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pH-Dependent Binding Behavior of the α-Lactalbumin/Glycyrrhizic Acid Complex in Relation to Their Foaming Characteristics in Bulk.

Ruijie ShiYue LiuYue MaPanpan ZhaoZhanmei JiangJuncai Hou
Published in: Journal of agricultural and food chemistry (2022)
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.
Keyphrases
  • pet ct
  • risk assessment
  • transcription factor
  • climate change
  • binding protein
  • dna binding
  • human health