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Characterization and mechanism of formation of fibrous and worm-like β-lactoglobulin self-assemblies

文献类型： 外文期刊

作者： Yuan, Jianhua 1 ; Wu, Ying 1 ; Shi, Yucong 1 ; Zhou, Lei 1 ; Zhang, Yanjun 2 ; Liu, Chengmei 1 ; Zhong, Junzhen 1 ;

作者机构： 1.Nanchang Univ, State Key Lab Food Sci & Resources, 235 Nanjing East Rd, Nanchang 330047, Jiangxi, Peoples R China

2.Chinese Acad Trop Agr Sci, Spice & Beverage Res Inst, Wanning, Hainan, Peoples R China

关键词： beta-lactoglobulin; disulfide bonding; formation mechanism; relevance analysis; self-assembly

期刊名称：JOURNAL OF FOOD SCIENCE （ 影响因子：3.4； 五年影响因子：4.1 ）

ISSN： 0022-1147

年卷期： 2025 年 90 卷 3 期

页码：

收录情况： SCI

摘要： In this study, a series of characterizations and analyses of fibrous beta-lactoglobulin self-assembly (FBS) and worm-like beta-lactoglobulin self-assembly (WBS) were carried out to investigate the key factors for the formation of self-assemblies of beta-lactoglobulin under two different induced conditions. Compared with natural beta-lactoglobulin, FBS was always positively charged, increasing to 9.69 mV when heated for 10 h, whereas WBS was always negatively charged, decreasing to -20.73 mV when heated for 20 min. Electrostatic interactions play a crucial role in the formation of both FBS and WBS. The free sulfhydryl content decreased by 10.4% at 20 min of heating compared with that at 1 min of heating. beta-Lactoglobulin converted the exposed free sulfhydryl groups to disulfide bonds when heated under neutral conditions, and disulfide bonds played a key role in the formation of WBS. The surface hydrophobicity of FBS reached its maximum at 1 h of heating, while that of WBS reached its maximum at 15 min of heating. The hydrophobic interactions played an extremely important role in the formation of the two self-assemblies. The investigation of the formation mechanism of FBS and WBS is of great significance for the preparation of beta-lactoglobulin self-assembled gels.

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