Bram J.N. Bemelmans , Juliette C. Verschoor , Ben H. Erné , R. Hans Tromp
{"title":"乳清蛋白和酪蛋白酸钠在胶体氧化铬上的吸附作为钢的预结垢模型","authors":"Bram J.N. Bemelmans , Juliette C. Verschoor , Ben H. Erné , R. Hans Tromp","doi":"10.1016/j.colsurfb.2025.114949","DOIUrl":null,"url":null,"abstract":"<div><h3>Hypothesis</h3><div>The fouling of stainless-steel heat exchangers used in pasteurization is a problem in the dairy industry. Thick, protein-rich layers must regularly be removed to prevent reduced flow of liquid and heat and biological hazards. We hypothesized that the adsorption of an initial monolayer of proteins is driven by electrostatic interactions.</div></div><div><h3>Experiments</h3><div>Mixtures of colloidal chromium oxide (Cr<sub>2</sub>O<sub>3</sub>) and whey proteins or sodium caseinate were studied at room temperature and pH 3–7. The surface of colloidal Cr<sub>2</sub>O<sub>3</sub> resembles the passivation layer of stainless steel, which essentially consists of Cr<sub>2</sub>O<sub>3</sub>. Stabilization of colloidal Cr<sub>2</sub>O<sub>3</sub> by adsorbed proteins was evaluated using optical microscopy, dynamic light scattering, and analytical centrifugation. Moreover, zeta potentials and adsorption isotherms were measured.</div></div><div><h3>Findings</h3><div>Despite isoelectric points at pH 2 or higher for Cr<sub>2</sub>O<sub>3</sub> and pH 5 for the proteins, the colloidal stabilization of Cr<sub>2</sub>O<sub>3</sub> by adsorbed proteins was largely pH-independent, even though the surface charge densities of Cr<sub>2</sub>O<sub>3</sub> and the proteins strongly depend on pH in our experimental pH range. Irrespective of pH, the adsorption isotherms demonstrated that a first partial monolayer of proteins was adsorbed irreversibly. We conclude that the initial adsorption of proteins onto stainless steel is probably not driven by electrostatics but by Van der Waals or hydrophobic interactions.</div></div>","PeriodicalId":279,"journal":{"name":"Colloids and Surfaces B: Biointerfaces","volume":"255 ","pages":"Article 114949"},"PeriodicalIF":5.4000,"publicationDate":"2025-07-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Adsorption of whey protein and sodium caseinate onto colloidal chromium oxide as a model for the pre-fouling of steel\",\"authors\":\"Bram J.N. Bemelmans , Juliette C. Verschoor , Ben H. Erné , R. Hans Tromp\",\"doi\":\"10.1016/j.colsurfb.2025.114949\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><h3>Hypothesis</h3><div>The fouling of stainless-steel heat exchangers used in pasteurization is a problem in the dairy industry. Thick, protein-rich layers must regularly be removed to prevent reduced flow of liquid and heat and biological hazards. We hypothesized that the adsorption of an initial monolayer of proteins is driven by electrostatic interactions.</div></div><div><h3>Experiments</h3><div>Mixtures of colloidal chromium oxide (Cr<sub>2</sub>O<sub>3</sub>) and whey proteins or sodium caseinate were studied at room temperature and pH 3–7. The surface of colloidal Cr<sub>2</sub>O<sub>3</sub> resembles the passivation layer of stainless steel, which essentially consists of Cr<sub>2</sub>O<sub>3</sub>. Stabilization of colloidal Cr<sub>2</sub>O<sub>3</sub> by adsorbed proteins was evaluated using optical microscopy, dynamic light scattering, and analytical centrifugation. Moreover, zeta potentials and adsorption isotherms were measured.</div></div><div><h3>Findings</h3><div>Despite isoelectric points at pH 2 or higher for Cr<sub>2</sub>O<sub>3</sub> and pH 5 for the proteins, the colloidal stabilization of Cr<sub>2</sub>O<sub>3</sub> by adsorbed proteins was largely pH-independent, even though the surface charge densities of Cr<sub>2</sub>O<sub>3</sub> and the proteins strongly depend on pH in our experimental pH range. Irrespective of pH, the adsorption isotherms demonstrated that a first partial monolayer of proteins was adsorbed irreversibly. We conclude that the initial adsorption of proteins onto stainless steel is probably not driven by electrostatics but by Van der Waals or hydrophobic interactions.