Protein and mineral characterisation of rendered meat and bone meal

• Published in: Food chemistry Vol. 134; no. 3; pp. 1267 - 1278
• Main Authors: Buckley, M., Penkman, K.E.H., Wess, T.J., Reaney, S., Collins, M.J.
• Format: Journal Article
• Language: English
• Published: Kidlington Elsevier Ltd 01.10.2012; Elsevier
• Subjects: amino acid composition; Amino Acids - analysis; Animal Feed - analysis; Animals; Biological and medical sciences; Biological Products - analysis; Cattle; Chickens; Collagen; Dietary Proteins - analysis; European Union; Food industries; Fundamental and applied biological sciences. Psychology; heat treatment; MALDI; mass spectrometry; MBM; Meat - analysis; meat and bone meal; minerals; Minerals - analysis; monitoring; new methods; Osteocalcin; quantitative analysis; rendering; Scattering, Small Angle; Sheep; species diversity; Species identification; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; structural proteins; Swine; taxonomy; temperature; X-Ray Diffraction; MBM; Osteocalcin; Species identification; Collagen; MALDI; Meat meal; Identification; Bone meal; Inorganic element; Species; Protein
• ISSN: 0308-8146; 1873-7072
• DOI: 10.1016/j.foodchem.2012.02.167

► We characterize organic and inorganic components of meat and bone meal. ► Avian MBM composition differs from mammalian MBM retaining more blood proteins. ► The proteins in bovine MBM were found to be much more degraded than in avian MBM. ► Type 1 collagen was by far the most abundant protein in MBM rendered at 133–145°C. ► Other proposed target proteins such as osteocalcin was found to be highly degraded. 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.