Performance of pseudo-specific cryogel in lysozyme purification from chicken egg white

Registro completo de metadados
MetadadosDescriçãoIdioma
Autor(es): dc.creatorMeira, Ana Cristina Freitas de Oliveira-
Autor(es): dc.creatorSilva, Richard Marins da-
Autor(es): dc.creatorNeves, Isabelle Cristina Oliveira-
Autor(es): dc.creatorMinim, Luis Antônio-
Autor(es): dc.creatorVeríssimo, Lizzy Ayra Alcântara-
Autor(es): dc.creatorResende, Jaime Vilela de-
Data de aceite: dc.date.accessioned2026-02-09T12:47:07Z-
Data de disponibilização: dc.date.available2026-02-09T12:47:07Z-
Data de envio: dc.date.issued2023-04-05-
Data de envio: dc.date.issued2023-04-05-
Data de envio: dc.date.issued2022-10-
Fonte completa do material: dc.identifierhttps://repositorio.ufla.br/handle/1/56514-
Fonte completa do material: dc.identifierhttps://onlinelibrary.wiley.com/doi/10.1002/cjce.24703-
Fonte: dc.identifier.urihttp://educapes.capes.gov.br/handle/capes/1168228-
Descrição: dc.descriptionThe application of cryogels for biomolecule purification has expanded due to their adsorption efficiency and operational advantages. In this study, polyacrylamide cryogels functionalized with l-phenylalanine (cryogel-Phe) via the glutaraldehyde method were designed for lysozyme adsorption. Cryogel functionalization was confirmed by Fourier-transform infrared spectroscopy and Kjeldahl analysis, indicating the immobilization of 458.65 mgphenylalanine gcryogel−1. Cryogel-Phe showed high porosity (0.95) and a Young's modulus of 526.71 kPa. Thermogravimetric analysis indicated that thermal degradation occurred above 200°C. Differential scanning calorimetry and X-ray diffraction confirmed that the cryogel material was amorphous. In addition, the column presented a hydraulic permeability of 4.15 × 10−13 m2, axial dispersion ranging from 10−7 to 10−6 m2 s−1, and a height equivalent to a theoretical plate ranging from 0.10 to 0.21 cm. The highest adsorption of lysozyme (67.65 mg g−1) was obtained using sodium thiocyanate saline solution (0.025 mol L−1, pH 5.0). The ability of the cryogel-Phe column to capture and purify lysozyme was confirmed by high enzymatic activity (1294.17 U ml−1), purity (87.92%), purification factor (11.49), and sulphate-polyacrylamide electrophoresis gel (SDS-PAGE) electrophoresis gel.-
Idioma: dc.languageen-
Publicador: dc.publisherCanadian Society for Chemical Engineering (CSChE)-
Direitos: dc.rightsrestrictAccess-
???dc.source???: dc.sourceThe Canadian Journal of Chemical Engineering (CJCE)-
Palavras-chave: dc.subjectFunctionalization of polymers-
Palavras-chave: dc.subjectMorphology-
Palavras-chave: dc.subjectPorous materials-
Palavras-chave: dc.subjectProteins-
Título: dc.titlePerformance of pseudo-specific cryogel in lysozyme purification from chicken egg white-
Tipo de arquivo: dc.typeArtigo-
Aparece nas coleções:Repositório Institucional da Universidade Federal de Lavras (RIUFLA)

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