</div></div>\",\"PeriodicalId\":279,\"journal\":{\"name\":\"Colloids and Surfaces B: Biointerfaces\",\"volume\":\"255 \",\"pages\":\"Article 114949\"},\"PeriodicalIF\":5.4000,\"publicationDate\":\"2025-07-11\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Colloids and Surfaces B: Biointerfaces\",\"FirstCategoryId\":\"1\",\"ListUrlMain\":\"https://www.sciencedirect.com/science/article/pii/S0927776525004564\",\"RegionNum\":2,\"RegionCategory\":\"医学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q1\",\"JCRName\":\"BIOPHYSICS\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Colloids and Surfaces B: Biointerfaces","FirstCategoryId":"1","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/S0927776525004564","RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q1","JCRName":"BIOPHYSICS","Score":null,"Total":0}
Adsorption of whey protein and sodium caseinate onto colloidal chromium oxide as a model for the pre-fouling of steel
Hypothesis
The fouling of stainless-steel heat exchangers used in pasteurization is a problem in the dairy industry. Thick, protein-rich layers must regularly be removed to prevent reduced flow of liquid and heat and biological hazards. We hypothesized that the adsorption of an initial monolayer of proteins is driven by electrostatic interactions.
Experiments
Mixtures of colloidal chromium oxide (Cr2O3) and whey proteins or sodium caseinate were studied at room temperature and pH 3–7. The surface of colloidal Cr2O3 resembles the passivation layer of stainless steel, which essentially consists of Cr2O3. Stabilization of colloidal Cr2O3 by adsorbed proteins was evaluated using optical microscopy, dynamic light scattering, and analytical centrifugation. Moreover, zeta potentials and adsorption isotherms were measured.
Findings
Despite isoelectric points at pH 2 or higher for Cr2O3 and pH 5 for the proteins, the colloidal stabilization of Cr2O3 by adsorbed proteins was largely pH-independent, even though the surface charge densities of Cr2O3 and the proteins strongly depend on pH in our experimental pH range. Irrespective of pH, the adsorption isotherms demonstrated that a first partial monolayer of proteins was adsorbed irreversibly. We conclude that the initial adsorption of proteins onto stainless steel is probably not driven by electrostatics but by Van der Waals or hydrophobic interactions.
期刊介绍:
Colloids and Surfaces B: Biointerfaces is an international journal devoted to fundamental and applied research on colloid and interfacial phenomena in relation to systems of biological origin, having particular relevance to the medical, pharmaceutical, biotechnological, food and cosmetic fields.
Submissions that: (1) deal solely with biological phenomena and do not describe the physico-chemical or colloid-chemical background and/or mechanism of the phenomena, and (2) deal solely with colloid/interfacial phenomena and do not have appropriate biological content or relevance, are outside the scope of the journal and will not be considered for publication.
The journal publishes regular research papers, reviews, short communications and invited perspective articles, called BioInterface Perspectives. The BioInterface Perspective provide researchers the opportunity to review their own work, as well as provide insight into the work of others that inspired and influenced the author. Regular articles should have a maximum total length of 6,000 words. In addition, a (combined) maximum of 8 normal-sized figures and/or tables is allowed (so for instance 3 tables and 5 figures). For multiple-panel figures each set of two panels equates to one figure. Short communications should not exceed half of the above. It is required to give on the article cover page a short statistical summary of the article listing the total number of words and tables/figures.