Tracking the driving forces for the unfolding and folding of kidney bean protein isolates: Revealing mechanisms of dynamic changes in structure and function. (15th February 2023)
- Record Type:
- Journal Article
- Title:
- Tracking the driving forces for the unfolding and folding of kidney bean protein isolates: Revealing mechanisms of dynamic changes in structure and function. (15th February 2023)
- Main Title:
- Tracking the driving forces for the unfolding and folding of kidney bean protein isolates: Revealing mechanisms of dynamic changes in structure and function
- Authors:
- Yan, Xinyue
Jia, Yijia
Man, Hui
Sun, Shiyan
Huang, Yuyang
Qi, Baokun
Li, Yang - Abstract:
- Graphical abstract: Highlights: The pH-shifting is irreversible, causes KPI depolymerization and rearrangement. Alkaline-shifting disrupts hydrogen bonds and electrostatic interactions of KPI. Acidic-shifting disrupts intermolecular hydrophobic interactions of KPI. Both acidic- and alkaline-shifting improve structures and functionalities of KPI. Abstract: Tracking the dynamic changes in the structure of kidney bean protein isolate (KPI) during extreme pH-shifting can reveal the different mechanisms that drive the unfolding and refolding of the protein from a conformational perspective and elucidate the relationship between its structure and function. The secondary and tertiary structures of KPI were analyzed using multispectral techniques. The results showed that acidic-shifting affected the hydrophobic interactions of KPI molecules, whereas alkaline-shifting affected hydrogen bonding and electrostatic interactions of the molecules. Therefore, alkaline-shifting was more likely to affect KPI conformation. SEM revealed that pH-shifting transformed the sheet structure of KPI into spheres and rods; moreover, it improved the surface hydrophobicity, thermal stability, emulsification, foaming, and antioxidant properties of KPI. In summary, each pH-shifting stage disrupts a different intermolecular force, resulting in protein conformational diversity, while structural changes further affect function. Therefore, pH-shifting treatment broadens the applications scope of KPI in the foodGraphical abstract: Highlights: The pH-shifting is irreversible, causes KPI depolymerization and rearrangement. Alkaline-shifting disrupts hydrogen bonds and electrostatic interactions of KPI. Acidic-shifting disrupts intermolecular hydrophobic interactions of KPI. Both acidic- and alkaline-shifting improve structures and functionalities of KPI. Abstract: Tracking the dynamic changes in the structure of kidney bean protein isolate (KPI) during extreme pH-shifting can reveal the different mechanisms that drive the unfolding and refolding of the protein from a conformational perspective and elucidate the relationship between its structure and function. The secondary and tertiary structures of KPI were analyzed using multispectral techniques. The results showed that acidic-shifting affected the hydrophobic interactions of KPI molecules, whereas alkaline-shifting affected hydrogen bonding and electrostatic interactions of the molecules. Therefore, alkaline-shifting was more likely to affect KPI conformation. SEM revealed that pH-shifting transformed the sheet structure of KPI into spheres and rods; moreover, it improved the surface hydrophobicity, thermal stability, emulsification, foaming, and antioxidant properties of KPI. In summary, each pH-shifting stage disrupts a different intermolecular force, resulting in protein conformational diversity, while structural changes further affect function. Therefore, pH-shifting treatment broadens the applications scope of KPI in the food industry. … (more)
- Is Part Of:
- Food chemistry. Volume 402(2023)
- Journal:
- Food chemistry
- Issue:
- Volume 402(2023)
- Issue Display:
- Volume 402, Issue 2023 (2023)
- Year:
- 2023
- Volume:
- 402
- Issue:
- 2023
- Issue Sort Value:
- 2023-0402-2023-0000
- Page Start:
- Page End:
- Publication Date:
- 2023-02-15
- Subjects:
- Kidney bean protein isolate -- pH-shifting -- Driving force -- Dynamic changes -- Spatial conformation -- Functional properties
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.2022.134230 ↗
- 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
British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 24107.xml