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Milk protein hydrolysates activate 5-HT2C serotonin receptors: influence of the starting substrate and isolation of bioactive fractions

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dc.contributor.author Nongonierma, Alice B.
dc.contributor.author Schellekens, Harriët
dc.contributor.author Dinan, Timothy G.
dc.contributor.author Cryan, John F.
dc.contributor.author Fitzgerald, Richard J.
dc.date.accessioned 2017-04-13T08:21:59Z
dc.date.available 2017-04-13T08:21:59Z
dc.date.issued 2013
dc.identifier.citation Nongonierma, AB,Schellekens, H,Dinan, TG,Cryan, JF,FitzGerald, RJ (2013) 'Milk protein hydrolysates activate 5-HT2C serotonin receptors: influence of the starting substrate and isolation of bioactive fractions'. Food & Function, 5 (4) :728-737. en_US
dc.identifier.uri http://hdl.handle.net/10344/5705
dc.description peer-reviewed en_US
dc.description.abstract Milk protein hydrolysates generated with different starting substrates, including sodium caseinate (NaCN), acid casein (Acid CN), skim milk powder (SMP) and glycomacropeptide (GMP) were demonstrated to behave as serotonin 2C (5-HT2C) receptor agonists. The 5-HT2C receptor activating potential of NaCN hydrolysates correlated with an increased protein hydrolysis, most likely due to enhanced release of bioactive peptides over the time course of hydrolysis. In its unhydrolysed form, GMP was the only starting substrate showing 5-HT2C serotonin receptor agonist activity. The 5-HT2C serotonin receptor agonist activity of its corresponding hydrolysate (GMPH-240 min) was significantly higher (P < 0.05). Fractionation of the 240 min NaCNH using ultrafiltration (UF), solid-phase extraction (SPE), semipreparative reverse-phase high performance liquid chromatography (RP-HPLC) and isoelectric focusing (IEF) was carried out. Characterisation of the fractions obtained shows that the bioactive peptides had a relatively low molecular mass (<1 kDa), were hydrophobic in nature and had a pI between 8.6 and 13.2. These different physicochemical characteristics together with the stability of NaCNH-240 min to simulated intestinal digestion, allow prediction of a favourable outcome regarding the bioavailability of the bioactive peptides therein. These results reinforce the potential of milk-derived bioactive peptides to be developed into functional foods targeted at 5-HT2C receptor modulation. en_US
dc.language.iso eng en_US
dc.publisher Royal Society of Chemistry en_US
dc.relation.ispartofseries Food and Function;5 (4), pp. 728-737
dc.relation.uri http://dx.doi.org/10.1039/c3fo30309h
dc.rights Personal use of this material is permitted. Permission from Royal Society of Chemistry must be obtained for all other uses. en_US
dc.subject alpha-lactalbumin increases en_US
dc.subject neutral amino-acids en_US
dc.subject whey proteins en_US
dc.subject appetite expression en_US
dc.title Milk protein hydrolysates activate 5-HT2C serotonin receptors: influence of the starting substrate and isolation of bioactive fractions en_US
dc.type info:eu-repo/semantics/article en_US
dc.type.supercollection all_ul_research en_US
dc.type.supercollection ul_published_reviewed en_US
dc.date.updated 2017-04-10T18:23:32Z
dc.description.version ACCEPTED
dc.identifier.doi 10.1039/c3fo30309h
dc.contributor.sponsor EI en_US
dc.relation.projectid CC20080001 en_US
dc.rights.accessrights info:eu-repo/semantics/openAccess en_US
dc.internal.rssid 1438307
dc.internal.copyrightchecked Yes
dc.identifier.journaltitle Food & Function
dc.description.status peer-reviewed


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