02019naa a2200289 a 450000100080000000500110000800800410001902400390006010000220009924501510012126000090027230000100028152011490029165000130144065300230145365300090147665300130148565300210149865300250151965300320154470000180157670000210159470000170161570000180163270000190165077300600166921601842023-12-21       2023    bl uuuu     u00u1 u    #d7 a10.1016/j.idairyj.2023.1056502DOI1 aCAVALCANTE, K. N.  aImpact of UV-C pretreatment on B-lactoglobulin hydrolysis by trypsinbproduction and bioavailability of bioactive peptides.h[electronic resource]  c2023  a12 p.  aThe effects of UV-C light irradiation and low-temperature long-time (LTLT) pasteurization on protein structural changes, degree of hydrolysis (DH) by trypsin, peptide profile of tryptic hydrolysates by MALDI-TOF/TOF-MS, and bioavailability of β-lactoglobulin were compared. Compared with native or LTLT pasteurised samples, the hydrolysis rate constant of β-lactoglobulin treated with UV-C increased significantly, implying that the protein backbone cleavage sites became more accessible, whereas thermal treatment produced aggregates that impede trypsin activity. Tryptic hydrolyses of UV-C light treated β-lactoglobulin yielded more peptides and a more diverse peptide mass profile. Six bioactive peptides were revealed in β-LG tryptic hydrolysates of UV-C-treated protein; transepithelial transport in Caco-2 cell monolayers showed intermediate in vivo transport and absorption for three (β-LG f87–91, β-LG f91–99, and β-LG f158–164). The moderate allergen peptide LSFNPTQLEEQCHI β-LG was absent after tryptic hydrolysis of UV-C-treated protein, indicating that UV-C photolysis may be a useful tool for allergenicity reduction.  aTripsina  aBioactive peptides  aLTLT  aLuz UV-C  aMALDI TOF TOF-MS  aPeptídeos bioativos  aRedução de alergenicidade1 aFEITOR, J. F.1 aMORAIS, S. T. B.1 aNASSU, R. T.1 aAHRNÉ, L. M.1 aCARDOSO, D. R.  tInternational Dairy Journalgv. 142, july 2023, 105650.