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The present study examined the effect of different heat treatments; (1) chilled, (2) boiled at 100°C for 30 min, and (3) autoclaved at 121°C at 15 psi for 20 min, on the expression of goat skeletal muscle proteins using two-dimensional gel electrophoresis. The molecular weight (MW) and isoelectric point (pI) of heat stable proteins were characterised followed by identification of the proteins by MALDI-TOF/TOF mass spectrometry. There were 153 protein spots obtained in the boiled samples, while only 46 protein spots were observed in the autoclaved samples. Thirteen spots that exhibited high intensity of protein were chosen from the autoclaved sample for MALDI-TOF/TOF mass spectrometry analysis. The putative heat stable proteins identified were myosin light chain (MLC), actin, tropomyosin (TPM), troponin T (TnT), myoglobin, and creatine kinase. The Proc-GLM analysis revealed that the heat treatments have resulted in significant differences in spot intensities of actin, troponin T (TnT), myoglobin, and creatine kinase with no significant changes noted in other proteins. [ABSTRACT FROM AUTHOR]

Different heat treatments, (1) chilled, 4°C (2) boiled at 100°C for 30 min and (3) autoclaved at 121°C at 15 psi for 20 min were employed on goat meat to mimic domestic and industrial cooking. The effects on intensity of actin proteins was observed using two-dimensional gel electrophoresis where significant differences (p>0.05) were observed in the spot intensity between chilled and boiled samples, similarly in chilled and autoclaved samples. However, no significant difference was observed between boiled and autoclaved samples. The slight changes observed in the cooking of meat confirmed that actin protein is susceptible to denaturation cause by heat. MALDI-TOF/TOF analysis revealed the peptide-mass fingerprint between positions 21 - 374 that not affected by heat treatment. Peptides from this position merit the candidature of actin as putative thermostable marker for detecting goat meat (chevon) in food product. [ABSTRACT FROM AUTHOR]

The purpose of this study was to identify porcine-specific peptide markers from thermally processed meat that could differentiate pork from beef, chevon and chicken meat. In the initial stage, markers from tryptic digested protein of chilled, boiled and autoclaved pork were identified using LC-QTOF-MS. An MRM method was then established for verification. A thorough investigation of LC-QTOF-MS data showed that only seven porcine-specific peptides were consistently detected. Among these peptides, two were derived from lactate dehydrogenase, one from creatine kinase, and four from serum albumin protein. However, MRM could only detect four peptides (EVTEFAK, LVVITAGAR, FVIER and TVLGNFAAFVQK) that were consistently present in pork samples. In conclusion, meat species determination through a tandem mass spectrometry platform shows high potential in providing scientifically valid and reliable results even at peptide level. Besides, the specificity and selectivity offered by the proteomics approach also provide a robust platform for Halal authentication., (Copyright © 2015 Elsevier Ltd. All rights reserved.)