{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,20]],"date-time":"2026-09-20T14:18:06Z","timestamp":1789913886031,"version":"4.0.1"},"reference-count":39,"publisher":"MDPI AG","issue":"22","license":[{"start":{"date-parts":[[2021,11,10]],"date-time":"2021-11-10T00:00:00Z","timestamp":1636502400000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100007111","name":"Bartin University","doi-asserted-by":"publisher","award":["2019-FEN-A-015"],"award-info":[{"award-number":["2019-FEN-A-015"]}],"id":[{"id":"10.13039\/501100007111","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100000781","name":"European Research Council","doi-asserted-by":"publisher","award":["261152"],"award-info":[{"award-number":["261152"]}],"id":[{"id":"10.13039\/501100000781","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100012774","name":"Innovationsfonden","doi-asserted-by":"publisher","award":["7076-00053 B"],"award-info":[{"award-number":["7076-00053 B"]}],"id":[{"id":"10.13039\/100012774","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Molecules"],"abstract":"<jats:p>The aim of this study was to investigate binding interactions between \u03b2-lactoglobulin (BLG) and two different mucins, bovine submaxillary mucins (BSM) and porcine gastric mucin (PGM), using intrinsic and extrinsic fluorescence spectroscopies. Intrinsic fluorescence spectra showed an enhanced decrease of fluorescence intensity of BLG at all pH conditions when BLG was mixed with PGM rather than with BSM. We propose that, unlike BSM, the tertiary structure of PGM changes and the hydrophobic regions are exposed at pH 3 due to protonation of negatively charged residues. Results suggest that PGM also facilitated the structural unfolding of BLG and its binding with PGM by a hydrophobic interaction, especially at acidic pH, which was further supported by extrinsic fluorescence spectroscopy. Hydrophobic interaction is suggested as the dominant interaction mechanism between BLG and PGM at pH 3, whereas electrostatic interaction is the dominant one between BLG and BSM.<\/jats:p>","DOI":"10.3390\/molecules26226799","type":"journal-article","created":{"date-parts":[[2021,11,11]],"date-time":"2021-11-11T23:04:46Z","timestamp":1636671886000},"page":"6799","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":18,"title":["Interactions of \u03b2-Lactoglobulin with Bovine Submaxillary Mucin vs. Porcine Gastric Mucin: The Role of Hydrophobic and Hydrophilic Residues as Studied by Fluorescence Spectroscopy"],"prefix":"10.3390","volume":"26","author":[{"given":"Hilal","family":"Y\u0131lmaz","sequence":"first","affiliation":[{"name":"Department of Biotechnology, Bart\u0131n University, Kutlubey Campus, Bart\u0131n 74100, Turkey"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Seunghwan","family":"Lee","sequence":"additional","affiliation":[{"name":"Department of Mechanical Engineering, Technical University of Denmark, DK-2800 Kgs. Lyngby, Denmark"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-8339-3564","authenticated-orcid":false,"given":"Ioannis S.","family":"Chronakis","sequence":"additional","affiliation":[{"name":"DTU-Food, Technical University of Denmark, Kemitorvet, B202, DK-2800 Kgs. Lyngby, Denmark"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2021,11,10]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"143","DOI":"10.1016\/S0141-8130(98)00037-3","article-title":"Some aspects of \u03b2-lactoglobulin structural properties in solution studied by fluorescence quenching","volume":"23","author":"Busti","year":"1998","journal-title":"Int. J. Biol. Macromol."},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"136","DOI":"10.1016\/S0167-4838(00)00160-6","article-title":"The core lipocalin, bovine \u03b2-lactoglobulin","volume":"1482","author":"Sawyer","year":"2000","journal-title":"Biochim. Biophys. Acta (BBA)-Protein Struct. Mol. Enzymol."},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"527","DOI":"10.1016\/j.bbagen.2009.04.003","article-title":"Structural dynamics and folding of \u03b2-lactoglobulin probed by heteronuclear NMR","volume":"1790","author":"Sakurai","year":"2009","journal-title":"Biochim. Biophys. Acta (BBA)-Gen. Subj."},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"203","DOI":"10.1016\/j.foodhyd.2015.04.026","article-title":"Spectroscopic studies of the interactions between \u03b2-lactoglobulin and bovine submaxillary mucin","volume":"50","author":"Meier","year":"2015","journal-title":"Food Hydrocoll."},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"143","DOI":"10.1016\/j.foodchem.2017.01.131","article-title":"Comparison of binding interaction between \u03b2-lactoglobulin and three common polyphenols using multi-spectroscopy and modeling methods","volume":"228","author":"Jia","year":"2017","journal-title":"Food Chem."},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"817","DOI":"10.3168\/jds.S0022-0302(75)84644-3","article-title":"Composition of milks of dairy cattle. I. Protein, lactose, and fat contents and distribution of protein fraction","volume":"58","author":"Cerbulis","year":"1975","journal-title":"J. Dairy Sci."