{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,25]],"date-time":"2026-08-25T17:20:01Z","timestamp":1787678401991,"version":"build-2784847793"},"reference-count":38,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2026,8,1]],"date-time":"2026-08-01T00:00:00Z","timestamp":1785542400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2026,8,1]],"date-time":"2026-08-01T00:00:00Z","timestamp":1785542400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2026,8,1]],"date-time":"2026-08-01T00:00:00Z","timestamp":1785542400000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-017"},{"start":{"date-parts":[[2026,8,1]],"date-time":"2026-08-01T00:00:00Z","timestamp":1785542400000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2026,8,1]],"date-time":"2026-08-01T00:00:00Z","timestamp":1785542400000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-012"},{"start":{"date-parts":[[2026,8,1]],"date-time":"2026-08-01T00:00:00Z","timestamp":1785542400000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2026,8,1]],"date-time":"2026-08-01T00:00:00Z","timestamp":1785542400000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-004"}],"funder":[{"DOI":"10.13039\/501100005230","name":"Chongqing Natural Science Foundation","doi-asserted-by":"publisher","award":["CSTB2023NSCQ-MSX0601"],"award-info":[{"award-number":["CSTB2023NSCQ-MSX0601"]}],"id":[{"id":"10.13039\/501100005230","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["International Journal of Biological Macromolecules"],"published-print":{"date-parts":[[2026,8]]},"DOI":"10.1016\/j.ijbiomac.2026.153111","type":"journal-article","created":{"date-parts":[[2026,6,18]],"date-time":"2026-06-18T15:54:01Z","timestamp":1781798041000},"page":"153111","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":0,"special_numbering":"C","title":["Effect of pH on the formation mechanism of riboflavin mediated photocrosslinking hydrogel of soybean protein nanofibrils"],"prefix":"10.1016","volume":"372","author":[{"given":"Xu","family":"Zhang","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hekai","family":"Zhao","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yao","family":"Lu","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sergey V.","family":"Simonenko","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Elena S.","family":"Simonenko","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Li-Tao","family":"Tong","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yang","family":"Li","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.ijbiomac.2026.153111_bb0005","article-title":"Recent advances in protein hydrogels: from design, structural and functional regulations to healthcare applications","volume":"451","author":"Zhang","year":"2023","journal-title":"Chem. Eng. J."},{"issue":"3","key":"10.1016\/j.ijbiomac.2026.153111_bb0010","doi-asserted-by":"crossref","first-page":"313","DOI":"10.1080\/87559129.2020.1858313","article-title":"Hydrogel: diversity of structures and applications in food science","volume":"37","author":"Li","year":"2021","journal-title":"Food Rev. Int."},{"key":"10.1016\/j.ijbiomac.2026.153111_bb0015","doi-asserted-by":"crossref","DOI":"10.1016\/j.foodhyd.2024.110796","article-title":"Amelioration of extremely acidic environment of soy protein amyloid fibrils to enhance gelation performance by dialysis strategy: effects of pH and ions","volume":"160","author":"Liang","year":"2025","journal-title":"Food Hydrocoll."},{"issue":"5","key":"10.1016\/j.ijbiomac.2026.153111_bb0020","doi-asserted-by":"crossref","first-page":"1643","DOI":"10.1016\/j.msec.2009.01.001","article-title":"pH effects on collagen fibrillogenesis in vitro: electrostatic interactions and phosphate binding","volume":"29","author":"Li","year":"2009","journal-title":"Mater. Sci. Eng. C"},{"key":"10.1016\/j.ijbiomac.2026.153111_bb0025","doi-asserted-by":"crossref","DOI":"10.1016\/j.foodhyd.2024.109735","article-title":"Study on the formation mechanism of pea protein nanofibrils and the changes of structural properties of fibril under different pH and temperature","volume":"150","author":"Liu","year":"2024","journal-title":"Food Hydrocoll."