Effect and mechanisms of thermal sterilization methods on the in vitro phenolic bioaccessibility of rose tea with milk

Rose polyphenols, key functional components in roses, require adequate bioaccessibility for their health benefits, subject to influence by food components and processing. Investigating the impact of various thermal sterilization methods on the bioaccessibility of rose polyphenols in rose tea with mi...

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Published inFood chemistry Vol. 458; p. 140248
Main Authors Zhu, Ruifang, Wang, Li, Chao, Ailun, Fan, Fangyu, Wang, Mingfu, Zhao, Yueliang
Format Journal Article
LanguageEnglish
Published England Elsevier Ltd 15.11.2024
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Summary:Rose polyphenols, key functional components in roses, require adequate bioaccessibility for their health benefits, subject to influence by food components and processing. Investigating the impact of various thermal sterilization methods on the bioaccessibility of rose polyphenols in rose tea with milk and the underlying mechanisms, our findings indicated a significant increase in bioaccessibility following treatment at 85 °C/30 min. Conversely, 121 °C/15 min treatment decreased bioaccessibility. Examining the interaction between β-casein in milk and rose polyphenols under different sterilization conditions, SEM and particle size analysis revealed binding, with fluorescence spectroscopy indicating non-covalent bonds. Binding forces followed the order 121 °C > 85 °C > 25 °C. Notably, at 85 °C, non-covalent binding improved polyphenol bioaccessibility, while the intensified binding at 121 °C decreased it. SDS-PAGE and amino acid analysis confirmed no covalent bond. This study establishes a theoretical basis for selecting thermal sterilization temperatures for milk-flower combinations, considering polyphenol bioaccessibility. •85 °C sterilization increased the polyphenol bioaccessibility of rose tea with milk.•121 °C sterilization decreased the polyphenol bioaccessibility of rose tea with milk.•Increased bioaccessibility at 85 °C was attributed to non-covalent binding.•SDS-PAGE and amino acid analysis confirmed no covalent bond.
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ISSN:0308-8146
1873-7072
1873-7072
DOI:10.1016/j.foodchem.2024.140248