Potential bioactive effects of casein hydrolysates on human cultured cells

Phelan, Martha; Aherne-Bruce, S. Aisling; O’Sullivan, Dara; Fitzgerald, Richard J.; O’Brien, Nora M.

doi:10.1016/j.idairyj.2008.12.004

Cited by 71 publications

(67 citation statements)

References 56 publications

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“…A similar observation was found after two hours of incubation of differentiated Caco-2 cells with a specific fraction of PPPs (Katayama et al, 2007). Likewise, an increase in CAT activity has been reported after treating Jurkat T cells for 24 h with a specific casein hydrolysate, obtained by hydrolyzing commercial sodium caseinate with proteinases (Phelan, Aherne-Bruce, O'Sullivan, FitzGerald, & O'Brien, 2009). Fig.…”

Section: Intracellular Redox Statussupporting

confidence: 80%

Caseinophosphopeptides exert partial and site-specific cytoprotection against H2O2-induced oxidative stress in Caco-2 cells

et al. 2011

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Section: Intracellular Redox Statussupporting

confidence: 80%

Caseinophosphopeptides exert partial and site-specific cytoprotection against H2O2-induced oxidative stress in Caco-2 cells

et al. 2011

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“…Whey protein hydrolysates can help decrease oxidative stress by their radical scavenging activity and by their ability to increase the production of antioxidant enzymes in vivo [13,21,31]. Similarly, caseins and casein-derived peptides have been associated with radical-scavenging properties in vitro [1,9,15,41] and with their ability to increase cellular catalase activity and GSH levels in human lymphocyte (Jurkat) cells [30]. More recently we have reported on two dipeptides, Val-Trp and Val-Trp, and different lactoferrin hydrolysates which can inhibit xanthine oxidase (XO) in vitro [28].…”

Section: Introductionmentioning

confidence: 99%

Dipeptidyl peptidase IV inhibitory and antioxidative properties of milk protein-derived dipeptides and hydrolysates

2013

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Selected synthetic dipeptides and milk protein hydrolysates were evaluated for their dipeptidyl peptidase IV (DPP-IV) inhibitory properties, and their superoxide (SO) and 2,2-diphenyl-1-picrylhydrazyl (DPPH) radical scavenging activities. DPP-IV inhibition was seen with eight out of the twelve dipeptides and 5 of the twelve hydrolysates studied. Trp-Val inhibited DPP-IV, however, inhibition was not observed with the reverse peptide Val-Trp. The most potent hydrolysate inhibitors were generated from casein (CasH2) and lactoferrin (LFH1). Two Trp containing dipeptides, Trp-Val and Val-Trp, and three lactoferrin hydrolysates scavenged DPPH. The dipeptides had higher SO EC 50 values compared to the milk protein hydrolysates (arising from three lactoferrin and one whey protein hydrolysates). Higher molecular mass fractions of the milk protein hydrolysates were associated with the SO scavenging activity. Trp-Val and one lactoferrin hydrolysate (LFH1) were multifunctional displaying both DPP-IV inhibitory and antioxidant (SO and DPPH scavenging) activities. These compounds may have potential as dietary ingredients in the management of type 2 diabetes by virtue of their ability to scavenge reactive oxygen species and to extend the half-life of incretin molecules.

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“…Antioxidant activity of sodium casein hydrolyzates has been demonstrated in cell culture of human Jurkat cells with an increase in cellular catalase activity and different effects on GSH depending on the hydrolyzate studied [69]. Milk and dairy products have also been associated with the prevention of gout in humans as they can reduce serum urate [10,11,17].…”

Section: Introductionmentioning

confidence: 99%