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Gibney E.R.,Food For Health Ireland
Heredity | Year: 2010

Transcription, translation and subsequent protein modification represent the transfer of genetic information from the archival copy of DNA to the short-lived messenger RNA, usually with subsequent production of protein. Although all cells in an organism contain essentially the same DNA, cell types and functions differ because of qualitative and quantitative differences in their gene expression. Thus, control of gene expression is at the heart of differentiation and development. Epigenetic processes, including DNA methylation, histone modification and various RNA-mediated processes, are thought to influence gene expression chiefly at the level of transcription; however, other steps in the process (for example, translation) may also be regulated epigenetically. The following paper will outline the role epigenetics is believed to have in influencing gene expression. © 2010 Macmillan Publishers Limited All rights reserved.


Nongonierma A.B.,Food For Health Ireland | FitzGerald R.J.,Food For Health Ireland
Journal of Functional Foods | Year: 2013

Dipeptides with a C terminal Pro inhibit dipeptidyl peptidase IV (DPP-IV), a key enzyme in incretin hormone processing. It was hypothesised that tri- and tetrapeptides with a proline at the C-terminus may also be DPP-IV inhibitors. Therefore, an in silico hydrolysis approach was used to release short (4≤amino acids) C terminal Pro peptides from the individual caseins which constitute Pro rich substrates. This was achieved using theoretical digestion of caseins with a prolyl oligopeptidase activity. Fifteen peptides were subsequently selected for in vitro DPP-IV inhibitory analysis. Stability of these peptides to gastrointestinal enzymes was also evaluated in silico and the predicted breakdown peptides were assessed for their DPP-IV inhibitory and antioxidant potential. New DPP-IV inhibitors were identified, the most potent being Phe-Leu-Gln-Pro (IC50 65.3±3.5μM). A low in vitro antioxidant (2,2-diphenyl-1-picrylhydrazyl (DPPH) scavenging) activity was also associated with the peptides studied. The strategy presented highlights the utility of employing an in silico approach for the prediction of food-derived peptides with a potential role in glycaemic management for subsequent development of functional foods. © 2013 Elsevier Ltd.


Feeney E.,Food For Health Ireland
Nutrition Bulletin | Year: 2011

A variation exists in the ability of individuals to detect bitterness from a group of compounds called 'thiourea' which are found in foods such as cruciferous vegetables. This has led to people being categorised as either super, medium or non-tasters, and is due in part to single nucleotide polymorphisms (SNP) of a bitter taste receptor gene, taste receptor, type 2 (TAS2R)38. The density of fungiform papillae (FP) which houses the taste buds may also affect taster status, and may lead to supertasters being more sensitive to oral sensations such as burn from chillies and textural properties from fats, and even fibre in bread. The TAS2R38 genotype and FP density may contribute to food choice, particularly glucosinolates which are found in cruciferous vegetables containing a thiourea component. This paper will review the literature available on supertasting and how it may influence food choices. © 2011 The Author. Journal compilation © 2011 British Nutrition Foundation.


Nongonierma A.B.,Food For Health Ireland | Fitzgerald R.J.,Food For Health Ireland
Food and Function | Year: 2013

Twenty seven Trp containing dipeptides were evaluated for their ability to inhibit dipeptidyl peptidase IV (DPP-IV), a key enzyme involved in incretin hormone processing. Novel DPP-IV inhibitors were identified comprising of three potent dipeptides (Trp-Arg, Trp-Lys and Trp-Leu) with half maximum inhibitory concentration (IC50 values) <45 μM. With the exception of Leu-Trp which was ∼20 times less potent than Trp-Leu, their reverse peptide did not inhibit DPP-IV. Trp-Asp was the only peptide studied herein with an N terminal Trp residue which was not a DPP-IV inhibitor. Phosphorylation resulted in an increase in DPP-IV IC50, giving values of 482.1 ± 12.9 and >11 000 μM for Trp-Thr and Trp-pThr, respectively. The mode of inhibition of these peptides was studied using Lineweaver and Burk kinetic analysis, which showed both competitive and non-competitive modes of inhibition depending on the peptide sequence. This suggested binding of the peptide inhibitors to different locations on DPP-IV. In silico analysis of the milk proteome revealed that some of the DPP-IV inhibitors identified herein may be released from milk proteins following enzymatic digestion. The results are relevant to understanding the mechanism(s) involved in DPP-IV inhibition by short peptides. This in turn may dictate a more targeted approach for the release of potent peptides from milk proteins with the view of developing biofunctional hydrolysates for the management of type 2 diabetes. © 2013 The Royal Society of Chemistry.


Nongonierma A.B.,Food For Health Ireland | Fitzgerald R.J.,Food For Health Ireland
Peptides | Year: 2013

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. © 2012 Elsevier Inc.


Brennan L.,Food For Health Ireland
Progress in Nuclear Magnetic Resonance Spectroscopy | Year: 2014

Metabolomics is the study of metabolites present in biological samples such as biofluids, tissue/cellular extracts and culture media. Measurement of these metabolites is achieved through use of analytical techniques such as NMR and mass spectrometry coupled to liquid chromatography. Combining metabolomic data with multivariate data analysis tools allows the elucidation of alterations in metabolic pathways under different physiological conditions. Applications of NMR-based metabolomics have grown in recent years and it is now widely used across a number of disciplines. The present review gives an overview of the developments in the key steps involved in an NMR-based metabolomics study. Furthermore, there will be a particular emphasis on the use of NMR-based metabolomics in nutrition research. © 2014 Elsevier B.V. All rights reserved.


