Physicochemical, structural and volatile changes of soybean protein isolate induced by hydroxyl radical generating system

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Physicochemical, structural and volatile changes of soybean protein isolate induced by hydroxyl radical generating system | Research Square window.SnipcartSettings = { analytics: { enabled: false } }; (function() { var accessVector = localStorage.getItem('access_vector') || ''; window.dataLayer = window.dataLayer || []; if (accessVector) { window.dataLayer.push({ user: { profile: { profileInfo: { snid: accessVector } } } }); } })(); (function(w,d,s,l,i){w[l]=w[l]||[];w[l].push({'gtm.start':new Date().getTime(),event:'gtm.js'});var f=d.getElementsByTagName(s)[0],j=d.createElement(s),dl=l!='dataLayer'?'&l='+l:'';j.async=true;j.src='https://www.googletagmanager.com/gtm.js?id='+i+dl;f.parentNode.insertBefore(j,f);})(window,document,'script','dataLayer','GTM-K279D39R'); Browse Preprints In Review Journals COVID-19 Preprints AJE Video Bytes Research Tools Research Promotion AJE Professional Editing AJE Rubriq About Preprint Platform In Review Editorial Policies Our Team Advisory Board Help Center Sign In Submit a Preprint Cite Share Download PDF Research Article Physicochemical, structural and volatile changes of soybean protein isolate induced by hydroxyl radical generating system Xiaoyan Zhao, Jinghui Feng, Fanghong Wang, Meng Wang, Hongkai Liu, and 1 more This is a preprint; it has not been peer reviewed by a journal. https://doi.org/ 10.21203/rs.3.rs-6756362/v1 This work is licensed under a CC BY 4.0 License Status: Under Review Version 1 posted 8 You are reading this latest preprint version Abstract The aim of the study was to investigate the effect of hydroxyl-radical on soybean protein isolate (SPI) properties. SPI were incubated with different H 2 O 2 concentrations of 0, 0.1, 1, 5, 10 and 15 mM for 24 h. The oxidization induced more porous microstructure in SPI surface. The total sulfhydryl group, water/oil holding capacity (WHC/OHC), enthalpy, solubility of SPI with increasing the concentration of H 2 O 2 decreased significantly ( p < 0.05), while H 2 O 2 prompted a significantly increase in protein carbonyl content ( p < 0.05). FTIR confirmed that oxidation resulted in the gradual loss of α-helical and β-sheet structures with the concomitant increase of β-turn and random coil structures. Compared with the raw SPI, the moderate H 2 O 2 concentration (1 mM) enhanced emulsifying properties while lower (0.1 mM) and higher (5 mM) H 2 O 2 concentration significantly increased the foaming properties and the value of zeta potential, respectively ( P < 0.05). With the increase of H 2 O 2 concentration, the intensities of volatile compound were strongly influenced by the oxidation levels of SPI, some compounds increased, some decreased, which was likely owing to the structure changes of modified SPI. All in all, these results offered evidences of how protein oxidation affected the properties and structure of SPI. Soy protein isolate Hydroxyl radical Secondary structure Functional properties Volatile compounds Full Text Additional Declarations No competing interests reported. Cite Share Download PDF Status: Under Review Version 1 posted Editorial decision: Revision requested 04 Sep, 2025 Reviews received at journal 28 Jun, 2025 Reviewers agreed at journal 10 Jun, 2025 Reviewers agreed at journal 04 Jun, 2025 Reviewers invited by journal 03 Jun, 2025 Editor assigned by journal 27 May, 2025 Submission checks completed at journal 27 May, 2025 First submitted to journal 27 May, 2025 You are reading this latest preprint version Research Square lets you share your work early, gain feedback from the community, and start making changes to your manuscript prior to peer review in a journal. As a division of Research Square Company, we’re committed to making research communication faster, fairer, and more useful. We do this by developing innovative software and high quality services for the global research community. Our growing team is made up of researchers and industry professionals working together to solve the most critical problems facing scientific publishing. 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SPI were incubated with different H\u003csub\u003e2\u003c/sub\u003eO\u003csub\u003e2 \u003c/sub\u003econcentrations of 0, 0.1, 1, 5, 10 and 15 mM for 24 h. The oxidization induced more porous microstructure in SPI surface. The total sulfhydryl group, water/oil holding capacity (WHC/OHC), enthalpy, solubility of SPI with increasing the concentration of H\u003csub\u003e2\u003c/sub\u003eO\u003csub\u003e2\u003c/sub\u003e decreased significantly (\u003cem\u003ep \u003c/em\u003e\u0026lt; 0.05), while H\u003csub\u003e2\u003c/sub\u003eO\u003csub\u003e2 \u003c/sub\u003eprompted a significantly increase in protein carbonyl content (\u003cem\u003ep\u003c/em\u003e \u0026lt; 0.05). FTIR confirmed that oxidation resulted in the gradual loss of α-helical and β-sheet structures with the concomitant increase of β-turn and random coil structures. 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