Journal Highlight: In-gel and OFFGEL-based proteomic approach for authentication of meat species from minced meat and meat products

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  • Published: Sep 4, 2017
  • Author: separationsNOW
  • Channels: Proteomics & Genomics
thumbnail image: Journal Highlight: In-gel and OFFGEL-based proteomic approach for authentication of meat species from minced meat and meat products

In-gel 2D gel electrophoresis and an OFFGEL-based proteomic method followed by the MALDI-TOF MS analysis of proteins have been used to authenticate raw and cooked water buffalo, sheep and goat meat and their mixes.

In-gel and OFFGEL-based proteomic approach for authentication of meat species from minced meat and meat products

Journal of the Science of Food and Agriculture, 2017, online
Basappa M Naveena, Deepak S Jagadeesh, Veeranna Kamuni, Muthukumar M, Vinayak V Kulkarni, Kiran M and Srikanth Rapole

Abstract: Fraudulent mislabelling of processed meat products on global scale which could not be detected using conventional techniques demand for sensitive, robust and accurate methods of meat authentication to ensure food safety and public health. In the present study, we developed in-gel (2-dimensional gel electrophoresis, 2DE) and OFFGEL-based proteomic method for authenticating raw and cooked water buffalo (Bubalus bubalis), sheep (Ovis aries) and goat (Caprus hircus) meat and their mixes. The MALDI-TOF MS analysis of proteins separated using 2DE or OFFGEL electrophoresis delineated species-specific peptide biomarkers derived from myosin light chain 1 and 2 (MLC1 and MLC2) of buffalo: sheep: goat meat mix in definite proportions @ 98:1:1, 99:0.5:0.5, 99.8:0.1:0.1 that were found stable to resist thermal processing. In-gel and OFFGEL-based proteomic approach are efficient in authenticating meat mixes spiked at minimum 1.0% and 0.1% level, respectively in triple meat mix for both raw and cooked samples. The study demonstrated that authentication of meat from a complex mix of three closely related species requires identification of more than one species-specific peptides due to close similarity between their amino acid sequences.

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