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Effects of screw-pressing temperature on the functional properties and structural characteristics of apricot (Prunus armeniaca L.) kernel protein isolates

文献类型： 外文期刊

作者： Zhang, Li 1 ; Wu, Hongyu 1 ; Wang, Mengshi 2 ; Zhou, Xianjin 3 ; Bayinkexike, Ruiguo 4 ; Cui, Ruiguo 1 ; Song, Lijun 2 ; Liu, Fengjuan 5 ;

作者机构： 1.Hebei Normal Univ Sci & Technol, Coll Food Sci & Technol, Qinhuangdao, Peoples R China

2.Hebei Normal Univ Sci & Technol, Hebei Key Lab Nat Prod Act Components & Funct, Qinhuangdao, Peoples R China

3.Bazhoujiamu Agrosci Co Ltd, Korla, Xinjiang, Peoples R China

4.Dev Exchange Ctr Bayingol Mongolian Autonomous Pre, Korla, Xinjiang, Peoples R China

5.Xinjiang Acad Agr Sci, Inst Qual Stand & Testing Technol Agroprod, Urumqi, Peoples R China

关键词： apricot kernel protein isolate; functional properties; structural characteristics; screw-pressing temperatures; multivariate statistical analysis

期刊名称：FRONTIERS IN NUTRITION （ 影响因子：5.1； 五年影响因子：5.4 ）

ISSN： 2296-861X

年卷期： 2025 年 12 卷

页码：

收录情况： SCI

摘要： This study aimed to investigate the effect of screw-pressing temperature on the quality of apricot kernel protein isolates (API). The API values at different screw-pressing temperatures (40-200 degrees C) were obtained, and the functional and structural properties of different API samples were comparatively studied. The results revealed that the total polyphenol content (TPC), total flavonoid content (TFC), and antioxidant activities (DPPH and FRAP assays) increased significantly with increasing temperature. High-temperature pressing also increased the surface hydrophobicity and emulsification of API. SDS-PAGE confirmed the preservation of the primary structure of API, with molecular weights ranging from 13 to 20 kDa and 36-56 kDa. Circular dichroism (CD) spectroscopy analysis revealed that the alpha-helix content increased (by 4-8%) and the beta-sheet content decreased (by 2-5%) when the samples were pressed at high temperatures. The decrease in fluorescence intensity and the fluorescence spectral shift indicated changes in the tertiary structure. Multivariate statistical analysis revealed that the antioxidant activities were positively correlated to protein carbonyls, free sulfhydryl groups, surface hydrophobicity, TPC, and TFC. Mechanistically, thermally-induced protein conformational changes and surface hydrophobicity modulation drove the observed enhancements in functional properties. These findings will collectively serve as a theoretical basis for the efficient preparation and application of API.

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