Selective coacervation between lactoferrin and the two isoforms of β-lactoglobulin

• Autor(a) principal: Tavares, Guilherme M.
• Data de Publicação: 2015
• Outros Autores: Croguennec, Thomas, Hamon, Pascaline, Carvalho, Antônio F., Bouhallab, Saïd
• Tipo de documento: Artigo
• Idioma: eng
• Título da fonte: LOCUS Repositório Institucional da UFV
• Texto Completo: https://doi.org/10.1016/j.foodhyd.2015.02.027; http://www.locus.ufv.br/handle/123456789/22644
• topic: β-Lactoglobulin isoforms; Lactoferrin; Co-assembly; Microspheres; Coacervates

This work reports on the impact of subtle change of protein charge on coacervation and subsequent liquid–liquid phase separation between two oppositely charged globular proteins. For this purpose, a comparative study was conducted on the coacervation of lactoferrin (LF) with the two β-lactoglobulin (β-LG) isoforms. Upon mixing LF with an excess of β-LG, microspheres were formed throughout coacervation under narrow pH range (5.4–6.0). At the optimal pH of coacervation, LF being the limiting partner under tested concentration ranges. The β-LG/LF molar ratio recovered in the formed coacervates varied from 4 to 8 depending on the total protein concentration. Remarkably, LF showed a selective coacervation with isoform A of β-LG as judged by a larger concentration domain for coacervation and a high yield of LF recovered once mixed with β-LG A i.e. 80% against a maximum of 42% with β-LG B. At thermodynamic level, the interaction of LF with both β-LG isoforms exhibited complex exothermic binding isotherms with both enthalpic and entropic contributions.