Dielectric-barrier discharge (DBD) plasma treatment reduces IgG binding capacity of β-lactoglobulin by inducing structural changes

•A significant reduction (58.2%) in IgG binding capacity of β-LG was achieved.•IgG binding capacity of β-LG was related to stepwise change in its structure.•Initial drop in IgG binding capacity was caused by conformational alteration.•Further drop in IgG binding capacity was due to fragmentation of...

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Veröffentlicht in:Food chemistry 2021-10, Vol.358, p.129821-129821, Article 129821
Hauptverfasser: Liu, Zhi-Wei, Liu, Lian-Jie, Zhou, Ying-Xue, Tan, Yi-Cheng, Cheng, Jun-Hu, Bekhit, Alaa El-Din, Inam-Ur-Raheem, Muhammad, Aadil, Rana Muhammad
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Sprache:eng
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Zusammenfassung:•A significant reduction (58.2%) in IgG binding capacity of β-LG was achieved.•IgG binding capacity of β-LG was related to stepwise change in its structure.•Initial drop in IgG binding capacity was caused by conformational alteration.•Further drop in IgG binding capacity was due to fragmentation of β-LG. The present study investigated the effects of dielectric-barrier-discharge (DBD) plasma treatment (12 kHz, 40 kV) at 1, 2, 3, and 4 min on the reduction of the immunoglobulin G (IgG) binding capacity of β-lactoglobulin (β-LG). The IgG binding capacity of β-LG was reduced by 58.21% following a plasma treatment time of 4 min, as confirmed by western-blot and ELISA analyses. The reduction in IgG binding capacity of β-LG was directly related to a stepwise change in its structure. The initial drop in the IgG binding capacity of β-LG was found to be caused by conformational alteration, free sulfhydryl exposure and cross-linkage of molecules induced by oxidation of NH–/NH2– functional groups of peptide bonds and of sensitive amino acid residues (Tyr, Trp) as confirmed by SDS-PAGE, surface hydrophobicity and multi-spectroscopic analyses. Plasma treatment of more than 3 min resulted in cleavage of disulfidebonds and fragmentation of β-LG that was confirmed by LC–MS/MS analysis, which resulted a further decline in the IgG binding capacity of β-LG. Plasma treatment therefore has great potential as a substitute treatment for enzymatic hydrolysis for the production of hypoallergenic milk protein-based products.
ISSN:0308-8146
1873-7072
DOI:10.1016/j.foodchem.2021.129821