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Updated: Sep 20, 2025
Measuring Enzymatic Stability by Isothermal Titration Calorimetry
Published on: March 26, 2019
Characterization of OSA-starch/tea polyphenol complexes with enhanced oil-water interfacial properties by molecular
Lidan Pan1, Xiaorui Liu1, Die Dong1
1Shandong Key Laboratory of Healthy Food Resources Exploration and Creation, Qilu University of Technology (Shandong Academy of Sciences), Jinan 250353, China; School of Food Science and Engineering, Qilu University of Technology (Shandong Academy of Sciences), Jinan 250353, China; State Key Laboratory of Biobased Material and Green Papermaking, Qilu University of Technology (Shandong Academy of Sciences), Jinan 250353, China.
Abstract:
Modifying the structure of natural emulsifiers can significantly alter their bulk properties and interfacial behavior. In this study, the binding mechanisms and interfacial adsorption of octenyl succinic anhydride starch (OSA-starch)/ epigallocatechin-3-gallate (EGCG) complexes were investigated for developing functional emulsifiers. Molecular dynamics simulations and isothermal titration calorimetry demonstrated that OSA-starch and EGCG interacted via van der Waals forces, electrostatic interactions, and hydrogen bonding. With EGCG concentrations increased from 0.05 % to 0.20 %, the number of hydrogen bonds between OSA-starch and EGCG changed from 8 to 26. The improved oil-water interfacial properties were evidenced by contact angle measurements and dynamic interfacial tension analysis. Specifically, when EGCG concentration was 0.05 %, the contact angle of the OSA-starch/EGCG complexes was increased to 71.29°, while the interfacial diffusion rate was rose to 0.0252 mN m-1 s-1/2. The structural features and interfacial behaviors of OSA-starch/EGCG complexes were closely interconnected, offering significant insights into the regulation of interfaces.
