0000000000496362
AUTHOR
Isidra Recio
Identification of Casein Phosphopeptides in β-casein and Commercial Hydrolysed Casein by Mass Spectrometry
Casein phosphopeptides (CPPs) in commercial hydrolysed casein (CE90CPP) and in β-CN (β-CN) after simulated gastrointestinal digestion (gastric stage pepsin, pH =2, 37°C 2h) and intestinal stage (pancreatic-bile extract, pH =5.2, 37°C 2h) were sequenced by on-line reversed-phase high performance liquid chromatography coupled to electrospray ionisation tandem mass spectrometry (RP-HPLC-ESIMS/MS). In β-CN digest five peptides that contained four to five phosphate groups and the cluster sequence SpSpSpEE (residues 17-21) were identified. All CPPs with one exception β-CN(1-24)4P, had the protein fragment β-CN(1-25)4P, which is one of the main CPPs produced in vivo digestion of casein and the re…
Antihypertensive effects of lactoferrin hydrolyzates: Inhibition of angiotensin- and endothelin-converting enzymes
The potential of bovine lactoferrin (LF) as a source of antihypertensive peptides acting on the renin-angiotensin system (RAS) and the endothelin (ET) system as dual vasopeptidase inhibitors has been examined. For this purpose enzymatic LF hydrolyzates (LFHs) were generated by trypsin and proteinase K digestions. Permeate fractions with molecular masses lower than 3 kDa (LFH <3 kDa) were orally administered to spontaneously hypertensive rats (SHRs). Although both LFHs <3 kDa showed in vitro angiotensin I-converting enzyme (ACE)-inhibitory activity, only proteinase K LFH <3 kDa exerted an in vivo antihypertensive effect. The proteinase K LFH <3 kDa and a previously characterized pepsin LFH <…
Milk versus caseinophosphopeptides added to fruit beverage: Resistance and release from simulated gastrointestinal digestion
The influence of simulated gastrointestinal digestion on caseinophosphopeptides (CPPs) formation in milk-based fruit beverage was evaluated, together with resistance of a pool of CPPs added to fruit beverage. In milk-based fruit beverage, four CPPs were identified that can be justified by their presence in raw milk or due to processing. When it was subjected to simulated gastrointestinal digestion, 10 CPPs were identified, and only 1 presented the cluster (SpSpSpEE) (3 phosphoseryl group followed by 2 glutamic acid residues), which corresponded to αs2-CN(1-19)4P. CPPs added to fruit beverage are resistant to simulated gastrointestinal digestion, and 16 CPPs were identified originating from …
Antihypertensive effect of a bovine lactoferrin pepsin hydrolysate: Identification of novel active peptides
et al.
Dairy Debaryomyces hansenii strains produce the antihypertensive casein-derived peptides LHLPLP and HLPLP
The ability of dairy Debaryomyces hansenii, Kluyveromyces lactis and Kluyveromyces marxianus strains to release the casein-derived antihypertensive sequences RYLGY, AYFYPEL, LHLPLP, HLPLP, VPP and/or IPP was examined. Yeast strains were grown in medium with casein as sole nitrogen source and the yeast casein hydrolysates (CSHs) were analysed by HPLC-MS/MS to search for the six antihypertensive sequences. Only LHLPLP and HLPLP were identified in CSHs and exclusively in D. hansenii Dh1 and Dh14 hydrolysates in which both antihypertensive sequences represented approximately 6 (CSH Dh1) and 10% (CSH Dh14) of total peptide content. In addition, a complete analysis of selected CSHs by HPLC-MS/MS …
Bioavailability of antihypertensive lactoferricin B-derived peptides: Transepithelial transport and resistance to intestinal and plasma peptidases
The transepithelial transport of the angiotensin I-converting enzyme (ACE)-inhibitory and antihypertensive lactoferricin B (LfcinB)-derived hexapeptide LfcinB20-25 (RRWQWR) and of its two main fragments RWQ and WQ were investigated using a human intestinal cell (Caco-2) monolayer. The three peptides were susceptible to the action of brush-border peptidases. Intact LfcinB20-25 was not transported across Caco-2 whereas RWQ and WQ were both absorbed through the cell monolayer. Apparent permeability (Papp) values for absorptive transport across the monolayer were 0.7×10-8cms-1 (RWQ) and 3.9×10-8cms-1 (WQ). The effect of pathway-selective inhibitors on peptide absorption suggested paracellular d…
Novel Antihypertensive Lactoferrin-Derived Peptides Produced by Kluyveromyces marxianus: Gastrointestinal Stability Profile and In Vivo Angiotensin I-Converting Enzyme (ACE) Inhibition
Novel antihypertensive peptides released by Kluyveromyces marxianus from bovine lactoferrin (LF) have been identified. K. marxianus LF permeate was fractionated by semipreparative high performance liquid chromatography and 35 peptides contained in the angiotensin I-converting enzyme (ACE)-inhibitory fractions were identified by using an ion trap mass spectrometer. On the basis of peptide abundance and common structural features, six peptides were chemically synthesized. Four of them (DPYKLRP, PYKLRP, YKLRP, and GILRP) exerted in vitro inhibitory effects on ACE activity and effectively decreased systolic blood pressure after oral administration to spontaneously hypertensive rats (SHRs). Stab…