| Texto completo | |
| Autor(es): |
Cavalcante, Keila N.
;
Feitor, Jessica F.
;
Morais, Sinara T. B.
;
Nassu, Renata T.
;
Ahrne, Lilia M.
;
Cardoso, Daniel R.
Número total de Autores: 6
|
| Tipo de documento: | Artigo Científico |
| Fonte: | INTERNATIONAL DAIRY JOURNAL; v. 142, p. 12-pg., 2023-03-31. |
| Resumo | |
The 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 fi-lactoglobulin were compared. Compared with native or LTLT pasteurised samples, the hydrolysis rate constant of fi-lactoglobulin treated with UV-C increased significantly, implying that the protein backbone cleavage sites became more accessible, whereas ther-mal treatment produced aggregates that impede trypsin activity. Tryptic hydrolyses of UV-C light treated fi-lactoglobulin yielded more peptides and a more diverse peptide mass profile. Six bioactive peptides were revealed in fi-LG tryptic hydrolysates of UV-C-treated protein; transepithelial transport in Caco-2 cell monolayers showed intermediate in vivo transport and absorption for three (fi-LG f87-91, fi-LG f91-99, and fi-LG f158-164). The moderate allergen peptide LSFNPTQLEEQCHI fi-LG was absent after tryptic hydrolysis of UV-C-treated protein, indicating that UV-C photolysis may be a useful tool for allergenicity reduction. (c) 2023 Elsevier Ltd. All rights reserved. (AU) | |
| Processo FAPESP: | 17/01189-0 - Novel aging: tecnologias e soluções para fabricar novos produtos lácteos para um envelhecimento saudável |
| Beneficiário: | Daniel Rodrigues Cardoso |
| Modalidade de apoio: | Auxílio à Pesquisa - Temático |