文献类型：期刊文献

英文题名：Molecular weight of fucoidan governs its interaction with ovalbumin: Multi-scale insights into complex formation, structural alteration, and binding mechanism

作者：Wu, Yingmei[1]; Sun, Yingying[1]; Xu, Longquan[2]; Geng, Fang[4]; Li, Xin[1]; Ai, Chao[3]; Chen, Lei[3]; Zhou, Yan[1]; Luo, Peng[1]; Huang, Qun[1]

机构：[1] School of Public Health, The Key Laboratory of Environmental Pollution Monitoring and Disease Control, Ministry of Education, Guizhou Province Engineering Research Center of Health Food Innovative Manufacturing, Guizhou Medical University, Guiyang, 561113, China; [2] Technology Center of China Tobacco Guizhou Industrial Co. Ltd., Guiyang, 550000, China; [3] College of Food Science and Technology, Guangdong Ocean University, Guangdong Provincial Key Laboratory of Aquatic Product Processing and Safety, Guangdong Province Engineering Laboratory for Marine Biological Products, Guangdong Provincial Engineering Technology Research Center of Seafood, Key Laboratory of Advanced Processing of Aquatic Product of Guangdong Higher Education Institution, Zhanjiang, 524088, China; [4] Institute for Egg Science and Technology, School of Food and Biological Engineering, Chengdu University, Chengdu, 610106, China

年份：2026

卷号：181

外文期刊名：Food Hydrocolloids

收录：EI(收录号：20262520944642)、Scopus(收录号：2-s2.0-105042060725)

语种：英文

外文关键词：Binding energy - Charge density - Complexation - Conformations - Hydrogen bonds - Particle size - Particle size analysis - Proteins - Scales (weighing instruments) - Shear thinning - Sulfur compounds

外文摘要：The molecular structural characteristics of polysaccharides decisively influence their interactions with proteins. This study systematically investigated the mechanism by which the molecular weight (Mw) of fucoidan (FUC) affected its interaction with ovalbumin (OVA). The complexes were characterized using a multi-scale approach. Results indicated that the low Mw HUF fraction (2.43?×?104?Da), characterized by higher charge density and flexible chain conformation, formed the most stable complex with OVA at a 3:1 mass ratio, exhibiting the highest turbidity, smallest particle size, significantly enhanced surface hydrophobicity, and typical shear-thinning behavior. CLSM observations visually revealed differences in the microstructures of complexes formed by polysaccharides of varying Mw. FT-IR and fluorescence spectroscopy analysis indicated significant changes in the secondary and tertiary structures of OVA during complexation. ITC analysis confirmed that the binding process between OVA and HUF was enthalpy-driven, exhibiting the strongest binding affinity (Kd?=?6.52?×?10?5?M). Molecular docking revealed that sulfate groups on FUC engaged key positive residues on OVA via salt bridges and hydrogen bonds. These findings elucidate Mw and charge density as decisive factors in protein-polysaccharide interactions, providing a foundation for designing functional composites in food and biomaterials. ? 2026 Elsevier Ltd. All rights are reserved, including those for text and data mining, AI training, and similar technologies.