Whey protein - folic acid complexes: formation, isolation and bioavailability in a Lactobacillus casei model.

ROCIO CORFIELD; KARINA D. MARTÍNEZ; MARIANA C.ALLIEVI; PATRICIO SANTAGAPITA; FLORENCIA MAZZOBRE; CAROLINA SCHEBOR; OSCAR E.PÉREZ

Food Structure

Elsevier

Lugar: Amsterdam; Año: 2020

2213-3291

The objective of this work was to explore the wheyproteins - folic acid (FA) ((β-lactoglobulin (β-lg) and a whey protein isolate(WPI) complexes formation via complexation at pH3.0. Complexes were formed through non-covalentinteractions, mainly electrostatic, as showed by ƺ-potentialdetermination. Whey proteinaggregation induced by the FA linkage was achieved, with particle sizes withinthe nano and microscales. Particle size distributionin aqueous solution was determined by dynamic light scattering (DLS) obtainingvalues between 15-200 nm. Complexes isolation was achieved by spontaneousphase separation and subsequent lyophilization, obtaining a glassy powder.Particles sizes increased upon both complexation and powder rehydration. Theinteractions between FA and proteins were corroborated by FTIR. Confocal lasermicroscopy revealed the heterogeneity and extensive aggregation upon complexation. Thebioavailability of the WPI-FA and β-lg-FA complexes, evaluated by Lactobacilluscasei BL23 model, was similar to that of FA alone demonstrating that thesecomplexes can be potentially used as a new functional protein-based ingredient.