Influence of moderate electric fields in β-lactoglobulin thermal unfolding and interactions. (30th January 2020)
- Record Type:
- Journal Article
- Title:
- Influence of moderate electric fields in β-lactoglobulin thermal unfolding and interactions. (30th January 2020)
- Main Title:
- Influence of moderate electric fields in β-lactoglobulin thermal unfolding and interactions
- Authors:
- Rodrigues, Rui M.
Avelar, Zita
Vicente, António A.
Petersen, Steffen B.
Pereira, Ricardo N. - Abstract:
- Abstract: In this study, the effects of moderate electric fields during thermal denaturation of β-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. Highlights: Thermal unfolding of β-lactoglobulin was affected by moderate electric field processing. Structural changes of β-lactoglobulin were assessed by an in situ circular dichroism analysis. Moderate electric fields change protein structure and subsequent molecular interactions. Structural changes were dependent of electric field strength andAbstract: In this study, the effects of moderate electric fields during thermal denaturation of β-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. Highlights: Thermal unfolding of β-lactoglobulin was affected by moderate electric field processing. Structural changes of β-lactoglobulin were assessed by an in situ circular dichroism analysis. Moderate electric fields change protein structure and subsequent molecular interactions. Structural changes were dependent of electric field strength and frequency. … (more)
- Is Part Of:
- Food chemistry. Volume 304(2020)
- Journal:
- Food chemistry
- Issue:
- Volume 304(2020)
- Issue Display:
- Volume 304, Issue 2020 (2020)
- Year:
- 2020
- Volume:
- 304
- Issue:
- 2020
- Issue Sort Value:
- 2020-0304-2020-0000
- Page Start:
- Page End:
- Publication Date:
- 2020-01-30
- Subjects:
- β-Lactoglobulin -- Moderate electric fields -- Thermal denaturation -- Proteins structure -- Protein interactions
Food -- Analysis -- Periodicals
Food -- Composition -- Periodicals
664 - Journal URLs:
- http://www.sciencedirect.com/science/journal/03088146 ↗
http://www.elsevier.com/journals ↗ - DOI:
- 10.1016/j.foodchem.2019.125442 ↗
- Languages:
- English
- ISSNs:
- 0308-8146
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 3977.284000
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