Abstract Title:

Influence of moderate electric fields inβ-lactoglobulin thermal unfolding and interactions.

Abstract Source:

Food Chem. 2020 Jan 30 ;304:125442. Epub 2019 Aug 28. PMID: 31491714

Abstract Author(s):

Rui M Rodrigues, Zita Avelar, António A Vicente, Steffen B Petersen, Ricardo N Pereira

Article Affiliation:

Rui M Rodrigues


In this study, the effects of moderate electric fields during thermal denaturation ofβ-lactoglobulin were examined through an in situ circular dichroism approach, complemented by intrinsic extrinsic fluorescence analysis. Results have shown that the effects of electric fields in protein unfolding were linearly dependent on the applied electric field intensity (V/cm) and increased by the use of low electric frequencies - i.e. 50 to 200 Hz. These electric effects caused significant changes on β-lactoglobulin melting temperature, unfolded conformation and subsequent intermolecular interactions, revealed by the increase of surface hydrophobicity (ANS affinity) and higher conservation of retinol binding. The obtained data provides a clear evidence that moderate electric fields contribute to distinct folding/unfolding of β-lactoglobulin, resulting in structural modifications. These findings are relevant for (bio)-technological applications involving electric fields processing, bringing new insights for the development of innovative strategies to control protein function and tune production of functional protein systems.

Study Type : Human Study

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