Bioengineering of nisin to enhance functionality against dairy pathogens
dc.check.chapterOfThesis | 4,5 | |
dc.check.embargoformat | Both hard copy thesis and e-thesis | en |
dc.check.opt-out | No | en |
dc.check.reason | This thesis is due for publication or the author is actively seeking to publish this material | en |
dc.contributor.advisor | Hill, Colin | en |
dc.contributor.advisor | Cotter, Paul D. | en |
dc.contributor.advisor | Ross, R. Paul | en |
dc.contributor.author | Healy, Brian | |
dc.contributor.funder | Department of Agriculture, Food and the Marine, Ireland | en |
dc.contributor.funder | Teagasc | en |
dc.date.accessioned | 2016-06-03T15:01:24Z | |
dc.date.issued | 2014 | |
dc.date.submitted | 2014 | |
dc.description.abstract | The bacteriocin class of antimicrobial peptides have emerged as a viable alternative to at least partially fill the void created by the end of the golden age of antibiotic discovery. Along with this potential use in a clinical setting, bacteriocins also play an important role as bio-preservatives in the food industry. This thesis focuses on a specific bacteriocin group, the lantibiotics (Lanthionine-containing antibiotics). Their numerous methods of appliance in a food setting and how their gene-encoded nature can be modified to improve on overall bioactivity and functionality are explored here. The use of a lantibiotic (lacticin 3147) producing starter culture to control the Crohn’s disease-linked pathogen Mycobacterium paratuberculosis was assessed in a raw milk cheese. Although lacticin 3147 production did not effectively control the pathogen, the study provided an impetus to employ a variety of PCR-based mutagenesis techniques with a view to the creation of enhanced lantibiotic derivatives. Through the use of these techniques, a number of enhanced derivatives were generated from the ‘hinge’ region of the nisin peptide. Furthermore, a derivative in which the three hinge amino acids were replaced with three alanines represents the first enhanced derivative of nisin to have been designed through a rational process. This derivative also formed the backbone for the creation of an active, trypsin resistant, variant. Through the employment of further mutagenesis methods a derivative was created with potential use as an oral anti-bacterial in the future. Finally a number of lead nisin derivatives were investigated to assess their anti- Streptococcus agalactiae ability, a mastitis associated pathogen. Also a system was developed to facilitate the large scale production of these candidates, or other nisin derivatives, from dairy substrates. | en |
dc.description.sponsorship | Department of Agriculture, Food and the Marine, Ireland (Food Institutional Research Measure (08/RD/C/691)) | en |
dc.description.status | Not peer reviewed | en |
dc.description.version | Accepted Version | |
dc.format.mimetype | application/pdf | en |
dc.identifier.citation | Healy, B. C. 2014. Bioengineering of nisin to enhance functionality against dairy pathogens. PhD Thesis, University College Cork. | en |
dc.identifier.endpage | 163 | en |
dc.identifier.uri | https://hdl.handle.net/10468/2696 | |
dc.language.iso | en | en |
dc.publisher | University College Cork | en |
dc.rights | © 2014, Brian C. Healy | en |
dc.rights.uri | http://creativecommons.org/licenses/by-nc-nd/3.0/ | en |
dc.subject | Nisin | en |
dc.subject | Lacticin 3147 | en |
dc.subject | Bacteriocin | en |
dc.subject | Lantibiotic | en |
dc.subject | Mutagenesis | en |
dc.subject | Bioengineering | en |
dc.subject | Streptococcus agalactiae | en |
dc.subject | Mycobacterium avium subspecies paratuberculosis | en |
dc.subject | Lactococcus lactis | en |
dc.thesis.opt-out | false | |
dc.title | Bioengineering of nisin to enhance functionality against dairy pathogens | en |
dc.type | Doctoral thesis | en |
dc.type.qualificationlevel | Doctoral | en |
dc.type.qualificationname | PhD (Science) | en |
ucc.workflow.supervisor | c.hill@ucc.ie |
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