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Influence of pH and ionic strength on the physicochemical and structural properties of soybean ß-conglycinin subunits in aqueous dispersions.
Ju, Qian; Wang, Jieru; Zhou, Hualu; Qin, Dingkui; Hu, Xiaoyan; McClements, David Julian; Luan, Guangzhong.
Afiliação
  • Ju Q; College of Food Science and Engineering, Northwest A&F University, Yangling 712100, China; Shaanxi Union Research Center of University and Enterprise for Grain Processing Technologies, Yangling, China; Biopolymers and Colloids Laboratory, Department of Food Science, University of Massachusetts,
  • Wang J; College of Food Science and Engineering, Northwest A&F University, Yangling 712100, China; Shaanxi Union Research Center of University and Enterprise for Grain Processing Technologies, Yangling, China.
  • Zhou H; Department of Food Science and Technology, College of Agricultural and Environmental Sciences, University of Georgia, Griffin, GA 30223, USA.
  • Qin D; Biopolymers and Colloids Laboratory, Department of Food Science, University of Massachusetts, Amherst, MA 01003, USA.
  • Hu X; Biopolymers and Colloids Laboratory, Department of Food Science, University of Massachusetts, Amherst, MA 01003, USA.
  • McClements DJ; Biopolymers and Colloids Laboratory, Department of Food Science, University of Massachusetts, Amherst, MA 01003, USA. Electronic address: mcclements@foodsci.umass.edu.
  • Luan G; College of Food Science and Engineering, Northwest A&F University, Yangling 712100, China; Shaanxi Union Research Center of University and Enterprise for Grain Processing Technologies, Yangling, China. Electronic address: qlgz@nwsuaf.edu.cn.
Int J Biol Macromol ; 253(Pt 3): 126927, 2023 Dec 31.
Article em En | MEDLINE | ID: mdl-37717873
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 ß-conglycinin and its subunit fractions αα' and ß 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 ß-conglycinin, αα'- and ß-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 ß-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 ß-conglycinin dispersions under different environmental conditions. Moreover, the N-linked glycans appeared to impact the conformation and aggregation state of the ß-conglycinin.
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Texto completo: 1 Base de dados: MEDLINE Assunto principal: Proteínas de Soja / Globulinas Idioma: En Ano de publicação: 2023 Tipo de documento: Article

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Proteínas de Soja / Globulinas Idioma: En Ano de publicação: 2023 Tipo de documento: Article