Interaction between Bovine Serum Albumin in Fresh Milk Cream and Encapsulated and Non-Encapsulated Polyphenols of Tamarillo.

Abstract

The fortification of dairy products with polyphenols is known to deliver additional health benefits. However, interactions between polyphenols may form complexes and cause a loss of functionality overall. This study aimed to investigate potential interactions between polyphenols, in encapsulated and non-encapsulated forms, extracted from tamarillo fruit and bovine serum albumin (BSA) from fresh milk cream. Fortification with tamarillo extract was made at 1, 2 and 3% (w/w), and the resultant changes in physicochemical, rheological and functional properties were studied. With an increase in fortification, the absorbance of protein-ligand in the protein-polyphenol complex was decreased by up to 55% and 67% in UV and fluorescent intensities, respectively. Chlorogenic acid and kaempferol-3-rutinoside were more affected than delphinidin-3-rutinoside and pelargonidin-3-rutinoside. Static quenching was the main mechanism in the fluorescence spectra. Tryptophan and tyrosine residues were the two major aromatic amino acids responsible for the interactions with BSA. There were at least three binding sites near the tryptophan residue on BSA. The rheological property remained unaffected after the addition of non-encapsulated tamarillo extracts. Antioxidant capacity was significantly decreased (p < 0.05) after the addition of encapsulated extracts. This may be explained by using a low concentration of maltodextrin (10% w/w) as an encapsulating agent and its high binding affinity to milk proteins.