Stability of casein micelles cross-linked with genipin: A physicochemical study as a function of pH

• Autor(a) principal: Casanova, Federico
• Data de Publicação: 2017
• Outros Autores: Silva, Naaman F. Nogueira, Gaucheron, Frédéric, Nogueira, Márcio H., Teixeira, Alvaro V. N. C., Perrone, Italo Tuler, Alves, Maura Pinhero, Fidelis, Priscila Cardoso, Carvalho, Antônio F. de
• Tipo de documento: Artigo
• Idioma: eng
• Título da fonte: LOCUS Repositório Institucional da UFV
• Texto Completo: https://doi.org/10.1016/j.idairyj.2016.12.006; http://www.locus.ufv.br/handle/123456789/21488
• topic: Function of pH; Stability of casein micelles cross-linked

Chemical or enzymatic cross-linking of casein micelles (CMs) increases their stability against dissociating agents. In this paper, a comparative study of stability between native CMs and CMs cross-linked with genipin (CMs-GP) as a function of pH is described. Stability to temperature and ethanol were investigated in the pH range 2.0e7.0. The size and the charge ( z -potential) of the particles were determined by dynamic light scattering. Native CMs precipitated below pH 5.5; CMs-GP precipitated from pH 3.5 to 4.5, whereas no precipitation was observed at pH 2.0e3.0 or pH 4.5e7.0. The isoelectric point of CMs-GP was determined to be pH 3.7. Highest stability against heat and ethanol was observed for CMs-GP at pH 2, where visible coagulation was determined only after 800 s at 140 C or 87.5% (v/v) of ethanol. These results confirmed the hypothesis that cross-linking by GP increased the stability of CMs.