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Molecular interactions involved in the complexation process between buffalo whey proteins concentrate and folic acid.
Bustos, Leandro Fabián; Judis, María Alicia; Vasile, Franco Emanuel; Pérez, Oscar Edgardo.
Affiliation
  • Bustos LF; Universidad Nacional del Chaco Austral & CONICET - Instituto de investigaciones en procesos tecnológicos avanzados (INIPTA), Comandante Fernández 755, Presidencia Roque Sáenz Peña 3700, Chaco, Argentina; Universidad de Buenos Aires, Facultad de Ciencias Exactas y Naturales, Departamento de Quími
  • Judis MA; Universidad Nacional del Chaco Austral & CONICET - Instituto de investigaciones en procesos tecnológicos avanzados (INIPTA), Comandante Fernández 755, Presidencia Roque Sáenz Peña 3700, Chaco, Argentina. Electronic address: majudis@uncaus.edu.ar.
  • Vasile FE; Universidad Nacional del Chaco Austral & CONICET - Instituto de investigaciones en procesos tecnológicos avanzados (INIPTA), Comandante Fernández 755, Presidencia Roque Sáenz Peña 3700, Chaco, Argentina. Electronic address: francovasile@uncaus.edu.ar.
  • Pérez OE; Universidad de Buenos Aires, Facultad de Ciencias Exactas y Naturales, Departamento de Química Biológica & CONICET-Universidad de Buenos Aires, Laboratorio Interdisciplinario de Dinámica Celular y Nano-Herramientas, Intendente Güiraldes 2160, CP 1428, Buenos Aires, Argentina. Electronic address:
Food Chem ; 396: 133734, 2022 Dec 01.
Article in En | MEDLINE | ID: mdl-35870246
ABSTRACT
Using buffalo whey proteins as carrier agents of sensitive molecules raises an interesting approach allowing adding value and minimizing the pollution impact of this by-product. In this context, this work aims to explore the molecular interactions between buffalo whey proteins concentrate (BWPC) and folic acid (FA). For this purpose, fluorescence, UV and FTIR analysis were performed on aqueous or solid dispersions of a buffalo whey protein concentrate (5 µM) (BWPC), with variable concentrations (0-20 µM) of FA. Fluorescence and absorption data were fitted by Stern-Volmer, Beckett, Förster resonance energy transfer, and sphere-of-action models (R2 > 0.9). Derived results suggest that BWPC strongly bind to FA through non-covalent interactions and form ground-state complexes. Additionally, BWPC improves the photostability of FA against UV radiation, and chemical denaturation negatively affects the binding properties. Obtained results encourage further studies of BWPC as carrier agents, which could promote innovative applications for this under-utilized proteins source.
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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Whey Proteins / Folic Acid Type of study: Prognostic_studies Limits: Animals Language: En Journal: Food Chem Year: 2022 Document type: Article

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Whey Proteins / Folic Acid Type of study: Prognostic_studies Limits: Animals Language: En Journal: Food Chem Year: 2022 Document type: Article