Amino acid-based hydrophobic affinity cryogel for protein purification from ora-pro-nobis (Pereskia aculeata Miller) leaves

Registro completo de metadados
MetadadosDescriçãoIdioma
Autor(es): dc.creatorNeves, Isabelle Cristina Oliveira-
Autor(es): dc.creatorRodrigues, Adrise Aparecida-
Autor(es): dc.creatorValentim, Thamires Teixeira-
Autor(es): dc.creatorMeira, Ana Cristina Freitas de Oliveira-
Autor(es): dc.creatorSilva, Sérgio Henrique-
Autor(es): dc.creatorVeríssimo, Lizzy Ayra Alcântara-
Autor(es): dc.creatorResende, Jaime Vilela de-
Data de aceite: dc.date.accessioned2026-02-09T12:34:59Z-
Data de disponibilização: dc.date.available2026-02-09T12:34:59Z-
Data de envio: dc.date.issued2021-08-27-
Data de envio: dc.date.issued2021-08-27-
Data de envio: dc.date.issued2020-11-
Fonte completa do material: dc.identifierhttps://repositorio.ufla.br/handle/1/47980-
Fonte completa do material: dc.identifierhttps://doi.org/10.1016/j.jchromb.2020.122435-
Fonte: dc.identifier.urihttp://educapes.capes.gov.br/handle/capes/1164205-
Descrição: dc.descriptionThe surfaces of the polyacrylamide cryogels were coated with L-tryptophan (cryogel-Trp) or L-phenylalanine (cryogel-Phe) to enhance crude leaf extract-derived ora-pro-nobis (OPN) protein binding via pseudo-specific hydrophobic interactions. Cryogels functionalized with amino acids were prepared and characterized through morphological, hydrodynamic, and thermal analyses. The adsorption capacities of cryogel-Phe and cryogel-Trp were evaluated in terms of type (sodium sulfate or sodium phosphate) and concentration (0.02 or 0.10 mol∙L−1) of saline solution, pH (4.0, 5.5, or 7.0), and NaCl concentration (0.0 or 0.5 mol∙L−1). The cryogel-Phe presented a higher adsorptive capacity, achieving its maximum value ( q= 92.53 mg∙g−1) when the crude OPN crude leaf extract was diluted in sodium sulfate 0.02 mol∙L−1 + NaCl 0.50 mol∙L−1, at pH = 7.0. The dilution rate significantly (p < 0.05) affected the recovered protein amount after the adsorption and elution processes, reaching 94.45% when the feedstock solution was prepared with a crude extract 5 times. The zeta potential for the eluted OPN proteins was 5.76 mV (pH = 3.23) for both dilution rates. The secondary structure composition mainly included β-sheets (46.50%) and α-helices (13.93%). The cryogel-Phe exhibited interconnected pores ranging 20–300 μm in size, with a Young modulus of 1.51 MPa, and thermal degradation started at 230 °C. These results indicate that the cryogel-Phe exhibited satisfactory properties as promising chromatography support for use in high-throughput purification of crude leaf extract-derived OPN proteins.-
Idioma: dc.languageen-
Publicador: dc.publisherElsevier-
Direitos: dc.rightsrestrictAccess-
???dc.source???: dc.sourceJournal of Chromatography B-
Palavras-chave: dc.subjectL-phenylalanine-
Palavras-chave: dc.subjectL-tryptophan-
Palavras-chave: dc.subjectAdsorption-
Palavras-chave: dc.subjectHydrophobic interaction-
Palavras-chave: dc.subjectProtein-
Palavras-chave: dc.subjectL-fenilalanina-
Palavras-chave: dc.subjectL-triptofano-
Palavras-chave: dc.subjectAdsorção-
Palavras-chave: dc.subjectInterações hidrofóbicas-
Palavras-chave: dc.subjectProteína - Biossíntese-
Palavras-chave: dc.subjectAminoácidos-
Título: dc.titleAmino acid-based hydrophobic affinity cryogel for protein purification from ora-pro-nobis (Pereskia aculeata Miller) leaves-
Tipo de arquivo: dc.typeArtigo-
Aparece nas coleções:Repositório Institucional da Universidade Federal de Lavras (RIUFLA)

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