},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"1101","DOI":"10.1038\/2141101a0","article-title":"Effect of p H on \u03b2-Lactoglobulins","volume":"214","author":"McKenzie","year":"1967","journal-title":"Nature"},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"11646","DOI":"10.1021\/la402729g","article-title":"pH effects on the molecular structure of \u03b2-lactoglobulin modified air\u2013water interfaces and its impact on foam rheology","volume":"29","author":"Engelhardt","year":"2013","journal-title":"Langmuir"},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"28","DOI":"10.1016\/0005-2795(80)90105-1","article-title":"Spectroscopic characterization of beta-lactoglobulin-retinol complex","volume":"625","author":"Fugate","year":"1980","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"481","DOI":"10.1016\/S0969-2126(97)00205-0","article-title":"Bovine \u03b2-lactoglobulin at 1.8 \u00c5 resolution\u2014still an enigmatic lipocalin","volume":"5","author":"Brownlow","year":"1997","journal-title":"Structure"},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"2874","DOI":"10.1016\/S0021-9258(18)69686-3","article-title":"Physico-chemical comparison of \u03b2-lactoglobulins A and B","volume":"234","author":"Tanford","year":"1959","journal-title":"J. Biol. Chem."},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"164","DOI":"10.1016\/j.cocis.2005.11.001","article-title":"Mucin structure, aggregation, physiological functions and biomedical applications","volume":"11","author":"Bansil","year":"2006","journal-title":"Curr. Opin. Colloid Interface Sci."},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"395","DOI":"10.1016\/j.cocis.2010.05.015","article-title":"Mucin layers and multilayers\u2014Physicochemical properties and applications","volume":"15","author":"Svensson","year":"2010","journal-title":"Curr. Opin. Colloid Interface Sci."},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"8344","DOI":"10.1021\/la050779w","article-title":"Porcine gastric mucin (PGM) at the water\/poly (dimethylsiloxane) (PDMS) interface: Influence of pH and ionic strength on its conformation, adsorption, and aqueous lubrication properties","volume":"21","author":"Lee","year":"2005","journal-title":"Langmuir"},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"9687","DOI":"10.1021\/acs.langmuir.6b02057","article-title":"Structural and mechanical properties of thin films of bovine submaxillary mucin versus porcine gastric mucin on a hydrophobic surface in aqueous solutions","volume":"32","author":"Madsen","year":"2016","journal-title":"Langmuir"},{"key":"ref_16","doi-asserted-by":"crossref","unstructured":"Lakowicz, J.R. (1999). Instrumentation for fluorescence spectroscopy. Principles of Fluorescence Spectroscopy, Springer.","DOI":"10.1007\/978-1-4757-3061-6"},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"1046","DOI":"10.1016\/j.foodchem.2011.01.079","article-title":"Milk \u03b2-lactoglobulin complexes with tea polyphenols","volume":"127","author":"Kanakis","year":"2011","journal-title":"Food Chem."},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"4114","DOI":"10.1021\/jf400711d","article-title":"Interactions of \u03b2-lactoglobulin variants A and B with vitamin A. Competitive binding of retinoids and carotenoids","volume":"61","author":"Mensi","year":"2013","journal-title":"J. Agric. Food Chem."},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"2023","DOI":"10.1016\/j.foodchem.2011.12.043","article-title":"Study of the acid and thermal stability of \u03b2-lactoglobulin\u2013ligand complexes using fluorescence quenching","volume":"132","author":"Liang","year":"2012","journal-title":"Food Chem."},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"234","DOI":"10.1016\/j.foodchem.2016.04.048","article-title":"Complexation of bovine \u03b2-lactoglobulin with malvidin-3-O-glucoside and its effect on the stability of grape skin anthocyanin extracts","volume":"209","author":"He","year":"2016","journal-title":"Food Chem."},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"79","DOI":"10.1016\/0301-4622(96)00009-9","article-title":"Use of fluorescence decay times of 8-ANS-protein complexes to study the conformational transitions in proteins which unfold through the molten globule state","volume":"60","author":"Uversky","year":"1996","journal-title":"Biophys. Chem."},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"1893","DOI":"10.1021\/bi00870a016","article-title":"Cooperative effects in binding by bovine serum albumin. I. The binding of 1-anilino-8-naphthalenesulfonate. Fluorimetric titrations","volume":"5","author":"Daniel","year":"1966","journal-title":"Biochemistry"},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"1700","DOI":"10.1016\/j.bbapap.2009.08.007","article-title":"Kinetics and thermodynamics of the interaction of 1-anilino-naphthalene-8-sulfonate with proteins","volume":"1794","author":"Cattoni","year":"2009","journal-title":"Biochim. Biophys. Acta (BBA)-Proteins Proteom."