UV-C light promotes the reductive cleavage of disulfide bonds in β-Lactoglobulin and improves in vitro gastric digestion
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β-Lactoglobulin (β-Lg) is the main protein in whey and is known for its allergenicity and resistance to the digestion of pepsin and trypsin. The UV-C photoinduced cleavage of disulfide bonds in β-Lactoglobulin, as promoted by excitation of tryptophan residues (Trp), is shown to induce changes in the protein's secondary structure, significantly reducing the protein's resistance to pepsin digestion. The UV-C light-induced changes in the protein secondary structure are marked by an increase in the contribution of β-sheet and α-helix structures with a concomitantly smaller contribution of the β-turn structural motif. The photoinduced cleavage of disulfide bonds in β-Lg has an apparent quantum yield of ф = 0.0015 ± 0.0003 and was shown by transient absorption laser flash photolysis to arise by two different pathways: a) the reduction of the disulfide bond Cys66Cys160 occurs by direct electron transfer from the triplet-excited 3Trp to the disulfide bond due to the existence of a CysCys/Trp triad (Cys66Cys160/Trp61) and b) the reduction of the buried Cys106Cys119 disulfide bond involves a reaction with a solvated electron originated by the photoejection of electrons from the triplet-excited 3Trp decay. The in vitro gastric digestion index for UV-C-treated β-Lg is revealed to have increased significantly by 36 ± 4 % and 9 ± 2 % under simulated elderly and young adult digestive conditions, respectively. When compared to the native protein, the peptide mass fingerprint profile of digested UV-C-treated β-Lg shows a higher content and variety of peptides, including the production of some exclusive bioactive peptides such as PMHIRL and EKFDKALKALPMH.
|Tidsskrift||Food Research International|
|Status||Udgivet - 2023|
This research is financed by FAPESP and the Innovation Fund Denmark as a part of a bilateral Brazilian-Danish collaboration [FAPESP grant number 2017/01189-0]. JFS and ATBMB thank CAPES for awarding them the PhD fellowship (Finance Code 001). The DRC thanks the National Council for Scientific and Technological Development (CNPq) for the productivity research grant grant number 309212/2019-7].
© 2023 Elsevier Ltd