Title
Electric field effects on β-lactoglobulin thermal unfolding as a function of pH – Impact on protein functionality
Author
Rui M. Rodrigues, António A. Vicente, Steffen B. Petersen, Ricardo N. Pereira
Year
2019
Journal
Innovative Food Science & Emerging Technologies
Abstract
The presence of moderate electric fields (MEF) during ohmic heating (OH) treatment of whey protein systems have demonstrated potential to change physicochemical and functional properties, like aggregation rate and extension or viscoelastic behaviour. However, the specific action of MEF upon the molecular structure of proteins, particularly during thermal processing has yet to be clarified. The effects of MEF in pure fractions of β-lactoglobulin (β-lg) under non-aggregating conditions (low concentration and ionic strength), were investigated in this work. Protein samples were identically heat-treated through conventional and OH methods and at different pH values. β-lg's structural features were characterized by evaluation of secondary structure distribution and local conformational changes using techniques such as circular dichroism, intrinsic and extrinsic fluorescenceand free thiol groups reactivity. It was confirmed that MEF affects β-lg upon thermal unfolding, resulting in distinctive structural features, surface hydrophobicity and SH reactivity. The mechanism of action is probably related with the molecular motion induced by the oscillating electric field and is more pronounced at neutral pH, where β-lg is more susceptible to thermal structural changes. These results contribute to a better understanding of OH processing and its effects in food matrices reinforce the possibility of using MEF as a toll to change protein functionality.
Instrument
J-1500
Keywords
Circular dichroism, Secondary structure, Chemical stability, Biochemistry