{"title":"超滤过程中乳清蛋白对膜表面结垢的影响机制","authors":"Wen-qiong Wang, Ji-yang Zhou, Jian-ju Li, Tang Cong-Cong","doi":"10.1007/s11483-023-09811-9","DOIUrl":null,"url":null,"abstract":"<div><p>Ultrafiltration (UF) is widely used in the fraction and concentration of whey proteins. During this process, protein polarization on the membrane surface increases the resistance of the membrane system and decreases the permeate flux. In this study, the protein structure changes as the protein surrounding the ionic environment changes, including Ca<sup>2+</sup>, K<sup>+</sup>, Na<sup>+</sup>, Mg<sup>2+</sup> and Zn<sup>2+</sup>, during the ultrafiltration process were investigated. It was found that when the ratio of Na<sup>+</sup> was higher than the other ions around the protein, the particle size of whey protein was increased and the zeta potential value decreased compared at 2–8 min. At this time, the protein surface hydrophilic group of tyrosine and tryptophan was exposed. The AFM results showed that an increase in the Na<sup>+</sup> ion ratio could lead to membrane fouling. Furthermore, the increased proportion of Zn<sup>2+</sup> could induce protein deposition on the membrane surface. The β-sheet content increased and the α-helix content decreased continuously after 21 min.</p><h3>Graphical abstract</h3><p>The dynamic change of whey protein structure with various ions’ environment concentration changes for membrane fouling formation during filtration process</p>\n<div><figure><div><div><picture><source><img></source></picture></div></div></figure></div></div>","PeriodicalId":564,"journal":{"name":"Food Biophysics","volume":"19 1","pages":"143 - 159"},"PeriodicalIF":2.8000,"publicationDate":"2023-10-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"The Mechanism of Whey Protein on Membrane Surface Fouling During Ultrafiltration Process\",\"authors\":\"Wen-qiong Wang, Ji-yang Zhou, Jian-ju Li, Tang Cong-Cong\",\"doi\":\"10.1007/s11483-023-09811-9\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><p>Ultrafiltration (UF) is widely used in the fraction and concentration of whey proteins. During this process, protein polarization on the membrane surface increases the resistance of the membrane system and decreases the permeate flux. In this study, the protein structure changes as the protein surrounding the ionic environment changes, including Ca<sup>2+</sup>, K<sup>+</sup>, Na<sup>+</sup>, Mg<sup>2+</sup> and Zn<sup>2+</sup>, during the ultrafiltration process were investigated. It was found that when the ratio of Na<sup>+</sup> was higher than the other ions around the protein, the particle size of whey protein was increased and the zeta potential value decreased compared at 2–8 min. At this time, the protein surface hydrophilic group of tyrosine and tryptophan was exposed. The AFM results showed that an increase in the Na<sup>+</sup> ion ratio could lead to membrane fouling. Furthermore, the increased proportion of Zn<sup>2+</sup> could induce protein deposition on the membrane surface. The β-sheet content increased and the α-helix content decreased continuously after 21 min.</p><h3>Graphical abstract</h3><p>The dynamic change of whey protein structure with various ions’ environment concentration changes for membrane fouling formation during filtration process</p>\\n<div><figure><div><div><picture><source><img></source></picture></div></div></figure></div></div>\",\"PeriodicalId\":564,\"journal\":{\"name\":\"Food Biophysics\",\"volume\":\"19 1\",\"pages\":\"143 - 159\"},\"PeriodicalIF\":2.8000,\"publicationDate\":\"2023-10-11\",\"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/s11483-023-09811-9\",\"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}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Food Biophysics","FirstCategoryId":"97","ListUrlMain":"https://link.springer.com/article/10.1007/s11483-023-09811-9","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}
The Mechanism of Whey Protein on Membrane Surface Fouling During Ultrafiltration Process
Ultrafiltration (UF) is widely used in the fraction and concentration of whey proteins. During this process, protein polarization on the membrane surface increases the resistance of the membrane system and decreases the permeate flux. In this study, the protein structure changes as the protein surrounding the ionic environment changes, including Ca2+, K+, Na+, Mg2+ and Zn2+, during the ultrafiltration process were investigated. It was found that when the ratio of Na+ was higher than the other ions around the protein, the particle size of whey protein was increased and the zeta potential value decreased compared at 2–8 min. At this time, the protein surface hydrophilic group of tyrosine and tryptophan was exposed. The AFM results showed that an increase in the Na+ ion ratio could lead to membrane fouling. Furthermore, the increased proportion of Zn2+ could induce protein deposition on the membrane surface. The β-sheet content increased and the α-helix content decreased continuously after 21 min.
Graphical abstract
The dynamic change of whey protein structure with various ions’ environment concentration changes for membrane fouling formation during filtration process
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.
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