Related Experiment Video
Updated: Jan 8, 2026

Composition and Properties of Aquafaba: Water Recovered from Commercially Canned Chickpeas
Published on: February 10, 2018
pH Cycling-Induced Formation of Chickpea Protein-Casein Dual-Protein Complexes: Interaction Mechanisms, Structure,
Wenjing Dong1, Xiuxiu Teng1, Shiyu Lin1
1College of Food Science and Engineering, Tianjin University of Science & Technology, Tianjin 300457, P. R. China.
None:
Single proteins have certain limitations in terms of functional properties, while composite products combining plant and animal proteins offer a practical and sustainable strategy to address this issue. This study aims to establish a dual-protein complex, the pH cycling-induced chickpea protein (CP)-casein (CA) complex (pH-CP/CA), to load curcumin and enhance its functionality. Results showed that pH-CP/CA (CP/CA = 2:1, mass ratio) exhibited a smaller particle size and a higher absolute value of zeta potential. Hydrogen-bonding, electrostatic, and hydrophobic interactions drove the pH-CP/CA formation, resulting in improved solubility, emulsification, foaming, and thermal stability. Curcumin (Cur) was loaded in pH-CP/CA through pH cycling to construct the Cur-containing complex (pH-CP/CA-Cur). The pH-CP/CA-Cur achieved an encapsulation efficiency of 83.04% (w/w) and exhibited enhanced stability compared with Cur. Furthermore, its bioavailability reached 85.82% in the simulated digestion. This study demonstrates the role of pH cycling in fabricating dual-protein complexes and establishes their potential as nanocarriers for bioactive molecules.
More Related Videos
04:58Author Spotlight: Investigating Lens Development and Function Through Microinjection of RCAS(A) Retrovirus in Embryonic Chicken Lens
Published on: September 1, 2023
08:48Development of a Backbone Cyclic Peptide Library as Potential Antiparasitic Therapeutics Using Microwave Irradiation
Published on: January 26, 2016
Related Concept Videos
Positive Regulator Molecules
Allosteric Proteins-ATCase
Aspartate transcarbamoylase (ATCase) is a cytosolic enzyme that catalyzes the condensation of L-aspartate and carbamoyl phosphate to N-carbamoyl-L-aspartate. This reaction is the first step in pyrimidine biosynthesis. UTP and CTP, the end products of the pyrimidine synthesis...
Chirality in Nature
Protein Folding
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
Protein Folding
Protein Complexes with Interchangeable Parts
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order...