},{"key":"10.1016\/j.ijbiomac.2026.153111_bb0030","doi-asserted-by":"crossref","DOI":"10.1016\/j.foodhyd.2021.107067","article-title":"Development of pH-responsive emulsions stabilized by whey protein fibrils","volume":"122","author":"Cui","year":"2022","journal-title":"Food Hydrocoll."},{"key":"10.1016\/j.ijbiomac.2026.153111_bb0035","doi-asserted-by":"crossref","DOI":"10.1016\/j.lwt.2026.119124","article-title":"Impact of pH shifting on structural and emulsifying characteristics of whey protein isolate amyloid fibrils","author":"Cheng","year":"2026","journal-title":"LWT"},{"issue":"4","key":"10.1016\/j.ijbiomac.2026.153111_bb0040","doi-asserted-by":"crossref","first-page":"512","DOI":"10.1021\/acsmacrolett.0c00109","article-title":"100th anniversary of macromolecular science viewpoint: synthetic protein hydrogels","volume":"9","author":"Li","year":"2020","journal-title":"ACS Macro Lett."},{"issue":"3","key":"10.1016\/j.ijbiomac.2026.153111_bb0045","doi-asserted-by":"crossref","DOI":"10.3390\/ma16031218","article-title":"Green chemistry for crosslinking biopolymers: recent advances in riboflavin-mediated photochemistry","volume":"16","author":"Lee","year":"2023","journal-title":"Materials"},{"key":"10.1016\/j.ijbiomac.2026.153111_bb0050","doi-asserted-by":"crossref","DOI":"10.1016\/j.lwt.2020.109791","article-title":"The application of ultraviolet-induced photo-crosslinking in edible film preparation and its implication in food safety","volume":"131","author":"Li","year":"2020","journal-title":"Lwt"},{"key":"10.1016\/j.ijbiomac.2026.153111_bb0055","doi-asserted-by":"crossref","first-page":"182","DOI":"10.1016\/j.jmst.2020.02.086","article-title":"Photochemistry of bioinspired dityrosine crosslinking","volume":"63","author":"Liu","year":"2021","journal-title":"J. Mater. Sci. Technol."},{"key":"10.1016\/j.ijbiomac.2026.153111_bb0060","doi-asserted-by":"crossref","DOI":"10.1016\/j.foodhyd.2025.111671","article-title":"Study on the mechanism of riboflavin\/UV induced soy protein nanofibrils hydrogel by photo crosslinking","volume":"170","author":"Zhang","year":"2026","journal-title":"Food Hydrocoll."},{"issue":"2","key":"10.1016\/j.ijbiomac.2026.153111_bb0065","doi-asserted-by":"crossref","first-page":"164","DOI":"10.1007\/s11483-019-09567-1","article-title":"The formation and disaggregation of soy protein isolate fibril: effects of pH","volume":"14","author":"Wan","year":"2019","journal-title":"Food Biophys."},{"issue":"2","key":"10.1016\/j.ijbiomac.2026.153111_bb0070","doi-asserted-by":"crossref","first-page":"328","DOI":"10.1021\/jf990393p","article-title":"Comparison of protein surface hydrophobicity measured at various pH values using three different fluorescent probes","volume":"48","author":"Alizadeh-Pasdar","year":"2000","journal-title":"J. Agric. Food Chem."},{"issue":"8","key":"10.1016\/j.ijbiomac.2026.153111_bb0075","doi-asserted-by":"crossref","first-page":"671","DOI":"10.1002\/anie.196506711","article-title":"Progress in the chemistry and molecular biology of Flavins and Flavocoenzymes","volume":"4","author":"Hemmerich","year":"1965","journal-title":"Angew. Chem. Int. Ed. Eng."},{"issue":"3","key":"10.1016\/j.ijbiomac.2026.153111_bb0080","doi-asserted-by":"crossref","first-page":"429","DOI":"10.1016\/S0301-0104(02)00731-0","article-title":"pH dependence of the absorption and emission behaviour of riboflavin in aqueous solution","volume":"282","author":"Dr\u00f6ssler","year":"2002","journal-title":"Chem. Phys."},{"issue":"1","key":"10.1016\/j.ijbiomac.2026.153111_bb0085","doi-asserted-by":"crossref","first-page":"199","DOI":"10.1016\/j.ijpharm.2004.05.020","article-title":"Photolysis of riboflavin in aqueous solution: a kinetic study","volume":"280","author":"Ahmad","year":"2004","journal-title":"Int. J. Pharm."