Nutraceutical and functional food bioactive peptides in beef

dc.check.date10000-01-01
dc.check.embargoformatHard bound copy in Library onlyen
dc.check.infoIndefiniteen
dc.check.opt-outYesen
dc.check.reasonThis thesis is due for publication or the author is actively seeking to publish this materialen
dc.check.typeNo Embargo Required
dc.contributor.advisorFitzgerald, Gerald F.en
dc.contributor.authorRyan, Joseph Thomas
dc.contributor.funderScience Foundation Irelanden
dc.contributor.funderDepartment of Agriculture, Fisheries and Food, Irelanden
dc.date.accessioned2014-02-03T17:24:34Z
dc.date.issued2013
dc.date.submitted2013
dc.description.abstractIn recent years, the potential to positively modulate human health through dietary approaches has received considerable attention. Bioactive peptides which are released during the hydrolysis or fermentation of food proteins or following digestion may exert beneficial physiological effects in vivo. The aim of this work was to isolate, characterise and evaluate Angiotensin-І-converting enzyme (ACE-І) inhibitory, antimicrobial and antioxidant peptides from the bovine myofibrillar proteins actin and myosin. In order to generate these peptides, the myofibrillar proteins actin and myosin were hydrolysed with digestive enzymes pepsin, trypsin and α-chymotrypsin, or with the industrial thermolysin-like enzyme “Thermoase”, Amano Inc. It was found that each hydrolysate generated contained peptides which possessed ACE inhibitory, antioxidant and antimicrobial activity. The peptides responsible in part for the observed ACE inhibitory, antioxidant and antimicrobial activity of a number of hydrolysates were isolated using the method of RP-HPLC and the bioactive peptides contained within each active fraction was determined using either MALDI-TOF MS/MS or N-terminal peptide sequencing. During the course of this thesis six ACE inhibitory and five antimicrobial peptides were identified. It was determined that the reported antioxidant activity was a direct result of a number of peptides working in synergy with each other. The IC50 values of the six ACE inhibitory peptides ranged in values of 6.85 to 75.7 µM which compare favourably to values previously reported for other food derived ACE inhibitory peptides, particularly the well known milk peptides IPP and VPP, IC50 values of 5 and 9 µM respectively. All five antimicrobial peptides identified in this thesis displayed activity against Escherichia coli, Salmonella typhimurium, Staphylococcus aureus and Listeria innocua with MIC values ranging from 0.625 to10 mM. The activity of each antimicrobial peptide was strain specific. Furthermore the role and importance of charged amino acids to the activity of antimicrobial peptides was also determined. Generally the removal of charged amino acids from the sequence of antimicrobial peptides resulted in a loss of antimicrobial activity. In conclusion, this thesis revealed that a range of bioactive peptides exhibiting ACE inhibitory, antioxidant and antimicrobial activities were encrypted in bovine myofibrillar proteins that could be released using digestive and industrial enzymes. Finally enzymatic hydrolysates of muscle proteins could potentially be incorporated into functional foods; however, the potential health benefits would need to be proven in human clinical studies.en
dc.description.statusNot peer revieweden
dc.description.versionAccepted Version
dc.format.mimetypeapplication/pdfen
dc.identifier.citationRyan, J. T. 2013. Nutraceutical and functional food bioactive peptides in beef. PhD Thesis, University College Cork.en
dc.identifier.urihttps://hdl.handle.net/10468/1361
dc.language.isoenen
dc.publisherUniversity College Corken
dc.rights© 2013, Joseph T. Ryan.en
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/3.0/en
dc.subjectBeefen
dc.subjectAntioxidanten
dc.subjectAngiotensin 1-converting enzymeen
dc.subjectBioactive peptidesen
dc.subjectAntimicrobialen
dc.subject.lcshAnti-infective agentsen
dc.subject.lcshAntioxidantsen
dc.thesis.opt-outtrue
dc.titleNutraceutical and functional food bioactive peptides in beefen
dc.typeDoctoral thesisen
dc.type.qualificationlevelDoctoralen
dc.type.qualificationnamePhD (Science)en
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