Influence of pH and ionic strength on the physicochemical and structural properties of soybean β-conglycinin subunits in aqueous dispersions

Understanding the impact of pH and ionic strength on the physicochemical and structural properties of soy proteins at subunit level is essential for design and fabrication of many plant-based foods. In this study, soybean β-conglycinin and its subunit fractions αα′ and β were dispersed in solutions...

Ausführliche Beschreibung

Gespeichert in:
Bibliographische Detailangaben
Veröffentlicht in:International journal of biological macromolecules 2023-12, Vol.253 (Pt 3), p.126927-126927, Article 126927
Hauptverfasser: Ju, Qian, Wang, Jieru, Zhou, Hualu, Qin, Dingkui, Hu, Xiaoyan, McClements, David Julian, Luan, Guangzhong
Format: Artikel
Sprache:eng
Schlagworte:
Online-Zugang:Volltext
Tags: Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
Beschreibung
Zusammenfassung:Understanding the impact of pH and ionic strength on the physicochemical and structural properties of soy proteins at subunit level is essential for design and fabrication of many plant-based foods. In this study, soybean β-conglycinin and its subunit fractions αα′ and β were dispersed in solutions with different pH values (3.7, 7.6, and 9.0) at low (5 mM NaCl) and high (400 mM NaCl) ionic strengths, respectively. The solubility, rheology, particle size, zeta potential, microstructure, secondary structure, and tertiary structure of the different dispersions were analyzed using a range of analytical methods. The β-conglycinin, αα′- and β-subunits aggregated near the isoelectric point (pH 3.7). Increasing the ionic strength led to the assembly of more homogeneous units. An increase in ionic strength at pH 7.6 and pH 9.0 led to electrostatic screening, which promoted dissociation of the aggregates. The β-subunit showed a greater sensitivity to pH and ionic strength than the αα′-subunits. Based on the evidence from a range of analytical methods, the highly hydrophilic extension region of the αα′-subunits played an important role in determining the stability of the β-conglycinin dispersions under different environmental conditions. Moreover, the N-linked glycans appeared to impact the conformation and aggregation state of the β-conglycinin. [Display omitted] •The influences of pH and ionic strength on the properties of soybean β-conglycinin subunit fractions αα' and β were studied.•At pH 7.6 and 9.0, the increase in ionic strength resulted in the dissociation of the aggregates into trimers or monomers.•The β-subunit showed a greater sensitivity to pH and ionic strength than the αα'-subunits.
ISSN:0141-8130
1879-0003
DOI:10.1016/j.ijbiomac.2023.126927