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通过碱性美拉德反应深入了解大豆11S球蛋白-脱支淀粉共轭物的结构、界面和功能特性。

Insight into the structural, interfacial and functional properties of soybean 11S globulin-debranched starch conjugates through alkaline Maillard reaction.

作者信息

Yang Zhen, Song Yuanyang, Chen Liang, Zhang Weimin, Xie Dan, Jiang Lianzhou, Huang Zhaoxian, Li Dongze

机构信息

School of Food Science and Engineering, Hainan University, Haikou 570228, China.

College of Biology and Food Engineering, Anhui Polytechnic University, Wuhu 241000, China.

出版信息

Carbohydr Polym. 2025 Feb 15;350:123054. doi: 10.1016/j.carbpol.2024.123054. Epub 2024 Nov 22.

Abstract

This study examined the effects of the alkaline Maillard reaction on the structural, interfacial, and functional properties of soybean 11S globulin-debranched starch (DBS) conjugates. The results showed that the degree of DBS binding to 11S globulin was influenced by the polymer ratios, which in turn affected the structural, interfacial, and functional characteristics. The 11S-DBS conjugates with a 2:1 biopolymer ratio exhibited the highest grafting degree, largest zeta potential absolute value, smallest particle size, and greatest thermal stability. Conjugates with higher globulin content demonstrated superior interfacial and functional properties, including improved solubility, increased surface hydrophobicity, and reduced interfacial tension. 3D fluorescence scanning revealed a decrease in the signal of aromatic amino acid residues, while microstructural observation provided insights into the binding behavior of different 11S-DBS conjugates. Molecular docking simulations highlighted the key role of hydrogen bonding in the formation of these conjugates. This study enhances understanding of soybean globulin-polysaccharide interaction mechanisms, expanding their potential applications in the food, medical, and bioengineering industries.

摘要

本研究考察了碱性美拉德反应对大豆11S球蛋白-脱支淀粉(DBS)共轭物的结构、界面和功能性质的影响。结果表明,DBS与11S球蛋白的结合程度受聚合物比例的影响,进而影响其结构、界面和功能特性。生物聚合物比例为2:1的11S-DBS共轭物表现出最高的接枝度、最大的ζ电位绝对值、最小的粒径和最大的热稳定性。球蛋白含量较高的共轭物表现出优异的界面和功能性质,包括改善的溶解性、增加的表面疏水性和降低的界面张力。三维荧光扫描显示芳香族氨基酸残基的信号减弱,而微观结构观察为不同11S-DBS共轭物的结合行为提供了见解。分子对接模拟突出了氢键在这些共轭物形成中的关键作用。本研究增进了对大豆球蛋白-多糖相互作用机制的理解,拓展了它们在食品、医学和生物工程行业的潜在应用。

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