Adsorção de glicomacropeptídeo por interação hidrofóbica em leito expandido

• Ano de defesa: 2007
• Autor(a) principal: Sierra, Omar Andrés Pérez
• Orientador(a): Minim, Luis Antonio
• Banca de defesa: Miranda, Everson Alves , Martins, Márcio Arêdes
• Tipo de documento: Tese
• Tipo de acesso: Acesso aberto
• Idioma: por
• Instituição de defesa: Universidade Federal de Viçosa
• Programa de Pós-Graduação: Doutorado em Ciência e Tecnologia de Alimentos
• Departamento: Ciência de Alimentos; Tecnologia de Alimentos; Engenharia de Alimentos
• País: BR
• Palavras-chave em Português: Glicomacropeptídeo; Interação hidrofóbica; Leito expandido
• Palavras-chave em Inglês: Glicomacropeptide; Hydrophobic interaction; Expanded bed
• Área do conhecimento CNPq: CNPQ::CIENCIAS AGRARIAS::CIENCIA E TECNOLOGIA DE ALIMENTOS::TECNOLOGIA DE ALIMENTOS
• Link de acesso: http://locus.ufv.br/handle/123456789/399

In this work was studied the adsorption process of glicomacropeptide, protein obtained from the cheese whey protein, with hydrophobic iteration chromatography, modifying the temperature and salt concentration conditions. The titillation calorimetric was used to develop a thermodynamic analysis of the process. The rupture curves were obtained starting from the hydrodynamic behaviour of expanded bed, and also was studied the adsorption kinetics of the GMP in the hydrophobic resin. With these results, and studying the GMP in the adsorption of the hydrophobic resin (Streamline Phenil), was possible to observe that this process is dependent of the temperature and salt concentration, verified by calorimetry that the process is spontaneous and entropically developed. The increase of the lineal speed and consequently, the expansion degree associated with the increase of the protein concentration decreases the efficiency of the column to adsorve the GMP, presenting a stable fluid dynamics. In the kinetic model was found that with the increase of the temperature and the increase of the concentration of the sodium sulphate presents a little variation in the equilibrium time. The model of mass transference applied was properly adjusted to the adsorption kinetics of the protein in the studied conditions.