Related Experiment Video
Updated: Oct 3, 2025

Study of Short Peptide Adsorption on Solution Dispersed Inorganic Nanoparticles Using Depletion Method
Published on: April 11, 2020
pH-Dependent Binding Behavior of the α-Lactalbumin/Glycyrrhizic Acid Complex in Relation to Their Foaming
Ruijie Shi1, Yue Liu1, Yue Ma1
1Key Laboratory of Dairy Science, Ministry of Education, Northeast Agricultural University, Harbin 150030, P. R. China.
Abstract:
This work aimed to understand the relationships of the interaction mechanism and foaming characteristics of α-lactalbumin (α-La) and glycyrrhizic acid (GA) after acidic (pH 2.5) and neutral (pH 7.0) treatment. The critical aggregation concentration (CAC) of GA in the presence of α-La was 0.6 mM at pH 7.0, while it was 1.0 mM at pH 2.5. Also, in the presence of a GA concentration of 0-15.00 mM, more GA molecules combined onto the α-La surface at pH 2.5 than at pH 7.0, as evident from the binding isotherms. The turbidity and particle size of α-La/GA were greater in acidic solution than those under neutral conditions. This result could be interpreted by the formation of aggregates under higher GA concentration at pH 2.5. Meanwhile, the viscosity of the complex was higher at pH 2.5 than at pH 7.0 in the presence of 3.00-15.00 mM GA, as analyzed from the rheological properties. The foaming ability (FA) of α-La was significantly enhanced in the presence of 10.00 mM GA. Simultaneously, acidic solution could generate a more stable foaming system with a thicker film layer stabilized by the complex compared with neutral solution. These findings could be beneficial for developing a kind of acidic food-grade foaming agent.
Related Concept Videos
Factors Affecting Protein-Drug Binding: Protein-Related Factors
The physicochemical properties of a drug play a significant role in its ability to bind to proteins. Lipophilic drugs, which dissolve in fats, oils, and lipids, can be...
Factors Affecting Protein-Drug Binding: Drug-Related Factors
One crucial factor in drug-protein binding is the drug's lipophilicity or its affinity for fat. More lipophilic drugs tend to have higher binding extents. For example, highly lipophilic drugs like cloxacillin exhibit substantial protein binding, with as much as 95% of the drug binding to proteins. In...
Drug Distribution: Plasma Protein Binding
Drug Binding to Blood Components
HSA is the most abundant plasma protein and is vital in drug binding. It contains distinct drug-binding sites, with different drugs exhibiting affinity for specific sites. There are three main drug-binding domains for HSA: sites I, II, and III. These domains are...
Factors Affecting Protein-Drug Binding: Patient-Related Factors
Age stands as a key determinant in protein-drug binding. Neonates, characterized by low albumin content, experience heightened concentrations of unbound drugs such as phenytoin and...
Factors Affecting Protein-Drug Binding: Drug Interactions
Displacement interactions can have varying outcomes, ranging from toxicity to virtually...

