Data/hora: 11/06/2024 09:45:28

Biblioteca(s): 	Embrapa Pecuária Sudeste.	
Tipo da produção científica: 	Artigo em Periódico Indexado	
Circulação/Nível: 	A - 2	
Data corrente: 	21/12/2023	
Data da última atualização: 	21/12/2023	
Autoria: 	CAVALCANTE, K. N.; FEITOR, J. F.; MORAIS, S. T. B.; NASSU, R. T.; AHRNÉ, L. M.; CARDOSO, D. R.	
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.	
Título: 	Impact of UV-C pretreatment on B-lactoglobulin hydrolysis by trypsin: production and bioavailability of bioactive peptides.	
Ano de publicação: 	2023	
Fonte/Imprenta: 	International Dairy Journal, v. 142, july 2023, 105650.	
Páginas: 	12 p.	
DOI: 	10.1016/j.idairyj.2023.105650	
Idioma: 	Inglês	
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.	
Palavras-Chave: 	Bioactive peptides; LTLT; Luz UV-C; MALDI TOF TOF-MS; Peptídeos bioativos; Redução de alergenicidade.	
Thesagro: 	Tripsina.	
Categoria do assunto: 	Q Alimentos e Nutrição Humana	
Registro original: 	Embrapa Pecuária Sudeste (CPPSE)	
Exemplares: 	CPPSE - (26268-1) - UPC - AP - DD - PROCI-2023.00126 - CAV - 2023.00299 - DIS