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Comparison of hydrolysis time and precipitation pH in the production of caseinophosphopeptides from a casein by-product

AutorCruz-Huerta, Elvia ; García-Nebot, María José ; Miralles, Beatriz ; Recio, Isidra ; Amigo, Lourdes
Fecha de publicación2014
Citación3rd ICFD (2014)
ResumenThe production of caseinophosphopeptides (CPPs) from a casein-derived by-product generated during the manufacture of an antihypertensive hydrolysate was attempted. CPPs are phosphorylated bioactive peptides that can be released from casein by enzymatic digestion. Due to the phosphorylated serines, these peptides are relatively resistant to be further hydrolysed and it has been proposed that they could prevent the precipitation of metal ions at alkaline pH in the distal small intestine. In order to isolate CPPs from the casein fraction of milk, an enzymatic hydrolysis process is often followed by selective precipitation with calcium chloride and ethanol using pHs in the range 3.5 to 8.5. It has been reported that at pH 3.5 only peptides containing the phosphorylated cluster sequence SerP-SerP-SerP-Glu-Glu selectively precipitate from a tryptic digest of casein. However, at higher pH an increase of the recoveries of the di- and monophosphorylated peptides was observed. The objective was to investigate if the hydrolysis time and pH used for the selective precipitation could determine the characteristics of the products recovered using tandem mass spectrometry for peptide sequencing. The casein by-product was submitted to tryptic hydrolysis during 30, 60, and 120 min and further precipitated with calcium chloride and ethanol at pH 4.0, 6.0 and 8.0. The results show the low influence of the hydrolysis time and suggest that precipitation at pH 6 and 8 permit to recover a valuable CPPs fraction and use this casein-derived by-product as source of CPPs. Identification of CPPs in the samples of CN-derived by-product after being subjected to simulated gastrointestinal digestion showed that this process generates CPP sequences very similar to those produced by tryptic hydrolysis. These results suggest that this CN-derived by-product can be used as a source for CPPs after its passage through the gastrointestinal tract opening the door for its use as functional ingredient to improve mineral bioavailability.
DescripciónPóster presentado a la 3rd Internacional Conference on Food Digestion celebrada en Wageningen (Holanda) del 11 al 13 de marzo de 2014.
Aparece en las colecciones: (CIAL) Comunicaciones congresos
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