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机制洞察枸杞多糖与乳清蛋白分离物的相互作用:功能和结构表征。

Mechanistic insights into the interaction of Lycium barbarum polysaccharide with whey protein isolate: Functional and structural characterization.

机构信息

College of Food and Bioengineering, Fujian Polytechnic Normal University, Fuqing, Fujian, China; Fujian Province-Indonesia Marine Food Joint Research and Development Center, College of Food and Bioengineering, Fujian Polytechnic Normal University, Fuqing, Fujian, China.

College of Food and Bioengineering, Fujian Polytechnic Normal University, Fuqing, Fujian, China.

出版信息

Food Chem. 2025 Jan 15;463(Pt 1):141080. doi: 10.1016/j.foodchem.2024.141080. Epub 2024 Sep 1.

DOI:10.1016/j.foodchem.2024.141080
PMID:39332052
Abstract

Protein-polysaccharide interactions are crucial for food system structure and stability. This study investigates the interaction of Lycium barbarum polysaccharide (LBP) at 0-2.00 % concentrations with whey protein isolate (WPI), focusing on functionality and structural changes. LBP covalently grafted onto WPI, as confirmed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), forming WPI-LBP complexes with a maximum degree of grafting (DG) of 44.58 % at 2.00 % LBP. This grafting reduced WPI's surface hydrophobicity (H) and improved solubility, emulsifying properties, and digestibility under certain conditions, with optimal antioxidant activity at 1.00 % LBP. Multispectral analysis and microscopy showed LBP grafting alters WPI's secondary, tertiary, crystalline, and micro/nanostructures. The comprehensive analysis indicates that the interaction between LBP and WPI involves covalent bonding, hydrogen bonding, hydrophobic interactions, and electrostatic forces, as supported by zeta potential and chemical forces results. These findings suggest LBP-protein complexes as promising food materials for enhancing functionality and stability in the food industry.

摘要

蛋白质-多糖相互作用对食品体系的结构和稳定性至关重要。本研究以乳清蛋白分离物(WPI)为对象,探讨了 0-2.00%浓度下枸杞多糖(LBP)与 WPI 的相互作用,重点关注其功能和结构变化。通过十二烷基硫酸钠-聚丙烯酰胺凝胶电泳(SDS-PAGE)证实,LBP 与 WPI 发生了共价结合,在 2.00%LBP 浓度下形成了最大接枝程度(DG)为 44.58%的 WPI-LBP 复合物。这种接枝降低了 WPI 的表面疏水性(H),并提高了其在一定条件下的溶解度、乳化性能和消化率,在 1.00%LBP 时具有最佳的抗氧化活性。多光谱分析和显微镜观察表明,LBP 的接枝改变了 WPI 的二级、三级、结晶和微/纳米结构。综合分析表明,LBP 与 WPI 之间的相互作用涉及共价键、氢键、疏水相互作用和静电力,这得到了zeta 电位和化学力结果的支持。这些发现表明,LBP-蛋白质复合物有望成为增强食品工业中功能性和稳定性的有前途的食品材料。

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