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 | Acesso ao texto completo restrito à biblioteca da Embrapa Pecuária Sudeste. Para informações adicionais entre em contato com cppse.biblioteca@embrapa.br. |
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Registro Completo |
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Biblioteca(s): |
Embrapa Pecuária Sudeste. |
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Data corrente: |
21/12/2023 |
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Data da última atualização: |
21/12/2023 |
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Tipo da produção científica: |
Artigo em Periódico Indexado |
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Autoria: |
CAVALCANTE, K. N.; FEITOR, J. F.; MORAIS, S. T. B.; NASSU, R. T.; AHRNÉ, L. M.; CARDOSO, D. R. |
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Afiliação: |
KEILA N. CAVALCANTE, Universidade de São Paulo; JESSICA F. FEITOR, Universidade de São Paulo; SINARA T. B. MORAIS, Universidade de São Paulo; RENATA TIEKO NASSU, CPPSE; LILIA M. AHRNÉ, University of Copenhagen; DANIEL R. CARDOSO, Universidade de São Paulo. |
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Título: |
Impact of UV-C pretreatment on B-lactoglobulin hydrolysis by trypsin: production and bioavailability of bioactive peptides. |
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Ano de publicação: |
2023 |
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Fonte/Imprenta: |
International Dairy Journal, v. 142, july 2023, 105650. |
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Páginas: |
12 p. |
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DOI: |
10.1016/j.idairyj.2023.105650 |
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Idioma: |
Inglês |
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Conteúdo: |
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 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. |
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Palavras-Chave: |
Bioactive peptides; LTLT; Luz UV-C; MALDI TOF TOF-MS; Peptídeos bioativos; Redução de alergenicidade. |
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Thesagro: |
Tripsina. |
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Categoria do assunto: |
Q Alimentos e Nutrição Humana |
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Marc: |
LEADER 02019naa a2200289 a 4500
001 2160184
005 2023-12-21
008 2023 bl uuuu u00u1 u #d
024 7 $a10.1016/j.idairyj.2023.105650$2DOI
100 1 $aCAVALCANTE, K. N.
245 $aImpact of UV-C pretreatment on B-lactoglobulin hydrolysis by trypsin$bproduction and bioavailability of bioactive peptides.$h[electronic resource]
260 $c2023
300 $a12 p.
520 $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.
650 $aTripsina
653 $aBioactive peptides
653 $aLTLT
653 $aLuz UV-C
653 $aMALDI TOF TOF-MS
653 $aPeptídeos bioativos
653 $aRedução de alergenicidade
700 1 $aFEITOR, J. F.
700 1 $aMORAIS, S. T. B.
700 1 $aNASSU, R. T.
700 1 $aAHRNÉ, L. M.
700 1 $aCARDOSO, D. R.
773 $tInternational Dairy Journal$gv. 142, july 2023, 105650.
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