Bleiel J.,Food For Health Ireland
International Dairy Journal | Year: 2010

Functional foods have become the corner stone of food innovation in the past few years. All big food companies are investing in functional foods because the mega trends in society seem to require healthy food with added benefits to improve the health, wellness and quality of life of people. The food companies have not only adapted their strategies and their communication to the health awareness and request of consumers but they have also changed their innovation process. And yet, there are more failures of functional food products out in the markets than there are global successes. The analysis of this phenomenon shows that the invention of new food products has to start in the mind of the consumers. A consequent orientation at consumer insights, translated into relevant, noticeable benefits, added to trustworthy and adequate brands, may be one potential route to market success. © 2009 Elsevier Ltd. All rights reserved.


Nongonierma A.B.,Food For Health Ireland | Fitzgerald R.J.,Food For Health Ireland
Food Chemistry | Year: 2014

In silico digestion of milk protein-derived peptides with gastrointestinal enzyme activities was used to predict the release of peptides with a Pro residue at position 2 from the N terminus. These peptides are known to act as preferred dipeptidyl peptidase IV (DPP-IV) substrates. Five casein-derived synthetic peptides (Ile-Pro-Ile-Gln-Tyr, Leu-Pro-Leu-Pro-Leu, Tyr-Pro-Tyr-Tyr, Leu-Pro-Tyr-Pro-Tyr and Ile-Pro-Ile) and a casein (CasH), whey (WPH) and lactoferrin hydrolysate (LFH) generated with gastrointestinal enzymes were incubated with DPP-IV at 37 C for 18 or 24 h. Peptide breakdown was evident following incubation with DPP-IV. Different modes of DPP-IV inhibition were observed depending on the test compound. Ile-Pro-Ile-Gln-Tyr, Tyr-Pro-Tyr-Tyr and Leu-Pro-Tyr-Pro-Tyr were substrate-, Leu-Pro-Leu-Pro-Leu and CasH were prodrug- while WPH and LFH were true DPP-IV inhibitors. These results are relevant for the bioactivity and bioavailability of functional foods targeting DPP-IV inhibition with potential blood glucose regulatory properties in humans. © 2013 Elsevier Ltd. All rights reserved.


Nongonierma A.B.,Food For Health Ireland | Fitzgerald R.J.,Food For Health Ireland
Peptides | Year: 2012

Of twelve dipeptides tested, only the Trp containing peptides Val-Trp and its reverse peptide Trp-Val showed a xanthine oxidase (XO) inhibitory activity. Studies with Val and Trp revealed that XO inhibition was mainly attributed to the Trp residue. No significant difference (P ≥ 0.05) was found for the XO inhibitory potency (IC50) values for Trp, Val-Trp and Trp-Val, which were about 200 times higher than that for Allopurinol. Lineweaver and Burke analysis demonstrated that Trp, Val-Trp and Trp-Val were non-competitive inhibitors while Allopurinol was a competitive inhibitor. Of the different milk-protein substrates hydrolyzed with gastro-intestinal enzyme activities, only lactoferrin (LF) hydrolyzates displayed XO inhibition. Peptides present in a LF hydrolyzate (GLF-240 min) were adsorbed onto activated carbon followed by subsequent desorption with stepwise elution using acetonitrile (ACN). Separation and detection of Trp containing peptides within the different fractions were achieved using RP-HPLC coupled with fluorescence detection. The desorbed fractions displayed different XO inhibitory properties, with no inhibition in the unbound fraction and highest inhibition in fractions eluted with 30, 40 and 70% ACN. The fraction eluting at 40% ACN was significantly more potent (19.1 ± 2.3% inhibition at 1.25 mg mL-1) than the GLF-240 min hydrolyzate (13.4 ± 0.4% inhibition at 1.25 mg mL-1), showing the potential for enrichment of the bioactive peptides on fractionation with activated carbon. © 2012 Elsevier Inc.


Mills S.,Food For Health Ireland
Annual review of food science and technology | Year: 2011

There is an increased desire for sophisticated foods, whereby consumers harbor higher expectations of health-promoting benefits above basic nutrition. Moreover, there is a move from the adulteration of foods with chemical preservatives toward biopreservation. Such expectations have led scientists to identify novel approaches to satisfy both demands, which utilize bacteriocin and peptide-based solutions. The best known examples of biopreservation involve bacteriocins. However, with the exception of nisin, bacteriocins have received limited use in the food industry. Peptides can be added to foods to improve consumer health. Some of the best known examples are angiotensin I-converting enzyme (ACE)-inhibitory peptides, which inhibit ACE, a key enzyme involved in blood pressure (BP) regulation. To be effective, these peptides must be bioavailable, but by their nature, peptides are degraded by digestion with proteolytic enzymes. This review critically discusses the use and potential of peptides and bacteriocins in food systems in terms of safety, quality, and improvement of human health.

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