A new technique for glycosylation modification of soy protein isolates using magnetically induced electric field: focus on structure and gel properties
{"title":"A new technique for glycosylation modification of soy protein isolates using magnetically induced electric field: focus on structure and gel properties","authors":"Xinnan Li, Yuhan Lan, Lina sun, Sitong Wu, Xibo Wang, Ning Xu","doi":"10.1016/j.jfoodeng.2025.112638","DOIUrl":null,"url":null,"abstract":"<div><div>In this study, soy protein isolate (SPI) glycosylated conjugates were successfully prepared by incorporating three sugars with different molecular weights (maltose, maltodextrin with dextrose equivalent of 16, and maltodextrin with dextrose equivalent of 11) into SPI using the magnetically induced electric field (MIEF) technique. The structural and gel properties of the conjugates were subsequently evaluated. The degree of grafting and SDS-PAGE results confirmed the formation of these covalent conjugates. Maltose, due to its smaller molecular weight, was more readily incorporated into SPI. Fluorescence and UV spectroscopy analyses demonstrated that MIEF-induced covalent cross-linking caused significant conformational changes in the SPI, leading to fluorescence quenching of SPI and the formation of a more hydrophilic microenvironment around the amino acid residues. FTIR revealed that MIEF triggered substantial alteration in the secondary structure of SPI, manifested by a pronounced reduction in α-helix content accompanied by a concomitant rise in random coil structures. MIEF-induced glycosylation modification of SPI enhanced its solubility, surface hydrophobicity, and free sulfhydryl content, resulting in a looser and more flexible protein structure that positively influenced the improvement of gel properties. Further investigation of the gel properties of the glycosylated conjugates demonstrated that the gel network structure became more ordered, with hardness increasing by 62.12 % and water-holding capacity improving by 23.39 %. Rheological analysis revealed that the glycosylated conjugates formed a viscoelastic gel network structure, with a significant increase in hydrogen bonding, thereby enhancing the stability of the protein gels.</div></div>","PeriodicalId":359,"journal":{"name":"Journal of Food Engineering","volume":"400 ","pages":"Article 112638"},"PeriodicalIF":5.3000,"publicationDate":"2025-05-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Journal of Food Engineering","FirstCategoryId":"97","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/S0260877425001736","RegionNum":2,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q1","JCRName":"ENGINEERING, CHEMICAL","Score":null,"Total":0}
引用次数: 0
Abstract
In this study, soy protein isolate (SPI) glycosylated conjugates were successfully prepared by incorporating three sugars with different molecular weights (maltose, maltodextrin with dextrose equivalent of 16, and maltodextrin with dextrose equivalent of 11) into SPI using the magnetically induced electric field (MIEF) technique. The structural and gel properties of the conjugates were subsequently evaluated. The degree of grafting and SDS-PAGE results confirmed the formation of these covalent conjugates. Maltose, due to its smaller molecular weight, was more readily incorporated into SPI. Fluorescence and UV spectroscopy analyses demonstrated that MIEF-induced covalent cross-linking caused significant conformational changes in the SPI, leading to fluorescence quenching of SPI and the formation of a more hydrophilic microenvironment around the amino acid residues. FTIR revealed that MIEF triggered substantial alteration in the secondary structure of SPI, manifested by a pronounced reduction in α-helix content accompanied by a concomitant rise in random coil structures. MIEF-induced glycosylation modification of SPI enhanced its solubility, surface hydrophobicity, and free sulfhydryl content, resulting in a looser and more flexible protein structure that positively influenced the improvement of gel properties. Further investigation of the gel properties of the glycosylated conjugates demonstrated that the gel network structure became more ordered, with hardness increasing by 62.12 % and water-holding capacity improving by 23.39 %. Rheological analysis revealed that the glycosylated conjugates formed a viscoelastic gel network structure, with a significant increase in hydrogen bonding, thereby enhancing the stability of the protein gels.
期刊介绍:
The journal publishes original research and review papers on any subject at the interface between food and engineering, particularly those of relevance to industry, including:
Engineering properties of foods, food physics and physical chemistry; processing, measurement, control, packaging, storage and distribution; engineering aspects of the design and production of novel foods and of food service and catering; design and operation of food processes, plant and equipment; economics of food engineering, including the economics of alternative processes.
Accounts of food engineering achievements are of particular value.