},{"key":"10.1016\/j.ijbiomac.2026.153111_bb0090","doi-asserted-by":"crossref","DOI":"10.1016\/j.foodcont.2024.111034","article-title":"pH triggered on-demand tannic acid release via \u201copen-close\u201d of soybean isolate proteins spatial structure for shrimp preservation","volume":"170","author":"Li","year":"2025","journal-title":"Food Control"},{"issue":"4","key":"10.1016\/j.ijbiomac.2026.153111_bb0095","doi-asserted-by":"crossref","first-page":"642","DOI":"10.1002\/pro.351","article-title":"Small-angle scattering for structural biology\u2014expanding the frontier while avoiding the pitfalls","volume":"19","author":"Jacques","year":"2010","journal-title":"Protein Sci."},{"key":"10.1016\/j.ijbiomac.2026.153111_bb0100","doi-asserted-by":"crossref","DOI":"10.1016\/j.ijbiomac.2023.129109","article-title":"High-moisture extrusion of curdlan: texture and structure","volume":"258","author":"Yang","year":"2024","journal-title":"Int. J. Biol. Macromol."},{"key":"10.1016\/j.ijbiomac.2026.153111_bb0105","doi-asserted-by":"crossref","DOI":"10.1016\/j.foodhyd.2021.107264","article-title":"Tunable self-assemblies of whey protein isolate fibrils for Pickering emulsions structure regulation","volume":"124","author":"Jiang","year":"2022","journal-title":"Food Hydrocoll."},{"key":"10.1016\/j.ijbiomac.2026.153111_bb0110","article-title":"Conformational analysis of pectins utilizing HPSEC-MALS-RI and SAXS: a comparative study","author":"Du","year":"2025","journal-title":"Food Hydrocoll."},{"issue":"7","key":"10.1016\/j.ijbiomac.2026.153111_bb0115","doi-asserted-by":"crossref","first-page":"1405","DOI":"10.1016\/j.bbapap.2010.04.001","article-title":"Molecular mechanism of Thioflavin-T binding to amyloid fibrils","volume":"1804","author":"Biancalana","year":"2010","journal-title":"Biochim. Biophy. Acta Proteins Proteomics"},{"issue":"1","key":"10.1016\/j.ijbiomac.2026.153111_bb0120","doi-asserted-by":"crossref","first-page":"30","DOI":"10.1016\/j.jsb.2004.08.002","article-title":"The binding of thioflavin-T to amyloid fibrils: localisation and implications","volume":"149","author":"Krebs","year":"2005","journal-title":"J. Struct. Biol."},{"issue":"5","key":"10.1016\/j.ijbiomac.2026.153111_bb0125","doi-asserted-by":"crossref","first-page":"850","DOI":"10.1002\/pro.2659","article-title":"Does deamidation cause protein unfolding? A top-down tandem mass spectrometry study","volume":"24","author":"Soulby","year":"2015","journal-title":"Protein Sci."},{"key":"10.1016\/j.ijbiomac.2026.153111_bb0130","doi-asserted-by":"crossref","DOI":"10.1016\/j.foodhyd.2024.110027","article-title":"Combining different ionic polysaccharides and pH treatment improved functional properties of soybean protein amyloid fibrils through structural modifications","volume":"153","author":"Feng","year":"2024","journal-title":"Food Hydrocoll."},{"key":"10.1016\/j.ijbiomac.2026.153111_bb0135","doi-asserted-by":"crossref","DOI":"10.1016\/j.foodhyd.2021.107301","article-title":"Engineering amyloid and amyloid-like morphologies of \u03b2-lactoglobulin","volume":"124","author":"Hoppenreijs","year":"2022","journal-title":"Food Hydrocoll."},{"key":"10.1016\/j.ijbiomac.2026.153111_bb0140","doi-asserted-by":"crossref","DOI":"10.1016\/j.foodhyd.2022.107974","article-title":"Environmental parameters-dependent rheological behaviors of whey protein fibril dispersions: shear and extensional flow behaviors","volume":"133","author":"Zhao","year":"2022","journal-title":"Food Hydrocoll."},{"key":"10.1016\/j.ijbiomac.2026.153111_bb0145","doi-asserted-by":"crossref","DOI":"10.1016\/j.foodhyd.2020.106335","article-title":"Consequences of heating under alkaline pH alone or in the presence of maltodextrin on solubility, emulsifying and foaming properties of faba bean protein","volume":"112","author":"Alavi","year":"2021","journal-title":"Food Hydrocoll."},{"issue":"3","key":"10.1016\/j.ijbiomac.2026.153111_bb0150","doi-asserted-by":"crossref","DOI":"10.1088\/1758-5090\/aa780f","article-title":"Correlating rheological properties and printability of collagen bioinks: the effects of riboflavin photocrosslinking and pH","volume":"9","author":"Diamantides","year":"2017","journal-title":"Biofabrication"},{"issue":"8","key":"10.1016\/j.ijbiomac.2026.153111_bb0155","doi-asserted-by":"crossref","first-page":"1945","DOI":"10.1016\/j.foodhyd.2011.02.006","article-title":"\u03b2-Lactoglobulin and WPI aggregates: formation, structure and applications","volume":"25","author":"Nicolai","year":"2011","journal-title":"Food Hydrocoll."