Maximilian Maidl, Daniel Van Opdenbosch, Cordt Zollfrank
{"title":"通过pH值处理、醋酸和超声波处理来调整罗苹蛋白薄膜的机械和功能特性","authors":"Maximilian Maidl, Daniel Van Opdenbosch, Cordt Zollfrank","doi":"10.1007/s10924-025-03638-w","DOIUrl":null,"url":null,"abstract":"<div><p>The ability of proteins to self-assemble into ordered structures is a key feature in nature to produce highly functional biomacromolecules. This spontaneous organization of polypeptides can be utilized in technology to develop environment-friendly, protein-based bioplastic films with enhanced properties from various proteins. This study focuses on tailoring the mechanical and functional properties of solvent-cast films by pH value manipulation (10, 7, 2), acetic acid treatment, and ultrasonication of heated (85 °C, 30 min) solutions of lupin protein isolate (LPI). A combination of acetic acid and ultrasonic treatment yielded LPI films that exhibited increased tensile strengths of 6.8 ± 0.4 MPa, Young’s moduli of 270 ± 18 MPa, and works of fracture of 4.4 ± 0.5 MPa, together with high optical transmissions and water stability compared to the other investigated films. Structural investigations indicated the formation of self-assembled protein nanostructures with an increased fraction of β-sheets. Small-angle X-ray scattering investigations were performed to gain insights into the nanostructural evolution of protein aggregates from LPI during the evaporation of water.</p></div>","PeriodicalId":659,"journal":{"name":"Journal of Polymers and the Environment","volume":"33 9","pages":"4091 - 4106"},"PeriodicalIF":5.0000,"publicationDate":"2025-07-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://link.springer.com/content/pdf/10.1007/s10924-025-03638-w.pdf","citationCount":"0","resultStr":"{\"title\":\"Tailoring the Mechanical and Functional Properties of Lupin Protein Films by pH Manipulation, Acetic Acid, and Ultrasonic Treatment\",\"authors\":\"Maximilian Maidl, Daniel Van Opdenbosch, Cordt Zollfrank\",\"doi\":\"10.1007/s10924-025-03638-w\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><p>The ability of proteins to self-assemble into ordered structures is a key feature in nature to produce highly functional biomacromolecules. This spontaneous organization of polypeptides can be utilized in technology to develop environment-friendly, protein-based bioplastic films with enhanced properties from various proteins. This study focuses on tailoring the mechanical and functional properties of solvent-cast films by pH value manipulation (10, 7, 2), acetic acid treatment, and ultrasonication of heated (85 °C, 30 min) solutions of lupin protein isolate (LPI). A combination of acetic acid and ultrasonic treatment yielded LPI films that exhibited increased tensile strengths of 6.8 ± 0.4 MPa, Young’s moduli of 270 ± 18 MPa, and works of fracture of 4.4 ± 0.5 MPa, together with high optical transmissions and water stability compared to the other investigated films. Structural investigations indicated the formation of self-assembled protein nanostructures with an increased fraction of β-sheets. Small-angle X-ray scattering investigations were performed to gain insights into the nanostructural evolution of protein aggregates from LPI during the evaporation of water.</p></div>\",\"PeriodicalId\":659,\"journal\":{\"name\":\"Journal of Polymers and the Environment\",\"volume\":\"33 9\",\"pages\":\"4091 - 4106\"},\"PeriodicalIF\":5.0000,\"publicationDate\":\"2025-07-17\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://link.springer.com/content/pdf/10.1007/s10924-025-03638-w.pdf\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Journal of Polymers and the Environment\",\"FirstCategoryId\":\"5\",\"ListUrlMain\":\"https://link.springer.com/article/10.1007/s10924-025-03638-w\",\"RegionNum\":3,\"RegionCategory\":\"工程技术\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q2\",\"JCRName\":\"ENGINEERING, ENVIRONMENTAL\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Journal of Polymers and the Environment","FirstCategoryId":"5","ListUrlMain":"https://link.springer.com/article/10.1007/s10924-025-03638-w","RegionNum":3,"RegionCategory":"工程技术","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q2","JCRName":"ENGINEERING, ENVIRONMENTAL","Score":null,"Total":0}
Tailoring the Mechanical and Functional Properties of Lupin Protein Films by pH Manipulation, Acetic Acid, and Ultrasonic Treatment
The ability of proteins to self-assemble into ordered structures is a key feature in nature to produce highly functional biomacromolecules. This spontaneous organization of polypeptides can be utilized in technology to develop environment-friendly, protein-based bioplastic films with enhanced properties from various proteins. This study focuses on tailoring the mechanical and functional properties of solvent-cast films by pH value manipulation (10, 7, 2), acetic acid treatment, and ultrasonication of heated (85 °C, 30 min) solutions of lupin protein isolate (LPI). A combination of acetic acid and ultrasonic treatment yielded LPI films that exhibited increased tensile strengths of 6.8 ± 0.4 MPa, Young’s moduli of 270 ± 18 MPa, and works of fracture of 4.4 ± 0.5 MPa, together with high optical transmissions and water stability compared to the other investigated films. Structural investigations indicated the formation of self-assembled protein nanostructures with an increased fraction of β-sheets. Small-angle X-ray scattering investigations were performed to gain insights into the nanostructural evolution of protein aggregates from LPI during the evaporation of water.
期刊介绍：
The Journal of Polymers and the Environment fills the need for an international forum in this diverse and rapidly expanding field. The journal serves a crucial role for the publication of information from a wide range of disciplines and is a central outlet for the publication of high-quality peer-reviewed original papers, review articles and short communications. The journal is intentionally interdisciplinary in regard to contributions and covers the following subjects - polymers, environmentally degradable polymers, and degradation pathways: biological, photochemical, oxidative and hydrolytic; new environmental materials: derived by chemical and biosynthetic routes; environmental blends and composites; developments in processing and reactive processing of environmental polymers; characterization of environmental materials: mechanical, physical, thermal, rheological, morphological, and others; recyclable polymers and plastics recycling environmental testing: in-laboratory simulations, outdoor exposures, and standardization of methodologies; environmental fate: end products and intermediates of biodegradation; microbiology and enzymology of polymer biodegradation; solid-waste management and public legislation specific to environmental polymers; and other related topics.
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