Qin Sun, Na Li, Jiangnan Chu, Zhengwei Wu, Fan Zhou
{"title":"等离子体活化水对大豆分离蛋白理化及功能特性影响的研究","authors":"Qin Sun, Na Li, Jiangnan Chu, Zhengwei Wu, Fan Zhou","doi":"10.1007/s11483-025-10013-8","DOIUrl":null,"url":null,"abstract":"<div><p>Alternative sustainable and green protein modification technologies for the improvement of functional properties of plant proteins are gaining increasing attention. This study investigated the novel application of plasma-activated water (PAW) as a gentle and uniform protein processing technology to enhance the functional properties of Soybean Protein Isolate (SPI). SPI was hydrated in PAW solutions prepared at different plasma exposure times (0–30 min) and then freeze-dried. Evaluations included Fourier transform infrared (FTIR) spectroscopy, sulfhydryl content, particle size, gel electrophoresis, surface hydrophobicity, solubility, water holding capacity, contact angle, and emulsifying activity and stability. Key findings revealed that PAW treatment induced partial unfolding of SPI, enhanced α-helix structure while reducing β-sheet content, particularly in the PAW20 group. Sulfhydryl group oxidation led to disulfide bond formation, transiently exposing buried groups and decreasing total sulfhydryl content. Surface hydrophobicity and solubility peaked at PAW15 treatment, significantly enhancing SPI’s emulsifying properties. Prolonged treatment (> 15 min) caused protein aggregation, diminishing functionality. Optimal PAW15 treatment improves SPI’s structural flexibility and interfacial properties, offering a sustainable strategy for developing high-performance plant protein ingredients in food systems. These results highlight the potential of PAW as a novel and effective method to improve the functional properties of plant proteins.</p></div>","PeriodicalId":564,"journal":{"name":"Food Biophysics","volume":"20 3","pages":""},"PeriodicalIF":3.2000,"publicationDate":"2025-08-13","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Investigation of the Effect of Plasma-Activated Water on the Physicochemical and Functional Attributes of Soybean Protein Isolate\",\"authors\":\"Qin Sun, Na Li, Jiangnan Chu, Zhengwei Wu, Fan Zhou\",\"doi\":\"10.1007/s11483-025-10013-8\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><p>Alternative sustainable and green protein modification technologies for the improvement of functional properties of plant proteins are gaining increasing attention. This study investigated the novel application of plasma-activated water (PAW) as a gentle and uniform protein processing technology to enhance the functional properties of Soybean Protein Isolate (SPI). SPI was hydrated in PAW solutions prepared at different plasma exposure times (0–30 min) and then freeze-dried. Evaluations included Fourier transform infrared (FTIR) spectroscopy, sulfhydryl content, particle size, gel electrophoresis, surface hydrophobicity, solubility, water holding capacity, contact angle, and emulsifying activity and stability. Key findings revealed that PAW treatment induced partial unfolding of SPI, enhanced α-helix structure while reducing β-sheet content, particularly in the PAW20 group. Sulfhydryl group oxidation led to disulfide bond formation, transiently exposing buried groups and decreasing total sulfhydryl content. Surface hydrophobicity and solubility peaked at PAW15 treatment, significantly enhancing SPI’s emulsifying properties. Prolonged treatment (> 15 min) caused protein aggregation, diminishing functionality. Optimal PAW15 treatment improves SPI’s structural flexibility and interfacial properties, offering a sustainable strategy for developing high-performance plant protein ingredients in food systems. These results highlight the potential of PAW as a novel and effective method to improve the functional properties of plant proteins.</p></div>\",\"PeriodicalId\":564,\"journal\":{\"name\":\"Food Biophysics\",\"volume\":\"20 3\",\"pages\":\"\"},\"PeriodicalIF\":3.2000,\"publicationDate\":\"2025-08-13\",\"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/s11483-025-10013-8\",\"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/s11483-025-10013-8","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}
Investigation of the Effect of Plasma-Activated Water on the Physicochemical and Functional Attributes of Soybean Protein Isolate
Alternative sustainable and green protein modification technologies for the improvement of functional properties of plant proteins are gaining increasing attention. This study investigated the novel application of plasma-activated water (PAW) as a gentle and uniform protein processing technology to enhance the functional properties of Soybean Protein Isolate (SPI). SPI was hydrated in PAW solutions prepared at different plasma exposure times (0–30 min) and then freeze-dried. Evaluations included Fourier transform infrared (FTIR) spectroscopy, sulfhydryl content, particle size, gel electrophoresis, surface hydrophobicity, solubility, water holding capacity, contact angle, and emulsifying activity and stability. Key findings revealed that PAW treatment induced partial unfolding of SPI, enhanced α-helix structure while reducing β-sheet content, particularly in the PAW20 group. Sulfhydryl group oxidation led to disulfide bond formation, transiently exposing buried groups and decreasing total sulfhydryl content. Surface hydrophobicity and solubility peaked at PAW15 treatment, significantly enhancing SPI’s emulsifying properties. Prolonged treatment (> 15 min) caused protein aggregation, diminishing functionality. Optimal PAW15 treatment improves SPI’s structural flexibility and interfacial properties, offering a sustainable strategy for developing high-performance plant protein ingredients in food systems. These results highlight the potential of PAW as a novel and effective method to improve the functional properties of plant proteins.
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.