gene is induced by steam-exploded sugarcane bagasse [ 66 ], which is composed of cellulose, hemicellulose, lignin, and wax ester [ 166 , 167 ].…”

Section: Involvement Of Hydrophobins In Solid Polymer Degradationmentioning

confidence: 99%

Aspergillus Hydrophobins: Physicochemical Properties, Biochemical Properties, and Functions in Solid Polymer Degradation

et al. 2022

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Hydrophobins are small amphipathic proteins conserved in filamentous fungi. In this review, the properties and functions of Aspergillus hydrophobins are comprehensively discussed on the basis of recent findings. Multiple Aspergillus hydrophobins have been identified and categorized in conventional class I and two non-conventional classes. Some Aspergillus hydrophobins can be purified in a water phase without organic solvents. Class I hydrophobins of Aspergilli self-assemble to form amphipathic membranes. At the air–liquid interface, RolA of Aspergillus oryzae self-assembles via four stages, and its self-assembled films consist of two layers, a rodlet membrane facing air and rod-like structures facing liquid. The self-assembly depends mainly on hydrophobin conformation and solution pH. Cys4–Cys5 and Cys7–Cys8 loops, disulfide bonds, and conserved Cys residues of RodA-like hydrophobins are necessary for self-assembly at the interface and for adsorption to solid surfaces. AfRodA helps Aspergillus fumigatus to evade recognition by the host immune system. RodA-like hydrophobins recruit cutinases to promote the hydrolysis of aliphatic polyesters. This mechanism appears to be conserved in Aspergillus and other filamentous fungi, and may be beneficial for their growth. Aspergilli produce various small secreted proteins (SSPs) including hydrophobins, hydrophobic surface–binding proteins, and effector proteins. Aspergilli may use a wide variety of SSPs to decompose solid polymers.

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“…In A. nidulans, two of the four cutinase encoding genes were induced by cutin and its monomers. They also appeared to be regulated by the fatty acid regulator A (FarA) transcription factor (Bermúdez-García et al, 2019). In Trichoderma, there are also examples of genes encoding cutinases being induced by cutin monomers, e.g.…”

Section: Relevance Of Gene Induction and Repression In Lignocellulose...mentioning

confidence: 99%

From lignocellulose to plastics: Knowledge transfer on the degradation approaches by fungi

Daly

Cai

Kubicek

et al. 2021

Biotechnology Advances

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Regulation of the cutinases expressed by Aspergillus nidulans and evaluation of their role in cutin degradation

Cited by 15 publications

References 37 publications

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

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

Aspergillus Hydrophobins: Physicochemical Properties, Biochemical Properties, and Functions in Solid Polymer Degradation

From lignocellulose to plastics: Knowledge transfer on the degradation approaches by fungi

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