LC-QTOF-MS identification of porcine-specific peptide in heat treated pork identifies candidate markers for meat species determination

被引:81
作者
Sarah, S. A. [1 ]
Faradalila, W. N. [1 ]
Salwani, M. S. [1 ]
Amin, I. [1 ,3 ]
Karsani, S. A. [4 ,5 ]
Sazili, A. Q. [1 ,2 ]
机构
[1] Univ Putra Malaysia, Halal Prod Res Inst, Serdang, Malaysia
[2] Univ Putra Malaysia, Fac Agr, Dept Anim Sci, Serdang, Malaysia
[3] Univ Putra Malaysia, Fac Med & Hlth Sci, Dept Nutr & Dietet, Serdang, Malaysia
[4] Univ Malaya, Inst Biol Sci, Kuala Lumpur, Malaysia
[5] Univ Malaya, Ctr Prote Res, Kuala Lumpur, Malaysia
关键词
Species authentication; Mass spectrometry; Peptide marker; MRM and Halal; ANALYSIS MASS-SPECTROMETRY; COOKED MEAT; BIOMARKER DISCOVERY; PROTEOMIC ANALYSIS; AUTHENTICATION; BEEF; FOOD; RAW; PRODUCTS; PROTEINS;
D O I
10.1016/j.foodchem.2015.11.121
中图分类号
O69 [应用化学];
学科分类号
081704 ;
摘要
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. (c) 2015 Elsevier Ltd. All rights reserved.
引用
收藏
页码:157 / 164
页数:8
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