Show simple item record

dc.contributor.authorYu, Tzer-Yangen
dc.contributor.authorMorton, James D.en
dc.contributor.authorClerens, S.en
dc.contributor.authorDyer, J. M.en
dc.date.accessioned2017-07-16T21:49:47Z
dc.date.available2015-09-18en
dc.date.issued2015en
dc.identifier.citationYu, T-Y., Morton, J.D., Clerens, S., & Dyer, J.M. (2015). Proteomic investigation of protein profile changes and amino acid residue level modification in cooked lamb meat: the effect of boiling. Journal of Agricultural and Food Chemistry, 63, 9112-9123. doi:10.1021/acs.jafc.5b03324en
dc.identifier.issn0021-8561en
dc.identifier.urihttps://hdl.handle.net/10182/8318
dc.description.abstractHydrothermal treatment (heating in water) is a common method of general food processing and preparation. For red-meat-based foods, boiling is common; however, how the molecular level effects of this treatment correlate to the overall food properties is not yet well-understood. The effects of differing boiling times on lamb meat and the resultant cooking water were here examined through proteomic evaluation. The longer boiling time was found to result in increased protein aggregation involving particularly proteins such as glyceraldehyde-3-phosphate dehydrogenase, as well as truncation in proteins such as in α-actinin-2. Heat-induced protein backbone cleavage was observed adjacent to aspartic acid and asparagine residues. Side-chain modifications of amino acid residues resulting from the heating, including oxidation of phenylalanine and formation of carboxyethyllysine, were characterized in the cooked samples. Actin and myoglobin bands from the cooked meat per se remained visible on sodium dodecyl sulfate-polyacrylamide gel electrophoresis, even after significant cooking time. These proteins were also found to be the major source of observed heat-induced modifications. This study provides new insights into molecular-level modifications occurring in lamb meat proteins during boiling and a protein chemistry basis for better understanding the effect of this common treatment on the nutritional and functional properties of red-meat-based foods.en
dc.format.extent9112-9123en
dc.language.isoenen
dc.publisherAmerican Chemical Societyen
dc.relationThe original publication is available from - American Chemical Society - https://doi.org/10.1021/acs.jafc.5b03324en
dc.relation.urihttps://doi.org/10.1021/acs.jafc.5b03324en
dc.rights© American Chemical Societyen
dc.subjectsheepen
dc.subjectlamben
dc.subjectmeaten
dc.subjectcookingen
dc.subjectproteomicsen
dc.subjectprotein modificationsen
dc.subjectboilingen
dc.subjectFood Scienceen
dc.subject.meshMuscle, Skeletalen
dc.subject.meshAnimalsen
dc.subject.meshAmino Acidsen
dc.subject.meshMuscle Proteinsen
dc.titleProteomic investigation of protein profile changes and amino acid residue level modification in cooked lamb meat: the effect of boilingen
dc.typeJournal Article
lu.contributor.unitLincoln Universityen
lu.contributor.unitFaculty of Agriculture and Life Sciencesen
lu.contributor.unitDepartment of Wine, Food and Molecular Biosciencesen
dc.identifier.doi10.1021/acs.jafc.5b03324en
dc.subject.anzsrc0908 Food Sciencesen
dc.subject.anzsrc090801 Food Chemistry and Molecular Gastronomy (excl. Wine)en
dc.subject.anzsrc090805 Food Processingen
dc.relation.isPartOfJournal of Agricultural and Food Chemistryen
pubs.issue41en
pubs.notesDate of acceptance: 2 September 2015en
pubs.organisational-group/LU
pubs.organisational-group/LU/Agriculture and Life Sciences
pubs.organisational-group/LU/Agriculture and Life Sciences/WFMB
pubs.organisational-group/LU/Research Management Office
pubs.organisational-group/LU/Research Management Office/QE18
pubs.publication-statusPublisheden
pubs.volume63en
dc.identifier.eissn1520-5118en
lu.identifier.orcid0000-0001-9645-5568


Files in this item

Default Thumbnail

This item appears in the following Collection(s)

Show simple item record