{"title":"Interactions Between Isolated Pea Globulins and Purified Egg White Proteins in Solution","authors":"Jian Kuang, Pascaline Hamon, Florence Rousseau, Eliane Cases, Saïd Bouhallab, Rémi Saurel, Valerie Lechevalier","doi":"10.1007/s11483-023-09797-4","DOIUrl":null,"url":null,"abstract":"<div><p>In the present work, the interactions and associations between low denatured pea globulins (PPI) and purified main egg white proteins (ovalbumin (OVA), ovotransferrin (OVT), and lysozyme (LYS)) were studied at pH 7.5 and 9.0 by using isothermal titration calorimetry (ITC), dynamic light scattering (DLS), laser granulometry and confocal laser scanning microscopy (CLSM). From ITC, we detected strong exothermic interactions between PPI and LYS at both pHs, which led to aggregation. At these pH values, the net positive charge of lysozyme favored electrostatic interactions with negative charges of pea proteins, and oligomers were formed during titration experiments. Furthermore, DLS, laser granulometry, and CLSM data showed that the particle size of the mixture increased with increasing LYS to PPI molar ratio (from 0.8 to 20). Large irregular aggregates up to 20–25 μm were formed at high molar ratios and no complex coacervate was observed. No or very weak interactions were detected between OVT or OVA and PPI whatever the pH. These results suggest the role of electrostatic interactions between LYS and PPI when considering protein mixtures.</p></div>","PeriodicalId":564,"journal":{"name":"Food Biophysics","volume":null,"pages":null},"PeriodicalIF":2.8000,"publicationDate":"2023-06-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"1","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Food Biophysics","FirstCategoryId":"97","ListUrlMain":"https://link.springer.com/article/10.1007/s11483-023-09797-4","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: 1
Abstract
In the present work, the interactions and associations between low denatured pea globulins (PPI) and purified main egg white proteins (ovalbumin (OVA), ovotransferrin (OVT), and lysozyme (LYS)) were studied at pH 7.5 and 9.0 by using isothermal titration calorimetry (ITC), dynamic light scattering (DLS), laser granulometry and confocal laser scanning microscopy (CLSM). From ITC, we detected strong exothermic interactions between PPI and LYS at both pHs, which led to aggregation. At these pH values, the net positive charge of lysozyme favored electrostatic interactions with negative charges of pea proteins, and oligomers were formed during titration experiments. Furthermore, DLS, laser granulometry, and CLSM data showed that the particle size of the mixture increased with increasing LYS to PPI molar ratio (from 0.8 to 20). Large irregular aggregates up to 20–25 μm were formed at high molar ratios and no complex coacervate was observed. No or very weak interactions were detected between OVT or OVA and PPI whatever the pH. These results suggest the role of electrostatic interactions between LYS and PPI when considering protein mixtures.
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.