Characterization of hen phosvitin in aqueous salt solutions: Size, structure, and aggregation. (August 2022)
- Record Type:
- Journal Article
- Title:
- Characterization of hen phosvitin in aqueous salt solutions: Size, structure, and aggregation. (August 2022)
- Main Title:
- Characterization of hen phosvitin in aqueous salt solutions: Size, structure, and aggregation
- Authors:
- Takeuchi, Machi
Mashima, Tsuyoshi
Sztucki, Michael
Petukhov, Andrei V.
Vis, Mark
Friedrich, Heiner
Tuinier, Remco - Abstract:
- Abstract: Phosvitins is a key egg yolk protein and can often be found in food emulsions. It is highly phosphorylated and hence phosvitins contain a large number of negatively charged amino acid groups, for pH > pI. Due to the presence of these phophoserines, phosvitins bind to positively charged multivalent ions. Its amphipolar structure makes phosvitin also an efficient emulsion stabilizer. The ion binding and emulsifying abilities of phosvitins are influenced by environmental conditions such as pH and ionic strength. Various physicochemical properties of phosvitins such as size and charge under various conditions, and how they self-assemble via multivalent ions are not well-understood. To gain more insight into these physical characteristics, we performed high brilliance synchrotron small angle X-ray scattering (SAXS) on phosvitin solutions. The structure factor S ( q ) obtained from the SAXS profiles showed that the double layer interactions between charged phosvitin assemblies are strongly affected by pH and ionic strength of the buffer. The effects of multivalent ions (Mg 2+, Fe 3+ ) on the size and structure of phosvitin were also investigated. Our results revealed that the aggregation of phosvitin mediated by metal ions is induced by electrostatic attraction and only occurs beyond a threshold cation concentration, where phosvitin loses long-range electrostatic double layer repulsions. These findings help understanding the effects of metal ions and pH on phosvitin inAbstract: Phosvitins is a key egg yolk protein and can often be found in food emulsions. It is highly phosphorylated and hence phosvitins contain a large number of negatively charged amino acid groups, for pH > pI. Due to the presence of these phophoserines, phosvitins bind to positively charged multivalent ions. Its amphipolar structure makes phosvitin also an efficient emulsion stabilizer. The ion binding and emulsifying abilities of phosvitins are influenced by environmental conditions such as pH and ionic strength. Various physicochemical properties of phosvitins such as size and charge under various conditions, and how they self-assemble via multivalent ions are not well-understood. To gain more insight into these physical characteristics, we performed high brilliance synchrotron small angle X-ray scattering (SAXS) on phosvitin solutions. The structure factor S ( q ) obtained from the SAXS profiles showed that the double layer interactions between charged phosvitin assemblies are strongly affected by pH and ionic strength of the buffer. The effects of multivalent ions (Mg 2+, Fe 3+ ) on the size and structure of phosvitin were also investigated. Our results revealed that the aggregation of phosvitin mediated by metal ions is induced by electrostatic attraction and only occurs beyond a threshold cation concentration, where phosvitin loses long-range electrostatic double layer repulsions. These findings help understanding the effects of metal ions and pH on phosvitin in more complex environments such as food emulsions. Graphical abstract: Image 1 Highlights: The physicochemical properties of phosvitins such as size and charge were measured using scattering. An improved purification method was developed to prepare high-purity phosvitins. SAXS yielded the structure factor S ( q ), showing phosvitins behave as charged colloidal spheres. Adding multivalent cations can induce aggregation of phosvitins. A threshold cation concentration is needed to initiate phosvitin aggregation. … (more)
- Is Part Of:
- Food hydrocolloids. Volume 129(2022)
- Journal:
- Food hydrocolloids
- Issue:
- Volume 129(2022)
- Issue Display:
- Volume 129, Issue 2022 (2022)
- Year:
- 2022
- Volume:
- 129
- Issue:
- 2022
- Issue Sort Value:
- 2022-0129-2022-0000
- Page Start:
- Page End:
- Publication Date:
- 2022-08
- Subjects:
- Phosvitin -- Small angle X-ray scattering -- Structure factor -- Electrostatic interaction
Hydrocolloids -- Periodicals
Food additives -- Periodicals
Colloïdes -- Périodiques
Aliments -- Additifs -- Périodiques
Colloids
Food additives
Periodicals
Electronic journals
664.06 - Journal URLs:
- http://www.sciencedirect.com/science/journal/0268005X ↗
http://www.elsevier.com/journals ↗ - DOI:
- 10.1016/j.foodhyd.2022.107545 ↗
- Languages:
- English
- ISSNs:
- 0268-005X
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 3977.556000
British Library DSC - BLDSS-3PM
British Library STI - ELD Digital store - Ingest File:
- 21280.xml