Use este identificador para citar ou linkar para este item: https://locus.ufv.br//handle/123456789/19805
Tipo: Artigo
Título: Recovery of casein-derived peptides with in vitro inhibitory activity of angiotensin converting enzyme (ACE) using aqueous two-phase systems
Autor(es): Souza Jr, Evaldo Cardozo de
Coimbra, Jane Sélia dos Reis
Oliveira, Eduardo Basílio de
Bonomo, Renata Cristina Ferreira
Abstract: Peptides inhibiting the activity of angiotensin converting enzyme (ACE) were obtained by trypsin-catalyzed hydrolysis of bovine milk casein, performed at 37 °C, during 1, 2, 5, 8 and 24 h. Results of in vitro inhibitory activity ranged between 13.4% and 78.5%. The highest ACE inhibitory activity was evidenced for hydrolysates obtained after 2 h of reaction. Aqueous two-phase systems (ATPS) formed by polyethylene glycol of 1500 g mol−1 (PEG 1500) + sodium phosphate or potassium phosphates were produced and evaluated, in terms of partition coefficients (K) and extraction yields (y), to recovery the casein hydrolysates at room temperature. In ATPS containing sodium phosphate, the peptides showed a slightly greater affinity toward the bottom salt-rich phase (0.1 ≤ K ≤ 0.9; 5.7% ≤ y ≤ 47%). In the case of ATPS containing potassium phosphates, these molecules showed substantially greater affinity toward the top polymer-rich phase (137 ≤ K ≤ 266; y ≥ 99%). These results point out extraction using PEG 1500/potassium phosphate ATPS is an efficient technique to recover casein hydrolysates containing ACE inhibitors peptides. Outlined data will be helpful in integrating such unit operation to larger scale processes.
Palavras-chave: Bioseparation
Bovine milk
Phase equilibrium
Protein
Trypsin
Antihypertensive
Editor: Journal of Chromatography B
Tipo de Acesso: Elsevier B.V.
URI: https://doi.org/10.1016/j.jchromb.2014.10.014
http://www.locus.ufv.br/handle/123456789/19805
Data do documento: 22-Out-2014
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