Protein and mineral characterisation of rendered meat and bone meal.

Autor: Buckley M; BioArCh Departments of Biology, Archaeology and Chemistry, University of York, Wentworth Way, York YO10 5DD, United Kingdom., Penkman KE; BioArCh Departments of Biology, Archaeology and Chemistry, University of York, Wentworth Way, York YO10 5DD, United Kingdom., Wess TJ; School of Optometry and Vision Sciences, Cardiff University, Maindy Road, Cathays, Cardiff, CF24 4LU, United Kingdom., Reaney S; Vetinary Laboratory Agency, West House, Station Road, Thirsk, North Yorkshire YO7 1PZ, United Kingdom., Collins MJ; BioArCh Departments of Biology, Archaeology and Chemistry, University of York, Wentworth Way, York YO10 5DD, United Kingdom.
Jazyk: angličtina
Zdroj: Food chemistry [Food Chem] 2012 Oct 01; Vol. 134 (3), pp. 1267-78. Date of Electronic Publication: 2012 Mar 14.
DOI: 10.1016/j.foodchem.2012.02.167
Abstrakt: We report the characterisation of meat and bone meal (MBM) standards (Set B-EFPRA) derived from cattle, sheep, pig and chicken, each rendered at four different temperatures (133, 137, 141 and 145 °C). The standards, prepared for an EU programme STRATFEED (to develop new methodologies for the detection and quantification of illegal addition of mammalian tissues in feeding stuffs), have been widely circulated and used to assess a range of methods for identification of the species composition of MBM. The overall state of mineral alteration and protein preservation as a function of temperature was monitored using small angle X-ray diffraction (SAXS), amino acid composition and racemization analyses. Progressive increases in protein damage and mineral alteration in chicken and cattle standards was observed. In the case of sheep and pig, there was greater damage to the proteins and alteration of the minerals at the lowest treatment temperature (133 °C), suggesting that the thermal treatments must have been compromised in some way. This problem has probably impacted upon the numerous studies which tested methods against these heat treatments. We use protein mass spectrometric methods to explore if thermostable proteins could be used to identify rendered MBM. In more thermally altered samples, so-called 'thermostable' proteins such as osteocalcin which has been proposed as a ideal target to speciate MBM were no longer detectable, but the structural protein type I collagen could be used to differentiate all four species, even in the most thermally altered samples.
(Copyright © 2012 Elsevier Ltd. All rights reserved.)
Databáze: MEDLINE
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