{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,14]],"date-time":"2026-08-14T20:13:26Z","timestamp":1786738406896,"version":"build-2736575974"},"reference-count":32,"publisher":"American Chemical Society (ACS)","issue":"6","license":[{"start":{"date-parts":[[2021,5,24]],"date-time":"2021-05-24T00:00:00Z","timestamp":1621814400000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2021,5,24]],"date-time":"2021-05-24T00:00:00Z","timestamp":1621814400000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2021,5,24]],"date-time":"2021-05-24T00:00:00Z","timestamp":1621814400000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-045"}],"funder":[{"DOI":"10.13039\/100011140","name":"Institute of Agriculture and Natural Resources","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100011140","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100011033","name":"Thermo Fisher Scientific","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100011033","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2021,6,4]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>Gluten-containing grains cause adverse health effects in individuals with celiac disease. Fermentation of these grains results in gluten-derived polypeptides with largely uncharacterized sizes and sequences, which may still trigger an immune response. This research used N-terminal labeling mass spectrometry to characterize protein hydrolysates during each stage of bench-scale brewing, including malting, mashing, boiling, fermentation, and aging. Gluten hydrolysates from each brewing step were tracked, and the immunotoxic potential was evaluated by sequence comparison with peptides known to stimulate celiac immune responses. The results indicate that proteolysis and precipitation of gliadins occurring during brewing differ by protein region and brewing stage. The termini of gliadins were hydrolyzed throughout the entire brewing process, but the central regions remained relatively stable. Most hydrolysis occurred during malting, and most precipitation occurred during boiling. The addition of yeast yielded new cleavage sites but did not result in complete hydrolysis. Consistent detection of peptides within the clinically important regions of gliadin corroborated the hydrolytic resistance of this region. N-terminal labeling mass spectrometry served as a novel approach to track the fate of gliadin\/gluten throughout bench-scale brewing. Consistently identified fragments could serve as improved targets for the detection of hydrolyzed gluten in fermented products.<\/jats:p>","DOI":"10.1021\/acs.jproteome.1c00076","type":"journal-article","created":{"date-parts":[[2021,5,24]],"date-time":"2021-05-24T13:43:21Z","timestamp":1621863801000},"page":"3230-3241","source":"Crossref","is-referenced-by-count":3,"title":["Tracking Gluten\nthroughout Brewing Using N\u2011Terminal\nLabeling Mass Spectrometry"],"prefix":"10.1021","volume":"20","author":[{"given":"Wanying","family":"Cao","sequence":"first","affiliation":[{"name":"University of Nebraska\ue5f8Lincoln , , 1901 North 21st Street , , ,","place":["Lincoln, Nebraska, United States, 68588"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Joseph L.","family":"Baumert","sequence":"additional","affiliation":[{"name":"University of Nebraska\ue5f8Lincoln , , 1901 North 21st Street , , ,","place":["Lincoln, Nebraska, United States, 68588"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-3753-3658","authenticated-orcid":true,"given":"Melanie L.","family":"Downs","sequence":"additional","affiliation":[{"name":"University of Nebraska\ue5f8Lincoln , , 1901 North 21st Street , , ,","place":["Lincoln, Nebraska, United States, 68588"]}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"316","published-online":{"date-parts":[[2021,5,24]]},"reference":[{"key":"2026081415112967900_cit1","doi-asserted-by":"crossref","DOI":"10.1094\/9781891127632","volume-title":"Principles of Cereal\nScience and Technology","author":"Delcour","year":"2010","edition":"3"},{"key":"2026081415112967900_cit2","doi-asserted-by":"publisher","first-page":"539","DOI":"10.1021\/ja02162a008","article-title":"The proteids\nof barley","volume":"17","author":"Osborne","year":"1895","journal-title":"J. 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Cereal Sci."},{"key":"2026081415112967900_cit9","doi-asserted-by":"publisher","first-page":"455","DOI":"10.1007\/s00251-012-0599-z","article-title":"Nomenclature and listing of celiac disease relevant\ngluten T-cell epitopes restricted by HLA-DQ molecules","volume":"64","author":"Sollid","year":"2012","journal-title":"Immunogenetics"},{"key":"2026081415112967900_cit10","doi-asserted-by":"publisher","first-page":"1013","DOI":"10.1016\/j.foodres.2012.11.028","article-title":"Beer proteomics analysis\nfor beer quality control and malting barley\nbreeding","volume":"54","author":"Iimure","year":"2013","journal-title":"Food Res. Int."},{"key":"2026081415112967900_cit11","volume-title":"Beer: Tap into the\nArt and Science of Brewing","author":"Bamforth","year":"2009","edition":"3"},{"key":"2026081415112967900_cit12","doi-asserted-by":"publisher","first-page":"D343","DOI":"10.1093\/nar\/gkv1118","article-title":"Twenty years of the MEROPS database\nof proteolytic enzymes, their substrates and inhibitors","volume":"44","author":"Rawlings","year":"2016","journal-title":"Nucleic Acids Res."},{"key":"2026081415112967900_cit13","doi-asserted-by":"publisher","first-page":"129","DOI":"10.1016\/j.tifs.2017.07.004","article-title":"The production of gluten-free beer:\nDegradation of hordeins during malting and brewing and the application\nof modern process technology focusing on endogenous malt peptidases","volume":"67","author":"Kerpes","year":"2017","journal-title":"Trends Food Sci. Technol."},{"key":"2026081415112967900_cit14","doi-asserted-by":"publisher","first-page":"262","DOI":"10.1016\/j.foodres.2011.10.033","article-title":"Proteome analysis\nof the wort boiling process","volume":"45","author":"Iimure","year":"2012","journal-title":"Food Res. Int."},{"key":"2026081415112967900_cit15","doi-asserted-by":"publisher","first-page":"1167","DOI":"10.4315\/0362-028X.JFP-14-546","article-title":"Detection\nand quantification of gluten during the brewing and fermentation of\nbeer using antibody-based technologies","volume":"78","author":"Panda","year":"2015","journal-title":"J. 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Biotechnol."},{"key":"2026081415112967900_cit22","doi-asserted-by":"publisher","first-page":"1578","DOI":"10.1038\/nprot.2011.382","article-title":"Identifying and\nquantifying proteolytic events and the natural N terminome by terminal\namine isotopic labeling of substrates","volume":"6","author":"Kleifeld","year":"2011","journal-title":"Nat.\nProtoc."},{"key":"2026081415112967900_cit23","doi-asserted-by":"publisher","DOI":"10.1016\/j.jprot.2019.103538","article-title":"Evaluation of N-terminal labeling\nmass spectrometry for characterization of partially hydrolyzed gluten\nproteins","volume":"210","author":"Cao","year":"2020","journal-title":"J. Proteomics"},{"key":"2026081415112967900_cit24","doi-asserted-by":"publisher","first-page":"5835","DOI":"10.1021\/jf500997j","article-title":"Characterization\nof grain-specific peptide markers for the detection of gluten by mass\nspectrometry","volume":"62","author":"Fiedler","year":"2014","journal-title":"J. Agric. 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