{"title":"Impact of the Covalent Interaction Between Ferulic Acid and Ovalbumin on the Structure and Functional Properties of the Protein","authors":"Bruno Sérgio Toledo Barbosa, Sanclayver Corrêa Araújo, Yraima Cordeiro, Edwin Elard Garcia-Rojas","doi":"10.1007/s11483-024-09919-6","DOIUrl":null,"url":null,"abstract":"<div><p>Protein-polyphenol conjugates, formed through chemical modifications, can alter the structure of proteins, thereby enhancing their functional properties and enabling the development of novel ingredients for diverse applications. Despite this potential, the covalent conjugation of ovalbumin (OVA) with ferulic acid (FA) and the determination of their optimal binding ratios have not been previously studied. To address this gap, we investigated the formation of OVA-FA conjugates using an alkaline method and identified an optimal ratio of 0.9 g of FA per g of OVA. The resulting conjugates displayed substantial alterations in the secondary and tertiary structures of OVA, increased hydrophobicity, and a higher molar mass. These structural modifications significantly improved the solubility, emulsification capacity, and foam-forming ability of OVA, while also enhancing its antioxidant activity compared to the unmodified protein. These findings demonstrate the potential of OVA-FA conjugates as multifunctional emulsifiers with antioxidant properties, broadening their applications in the food and nutraceutical industries.</p></div>","PeriodicalId":564,"journal":{"name":"Food Biophysics","volume":"20 1","pages":""},"PeriodicalIF":2.8000,"publicationDate":"2024-12-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Food Biophysics","FirstCategoryId":"97","ListUrlMain":"https://link.springer.com/article/10.1007/s11483-024-09919-6","RegionNum":4,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q2","JCRName":"FOOD SCIENCE & TECHNOLOGY","Score":null,"Total":0}
引用次数: 0
Abstract
Protein-polyphenol conjugates, formed through chemical modifications, can alter the structure of proteins, thereby enhancing their functional properties and enabling the development of novel ingredients for diverse applications. Despite this potential, the covalent conjugation of ovalbumin (OVA) with ferulic acid (FA) and the determination of their optimal binding ratios have not been previously studied. To address this gap, we investigated the formation of OVA-FA conjugates using an alkaline method and identified an optimal ratio of 0.9 g of FA per g of OVA. The resulting conjugates displayed substantial alterations in the secondary and tertiary structures of OVA, increased hydrophobicity, and a higher molar mass. These structural modifications significantly improved the solubility, emulsification capacity, and foam-forming ability of OVA, while also enhancing its antioxidant activity compared to the unmodified protein. These findings demonstrate the potential of OVA-FA conjugates as multifunctional emulsifiers with antioxidant properties, broadening their applications in the food and nutraceutical industries.
通过化学修饰形成的蛋白质-多酚偶联物可以改变蛋白质的结构,从而增强其功能特性,并使开发用于各种应用的新成分成为可能。尽管有这种潜力,但卵清蛋白(OVA)与阿魏酸(FA)的共价偶联及其最佳结合比率的确定尚未得到研究。为了解决这一差距,我们使用碱性方法研究了OVA-FA偶联物的形成,并确定了每g OVA的最佳比例为0.9 g FA。所得到的共轭物显示出OVA的二级和三级结构发生了实质性的变化,疏水性增强,摩尔质量更高。与未修饰的蛋白相比,这些结构修饰显著提高了OVA的溶解度、乳化能力和泡沫形成能力,同时也增强了其抗氧化活性。这些发现证明了OVA-FA偶联物作为具有抗氧化性能的多功能乳化剂的潜力,扩大了它们在食品和营养保健工业中的应用。
期刊介绍:
Biophysical studies of foods and agricultural products involve research at the interface of chemistry, biology, and engineering, as well as the new interdisciplinary areas of materials science and nanotechnology. Such studies include but are certainly not limited to research in the following areas: the structure of food molecules, biopolymers, and biomaterials on the molecular, microscopic, and mesoscopic scales; the molecular basis of structure generation and maintenance in specific foods, feeds, food processing operations, and agricultural products; the mechanisms of microbial growth, death and antimicrobial action; structure/function relationships in food and agricultural biopolymers; novel biophysical techniques (spectroscopic, microscopic, thermal, rheological, etc.) for structural and dynamical characterization of food and agricultural materials and products; the properties of amorphous biomaterials and their influence on chemical reaction rate, microbial growth, or sensory properties; and molecular mechanisms of taste and smell.
A hallmark of such research is a dependence on various methods of instrumental analysis that provide information on the molecular level, on various physical and chemical theories used to understand the interrelations among biological molecules, and an attempt to relate macroscopic chemical and physical properties and biological functions to the molecular structure and microscopic organization of the biological material.