},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"194","DOI":"10.1016\/S0167-4838(99)00105-3","article-title":"Evidence of heterogeneous 1-anilinonaphthalene-8-sulfonate binding to \u03b2-lactoglobulin from fluorescence spectroscopy","volume":"1432","author":"Collini","year":"1999","journal-title":"Biochim. Biophys. Acta (BBA)-Protein Struct. Mol. Enzymol."},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"1968","DOI":"10.1110\/ps.9.10.1968","article-title":"New insight on \u03b2-lactoglobulin binding sites by 1-anilinonaphthalene-8-sulfonate fluorescence decay","volume":"9","author":"Collini","year":"2000","journal-title":"Protein Sci."},{"key":"ref_26","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","year":"2000","journal-title":"J. Agric. Food Chem."},{"key":"ref_27","first-page":"4049","article-title":"Monitoring the Tanford transition in \u03b2-lactoglobulin by 8-anilino-1-naphthalene sulfonate and mass spectrometry","volume":"22","author":"Santambrogio","year":"2008","journal-title":"Rapid Commun. Mass Spectrom. Int. J. Devoted Rapid Dissem. Up-to-the-Minute Res. Mass Spectrom."},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"427","DOI":"10.1016\/j.foodchem.2017.02.027","article-title":"Molecular study of mucin-procyanidin interaction by fluorescence quenching and Saturation Transfer Difference (STD)-NMR","volume":"228","author":"Silva","year":"2017","journal-title":"Food Chem."},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"125795","DOI":"10.1016\/j.foodchem.2019.125795","article-title":"Instantaneous interaction of mucin with pectin-and carrageenan-coated nanoemulsions","volume":"309","author":"Celli","year":"2020","journal-title":"Food Chem."},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"589","DOI":"10.1042\/bj2820589","article-title":"Spectrofluorimetric assessment of the surface hydrophobicity of proteins","volume":"282","author":"Cardamone","year":"1992","journal-title":"Biochem. J."},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"618","DOI":"10.1016\/0005-2795(75)90168-3","article-title":"A conformational change in bovine \u03b2-lactoglobulin at low pH","volume":"379","author":"Mills","year":"1975","journal-title":"Biochim. Biophys. Acta (BBA)-Protein Struct."},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"461","DOI":"10.1016\/0969-8043(95)00311-8","article-title":"Effect of solvent on the fluorescence quenching of organic liquid scintillators by aniline and carbon tetrachloride","volume":"47","author":"Giraddi","year":"1996","journal-title":"Appl. Radiat. Isot."},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"158","DOI":"10.1021\/jf048693g","article-title":"Interaction of flavonoids with bovine serum albumin: A fluorescence quenching study","volume":"53","author":"Papadopoulou","year":"2005","journal-title":"J. Agric. Food Chem."},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"1250","DOI":"10.1016\/S0006-3495(99)77288-7","article-title":"pH-dependent conformational change of gastric mucin leads to sol-gel transition","volume":"76","author":"Cao","year":"1999","journal-title":"Biophys. J."},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"12170","DOI":"10.1016\/S0021-9258(20)71335-9","article-title":"Hydrophobic binding properties of bovine gallbladder mucin","volume":"259","author":"Smith","year":"1984","journal-title":"J. Biol. Chem."},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"431","DOI":"10.1016\/j.foodchem.2016.06.105","article-title":"Characterization of flavonoid-protein interactions using fluorescence spectroscopy: Binding of pelargonidin to dairy proteins","volume":"213","author":"McClements","year":"2016","journal-title":"Food Chem."},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"13635","DOI":"10.1021\/bi9907835","article-title":"8-anilino-1-naphthalene sulfonic acid (ANS) induces folding of acid unfolded cytochrome c to molten globule state as a result of electrostatic interactions","volume":"38","author":"Ali","year":"1999","journal-title":"Biochemistry"},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"57","DOI":"10.1016\/j.foodhyd.2015.09.013","article-title":"Investigation of the interaction between mucins and \u03b2-lactoglobulin under tribological stress","volume":"54","author":"Chronakis","year":"2016","journal-title":"Food Hydrocoll."},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"64","DOI":"10.1080\/10408398.2018.1512950","article-title":"Interactions of salivary mucins and saliva with food proteins: A review","volume":"60","author":"Lee","year":"2020","journal-title":"Crit. Rev. Food Sci. Nutr."}],"container-title":["Molecules"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/1420-3049\/26\/22\/6799\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,11]],"date-time":"2025-10-11T07:28:19Z","timestamp":1760167699000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/1420-3049\/26\/22\/6799"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2021,11,10]]},"references-count":39,"journal-issue":{"issue":"22","published-online":{"date-parts":[[2021,11]]}},"alternative-id":["molecules26226799"],"URL":"https:\/\/doi.org\/10.3390\/molecules26226799","relation":{},"ISSN":["1420-3049"],"issn-type":[{"value":"1420-3049","type":"electronic"}],"subject":[],"published":{"date-parts":[[2021,11,10]]}}}