Comparison in structure, physicochemical and emulsifying properties of alpha lactoglobulin and beta lactalbumin exposed to prior γ-oryzanol by the multi-spectroscopic and silico methods

被引：2

作者：

Huang, Qiang ^{[1
]}

Mu, Zhishen ^{[2
]}

Xu, Heyang ^{[1
]}

Bilawal, Akhunzada ^{[1
]}

Jiang, Zhanmei ^{[1
]}

Han, Liying ^{[1
]}

机构：

[1] Northeast Agr Univ, Coll Food Sci, Key Lab Dairy Sci, Minist Educ, Harbin 150030, Peoples R China

[2] Inner Mongolia Mengniu Dairy Grp Co Ltd, Natl Enterprise Technol Ctr, Hohhot 011500, Peoples R China

来源：

INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES | 2024年 / 282卷

关键词：

(3-Lactoglobulin; alpha-Lactalbumin; gamma-Oryzanol; Emulsifying properties; Interaction; BOVINE SERUM-ALBUMIN; WHEY PROTEINS; BINDING; RICE; OIL;

D O I：

10.1016/j.ijbiomac.2024.136771

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

In this work, effects of gamma-oryzanol (GO) on structure, physicochemical and emulsifying properties of alpha-lactalbumin (alpha-La) and (3-lactoglobulin ((3-Lg) were compared by using multi-spectroscopic analysis and computer simulation. Specifically, the intrinsic fluorescence of both whey proteins was quenched by GO, with GO being a stronger quenching for (3-Lg than for alpha-La. The addition of GO caused the backbone of alpha-La to become denser, whereas for (3-Lg, its spatial structure shifted from ordered to disordered after the addition of GO. Additionally, the surface hydrophobicity, emulsifying properties, and DPPH free radical scavenging capacity of (3-Lg were higher than alpha-La after the addition of GO. Molecular docking indicated that the primary driving force in the whey protein-GO system was hydrophobic force. The hydrophobic pocket at the cleft between two structural domains in (3-Lg and alpha-La was the binding area for GO, and GO had greater binding affinity for (3-Lg than alpha-La. Furthermore, molecular dynamics simulations demonstrated that (3-Lg-GO system was more stabilized than alpha-LaGO system. This research contributed to a deeper understanding of the mechanisms by which alpha-La and (3-Lg interact with GO, offering the potential to develop whey protein-GO complexes as novel emulsifiers.

引用

页数：9

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