Homologous expression, purification, and characterization of a recombinant acetylxylan esterase from Aspergillus nidulans (2024)
- Authors:
- USP affiliated authors: SEGATO, FERNANDO - EEL ; POLIZELI, MARIA DE LOURDES TEIXEIRA DE MORAES - FFCLRP ; WARD, RICHARD JOHN - FFCLRP ; MARIANO, CLARA BORTOLETTO - FFCLRP ; ALNOCH, ROBSON CARLOS - FFCLRP ; ANDRADES, DIANDRA DE - FFCLRP ; BERTO, GABRIELA LEILA - EEL ; SALGADO, JOSÉ CARLOS DOS SANTOS - FFCLRP
- Unidades: EEL; FFCLRP
- DOI: 10.1016/j.ijbiomac.2024.135816
- Assunto: BIOTECNOLOGIA
- Keywords: Acetylxylan esterases; Carbohydrate esterases; Aspergillus nidulans; Homologous expression; Synergism; Xylooligosaccharides
- Agências de fomento:
- Language: Inglês
- Abstract: Acetylxylan esterases (AXEs) are essential enzymes that break down the acetyl groups in acetylated xylan found in plant cell walls polysaccharides. They work synergistically with backbone-depolymerizing xylanolytic enzymes to accelerate the degradation of complex polysaccharides. In this study, we cloned the gene axeA, which encodes the acetylxylan esterase from Aspergillus nidulans FGSC A4 (AxeAN), into the pEXPYR expression vector and introduced it into the high protein-producing strain A. nidulans A773. The purified AxeAN, with a molecular weight of 33.5 kDa as confirmed by SDS-PAGE, was found to be active on ρ-nitrophenyl acetate (ρNPA), exhibiting a remarkably high specific activity (170 U mg−1) at pH 7.0 and 55 °C. AxeAN demonstrated stability over a wide pH range (5.5–9.0), retaining >80% of its initial activity after 24 h. The KM and Vmax were 0.098 mmol L−1 and 320 U mg−1, respectively, using ρNPA as a substrate. We also evaluated the synergistic effect of AxeAN with an endo-1,4-β-xylanase from Malbranchea pulchella (MpXyn10) in the hydrolysis of four different xylans (Birchwood, Beechwood, Oat spelt, and Arabinoxylan) to produce xylooligosaccharides (XOS). The best results were obtained using Birchwood xylan as substrate and MpXyn10-AxeAN as biocatalysts after 24 h of reaction (50 °C), with a XOS-yield of 91%, value 41% higher when compared to MpXyn10 (XOS-yield of 63%). These findings showed the potential of the application of AxeAN, together with other xylanases, to produce xylooligosaccharides with high purity and other products with high added value in the field of lignocellulosic biorefinery.
- Imprenta:
- Publisher: Elsevier
- Publisher place: Greeley-CO
- Date published: 2024
- Source:
- Título: International journal of biological macromolecules
- ISSN: 0141-8130
- Volume/Número/Paginação/Ano: v.280, part. 2, art. n.135816, p. 1-12, 2024
- Este periódico é de acesso aberto
- Este artigo NÃO é de acesso aberto
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ABNT
ALVES, Gabriela Souza et al. Homologous expression, purification, and characterization of a recombinant acetylxylan esterase from Aspergillus nidulans. International journal of biological macromolecules, v. 280, n. art. 135816, p. 1-12, 2024Tradução . . Disponível em: https://doi.org/10.1016/j.ijbiomac.2024.135816. Acesso em: 13 fev. 2026. -
APA
Alves, G. S., Polizeli, M. D. L. T. D. M., Andrades, D. de, Salgado, J. C. S., Mariano, C. B., Berto, G. L., et al. (2024). Homologous expression, purification, and characterization of a recombinant acetylxylan esterase from Aspergillus nidulans. International journal of biological macromolecules, 280( art. 135816), 1-12. doi:10.1016/j.ijbiomac.2024.135816 -
NLM
Alves GS, Polizeli MDLTDM, Andrades D de, Salgado JCS, Mariano CB, Berto GL, Segato F, Ayub MAZ, Ward RJ, Alnoch RC. Homologous expression, purification, and characterization of a recombinant acetylxylan esterase from Aspergillus nidulans [Internet]. International journal of biological macromolecules. 2024 ;280( art. 135816): 1-12.[citado 2026 fev. 13 ] Available from: https://doi.org/10.1016/j.ijbiomac.2024.135816 -
Vancouver
Alves GS, Polizeli MDLTDM, Andrades D de, Salgado JCS, Mariano CB, Berto GL, Segato F, Ayub MAZ, Ward RJ, Alnoch RC. Homologous expression, purification, and characterization of a recombinant acetylxylan esterase from Aspergillus nidulans [Internet]. International journal of biological macromolecules. 2024 ;280( art. 135816): 1-12.[citado 2026 fev. 13 ] Available from: https://doi.org/10.1016/j.ijbiomac.2024.135816 - Recombinant GH3 β-glucosidase stimulated by xylose and tolerant to furfural and 5-hydroxymethylfurfural obtained from Aspergillus nidulans
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Informações sobre o DOI: 10.1016/j.ijbiomac.2024.135816 (Fonte: oaDOI API)
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