Protein-polyphenol complexation vs. conjugation: A review on mechanisms, functional differences, and antioxidant-emulsifier roles

IF 11 1区 农林科学 Q1 CHEMISTRY, APPLIED
Peyman Ebrahimi , Anna Lante , Lutz Grossmann
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引用次数: 0

Abstract

The interaction between proteins and polyphenols has gained attention for improving the stability and physicochemical properties of colloidal systems. This review focuses on recent advances in their interaction mechanisms and functional impacts. Protein-polyphenol assemblies are formed through covalent bonding (i.e., conjugation) or non-covalent bonding (i.e., complexation). These interactions may lead to distinct functionalities and properties influenced by environmental conditions. The conjugation is usually initiated by the oxidation of polyphenols through alkaline treatment, free radicals, etc., while complexation occurs even under milder conditions, such as neutral pH and room temperature, resulting in weaker and reversible interactions. Despite the significant increase in the number of studies on protein-polyphenol interactions in recent years, there is no clear consensus in the previous literature on whether covalent or non-covalent bonding provides better stability under different processing conditions. In emulsion-based food systems, protein-polyphenol assemblies can function dually as antioxidant-emulsifiers, where proteins provide the emulsifying ability, and polyphenols contribute antioxidant activity. This effect is due to the positioning of these assemblies in the oil-water interface. Understanding the distinct roles and conditions of protein-polyphenol interactions is crucial for optimizing their use in designing stable, functional colloidal systems, particularly in emulsion-based foods.
蛋白质-多酚络合与偶联:机制、功能差异和抗氧化-乳化剂作用的综述
蛋白质与多酚之间的相互作用在改善胶体系统的稳定性和理化性质方面已引起人们的关注。本文就其相互作用机制和功能影响的研究进展作一综述。蛋白质-多酚组合通过共价键(即共轭)或非共价键(即络合)形成。这些相互作用可能导致受环境条件影响的不同功能和特性。偶联反应通常是由多酚通过碱性处理、自由基等氧化引起的,而络合反应即使在更温和的条件下也会发生,如中性pH和室温,从而导致较弱的可逆相互作用。尽管近年来对蛋白质-多酚相互作用的研究显著增加,但在不同的加工条件下,共价键和非共价键究竟是稳定性更好,在以往的文献中并没有明确的共识。在以乳化为基础的食品系统中,蛋白质-多酚组合物可以作为抗氧化剂-乳化剂发挥双重作用,其中蛋白质提供乳化能力,而多酚提供抗氧化活性。这种影响是由于这些组件在油水界面中的定位。了解蛋白质-多酚相互作用的独特作用和条件对于优化它们在设计稳定、功能性胶体系统中的应用至关重要,特别是在乳化食品中。
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来源期刊
Food Hydrocolloids
Food Hydrocolloids 工程技术-食品科技
CiteScore
19.90
自引率
14.00%
发文量
871
审稿时长
37 days
期刊介绍: Food Hydrocolloids publishes original and innovative research focused on the characterization, functional properties, and applications of hydrocolloid materials used in food products. These hydrocolloids, defined as polysaccharides and proteins of commercial importance, are added to control aspects such as texture, stability, rheology, and sensory properties. The research's primary emphasis should be on the hydrocolloids themselves, with thorough descriptions of their source, nature, and physicochemical characteristics. Manuscripts are expected to clearly outline specific aims and objectives, include a fundamental discussion of research findings at the molecular level, and address the significance of the results. Studies on hydrocolloids in complex formulations should concentrate on their overall properties and mechanisms of action, while simple formulation development studies may not be considered for publication. The main areas of interest are: -Chemical and physicochemical characterisation Thermal properties including glass transitions and conformational changes- Rheological properties including viscosity, viscoelastic properties and gelation behaviour- The influence on organoleptic properties- Interfacial properties including stabilisation of dispersions, emulsions and foams- Film forming properties with application to edible films and active packaging- Encapsulation and controlled release of active compounds- The influence on health including their role as dietary fibre- Manipulation of hydrocolloid structure and functionality through chemical, biochemical and physical processes- New hydrocolloids and hydrocolloid sources of commercial potential. The Journal also publishes Review articles that provide an overview of the latest developments in topics of specific interest to researchers in this field of activity.
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