},{"issue":"11","key":"10.1016\/j.ijbiomac.2026.153111_bb0160","doi-asserted-by":"crossref","first-page":"2910","DOI":"10.1110\/ps.051625305","article-title":"Hydrogen-bonded turns in proteins: the case for a recount","volume":"14","author":"Panasik","year":"2005","journal-title":"Protein Sci."},{"issue":"41","key":"10.1016\/j.ijbiomac.2026.153111_bb0165","doi-asserted-by":"crossref","first-page":"9566","DOI":"10.1039\/D0TB01731K","article-title":"Rapid and cytocompatible cell-laden silk hydrogel formation via riboflavin-mediated crosslinking","volume":"8","author":"Piluso","year":"2020","journal-title":"J. Mater. Chem. B"},{"key":"10.1016\/j.ijbiomac.2026.153111_bb0170","doi-asserted-by":"crossref","DOI":"10.1016\/j.foodhyd.2024.110531","article-title":"Promoting ovalbumin amyloid fibrils formation by cold plasma treatment and improving its emulsifying properties","volume":"158","author":"Liu","year":"2025","journal-title":"Food Hydrocoll."},{"issue":"1","key":"10.1016\/j.ijbiomac.2026.153111_bb0175","doi-asserted-by":"crossref","first-page":"6985","DOI":"10.1038\/s41598-019-43439-5","article-title":"Stability mechanism of two soybean protein-phosphatidylcholine Nanoemulsion preparation methods from a structural perspective: a Raman spectroscopy analysis","volume":"9","author":"Zhu","year":"2019","journal-title":"Sci. Rep."},{"issue":"7","key":"10.1016\/j.ijbiomac.2026.153111_bb0180","doi-asserted-by":"crossref","first-page":"846","DOI":"10.1016\/j.idairyj.2006.10.002","article-title":"Heat-induced whey protein isolate fibrils: conversion, hydrolysis, and disulphide bond formation","volume":"17","author":"Bolder","year":"2007","journal-title":"Int. Dairy J."},{"issue":"24","key":"10.1016\/j.ijbiomac.2026.153111_bb0185","doi-asserted-by":"crossref","first-page":"14615","DOI":"10.1021\/acscatal.0c04515","article-title":"Oxidative photocatalytic homo-and cross-coupling of phenols: nonenzymatic, catalytic method for coupling tyrosine","volume":"10","author":"Niederer","year":"2020","journal-title":"ACS Catal."},{"key":"10.1016\/j.ijbiomac.2026.153111_bb0190","doi-asserted-by":"crossref","DOI":"10.1016\/j.foodchem.2025.143406","article-title":"Amyloid fibrils from black kidney bean protein self-assemble into hydrogels: impact of heating time on gel structure and rheological properties","volume":"476","author":"Wang","year":"2025","journal-title":"Food Chem."}],"container-title":["International Journal of Biological Macromolecules"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0141813026030382?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0141813026030382?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2026,8,25]],"date-time":"2026-08-25T16:35:37Z","timestamp":1787675737000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0141813026030382"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,8]]},"references-count":38,"alternative-id":["S0141813026030382"],"URL":"https:\/\/doi.org\/10.1016\/j.ijbiomac.2026.153111","relation":{},"ISSN":["0141-8130"],"issn-type":[{"value":"0141-8130","type":"print"}],"subject":[],"published":{"date-parts":[[2026,8]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Effect of pH on the formation mechanism of riboflavin mediated photocrosslinking hydrogel of soybean protein nanofibrils","name":"articletitle","label":"Article Title"},{"value":"International Journal of Biological Macromolecules","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.ijbiomac.2026.153111","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2026 Elsevier B.V. All rights are reserved, including those for text and data mining, AI training, and similar technologies.","name":"copyright","label":"Copyright"}],"article-number":"153111"}}