Adsorption kinetics and dilatational rheological properties of recombinant Pea Albumin-2 at the oil-water interface. (November 2021)
- Record Type:
- Journal Article
- Title:
- Adsorption kinetics and dilatational rheological properties of recombinant Pea Albumin-2 at the oil-water interface. (November 2021)
- Main Title:
- Adsorption kinetics and dilatational rheological properties of recombinant Pea Albumin-2 at the oil-water interface
- Authors:
- Luo, Yilun
Zheng, Wei
Shen, Qian
Zhang, Li
Tang, Cuie
Song, Rong
Liu, Shilin
Li, Bin
Chen, Yijie - Abstract:
- Abstract: To investigate the adsorption kinetics and dilatational rheological properties of Pea Albumin-2 (PA-2) at the oil-water interface, recombinant PA-2 was expressed and purified. Our native-PAGE, SDS-PAGE, and homology modeling results indicated that PA-2, a kind of globular protein, could form dimers by non-covalent interactions rather than disulfide bonds. The TEM results showed that some PA-2 proteins could form aggregates with the size of around 2–3 μm. Unlike other globular proteins, PA-2 exhibited the non-monotonic kinetic dependency of the dynamic viscoelastic modulus (E). Besides, the rate of rearrangement ( k R ) of PA-2 was significantly higher than that of other typical food proteins. Our results demonstrated that PA-2 could adsorb to the oil-water interface in the form of aggregates. The addition of 2-ME (β-mercaptoethanol) would impact dilatational rheological properties of PA-2, leading to disaggregation and higher rearrangement of PA-2 protein aggregates at the oil-water interface. Our data offered more information on the interfacial dynamic properties of globular proteins, and provided a new insight to the conformational changes of globular proteins at the oil-water interface, basing on their dynamic viscoelastic behaviors. Graphical abstract: Image 1 Highlights: PA-2 could adsorb to the oil-water interface in the form of aggregations. PA-2 exhibits a non-monotonic kinetic dependency of the viscoelastic modulus (E). PA-2 with β-mercaptoethanolAbstract: To investigate the adsorption kinetics and dilatational rheological properties of Pea Albumin-2 (PA-2) at the oil-water interface, recombinant PA-2 was expressed and purified. Our native-PAGE, SDS-PAGE, and homology modeling results indicated that PA-2, a kind of globular protein, could form dimers by non-covalent interactions rather than disulfide bonds. The TEM results showed that some PA-2 proteins could form aggregates with the size of around 2–3 μm. Unlike other globular proteins, PA-2 exhibited the non-monotonic kinetic dependency of the dynamic viscoelastic modulus (E). Besides, the rate of rearrangement ( k R ) of PA-2 was significantly higher than that of other typical food proteins. Our results demonstrated that PA-2 could adsorb to the oil-water interface in the form of aggregates. The addition of 2-ME (β-mercaptoethanol) would impact dilatational rheological properties of PA-2, leading to disaggregation and higher rearrangement of PA-2 protein aggregates at the oil-water interface. Our data offered more information on the interfacial dynamic properties of globular proteins, and provided a new insight to the conformational changes of globular proteins at the oil-water interface, basing on their dynamic viscoelastic behaviors. Graphical abstract: Image 1 Highlights: PA-2 could adsorb to the oil-water interface in the form of aggregations. PA-2 exhibits a non-monotonic kinetic dependency of the viscoelastic modulus (E). PA-2 with β-mercaptoethanol treatment exhibits higher conformational flexibility. The increasing conformational flexibility improves the interfacial rearrangement. The high viscoelastic modulus (E) is mainly provided by rigid globular monomer. … (more)
- Is Part Of:
- Food hydrocolloids. Volume 120(2021)
- Journal:
- Food hydrocolloids
- Issue:
- Volume 120(2021)
- Issue Display:
- Volume 120, Issue 2021 (2021)
- Year:
- 2021
- Volume:
- 120
- Issue:
- 2021
- Issue Sort Value:
- 2021-0120-2021-0000
- Page Start:
- Page End:
- Publication Date:
- 2021-11
- Subjects:
- Pea -- Albumin-2 -- Adsorption dynamics -- Dilatational rheological properties -- Oil-water interface
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.2021.106866 ↗
- 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:
- 17535.xml