Characterization of Conjugates between α-Lactalbumin and Benzyl Isothiocyanate—Effects on Molecular Structure and Proteolytic Stability

dc.contributor.authorSpöttel, Jenny
dc.contributor.authorBrockelt, Johannes
dc.contributor.authorFalke, Sven
dc.contributor.authorRohn, Sascha
dc.date.accessioned2021-11-08T12:11:24Z
dc.date.available2021-11-08T12:11:24Z
dc.date.issued2021-10-15
dc.date.updated2021-11-04T23:25:15Z
dc.description.abstractIn complex foods, bioactive secondary plant metabolites (SPM) can bind to food proteins. Especially when being covalently bound, such modifications can alter the structure and, thus, the functional and biological properties of the proteins. Additionally, the bioactivity of the SPM can be affected as well. Consequently, knowledge of the influence of chemical modifications on these properties is particularly important for food processing, food safety, and nutritional physiology. As a model, the molecular structure of conjugates between the bioactive metabolite benzyl isothiocyanate (BITC, a hydrolysis product of the glucosinolate glucotropaeolin) and the whey protein α-lactalbumin (α-LA) was investigated using circular dichroism spectroscopy, anilino-1-naphthalenesulfonic acid fluorescence, and dynamic light scattering. Free amino groups were determined before and after the BITC conjugation. Finally, mass spectrometric analysis of the BITC-α-LA protein hydrolysates was performed. As a result of the chemical modifications, a change in the secondary structure of α-LA and an increase in surface hydrophobicity and hydrodynamic radii were documented. BITC modification at the ε-amino group of certain lysine side chains inhibited tryptic hydrolysis. Furthermore, two BITC-modified amino acids were identified, located at two lysine side chains (K32 and K113) in the amino acid sequence of α-LA.en
dc.description.sponsorshipDFG, 414044773, Open Access Publizieren 2021 - 2022 / Technische Universität Berlinde
dc.identifier.eissn1420-3049
dc.identifier.urihttps://depositonce.tu-berlin.de/handle/11303/13826
dc.identifier.urihttp://dx.doi.org/10.14279/depositonce-12602
dc.language.isoenen
dc.rights.urihttps://creativecommons.org/licenses/by/4.0/en
dc.subject.ddc540 Chemie und zugeordnete Wissenschaftende
dc.subject.otherrotein modificationsen
dc.subject.otherα-lactalbuminen
dc.subject.otherwhey proteinsen
dc.subject.otherbenzyl isothiocyanateen
dc.subject.othercd spectroscopyen
dc.subject.otherhydrophobicityen
dc.subject.otherhydrodynamic radiusen
dc.subject.othertryptic digestionen
dc.subject.othermass spectrometric analysisen
dc.titleCharacterization of Conjugates between α-Lactalbumin and Benzyl Isothiocyanate—Effects on Molecular Structure and Proteolytic Stabilityen
dc.typeArticleen
dc.type.versionpublishedVersionen
dcterms.bibliographicCitation.articlenumber6247en
dcterms.bibliographicCitation.doi10.3390/molecules26206247en
dcterms.bibliographicCitation.issue20en
dcterms.bibliographicCitation.journaltitleMoleculesen
dcterms.bibliographicCitation.originalpublishernameMDPIen
dcterms.bibliographicCitation.originalpublisherplaceBaselen
dcterms.bibliographicCitation.volume26en
tub.accessrights.dnbfreeen
tub.affiliationFak. 3 Prozesswissenschaften::Inst. Lebensmitteltechnologie und Lebensmittelchemie::FG Lebensmittelchemie und Analytikde
tub.affiliation.facultyFak. 3 Prozesswissenschaftende
tub.affiliation.groupFG Lebensmittelchemie und Analytikde
tub.affiliation.instituteInst. Lebensmitteltechnologie und Lebensmittelchemiede
tub.publisher.universityorinstitutionTechnische Universität Berlinen

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