Suratno Suratno , Anjar Windarsih , Ayu Septi Anggraeni , Lucky Prabowo Miftachul Alam , Hendy Dwi Warmiko , Siti Nurul Aisyiyah Jenie , Hilda Novianty , Yaya Ihya Ulumuddin , Ade Marmita , Ni Putu Sri Ayuni , Anastasia Wheni Indrianingsih , Abdul Rohman
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引用次数: 0
Abstract
The authenticity of halal meat is a global issue because pork adulteration occurs. Certain religions, such as Islam and Judaism, prohibit the use of pork in food products. The purpose of this study was to evaluate the volume of trypsin with 10, 50 and 100 μL (20 μg/100 μL) and the digestion time from overnight to 30–120 min to establish a fast and straightforward procedure on proteomic analysis for halal authentication of meat and meat products. The method was applied to raw meat and processed pork products. The results show that 30 min digestion time and 50 μL of trypsin could detect specific peptides from pork. The proteins such as L-lactate dehydrogenase (D2SW96), haemoglobin subunit beta (F1RII7), carbonic anhydrase (A0A4XIUCS1), and myosin-1 (A0A481AX92) could be the alternative protein that contains specific peptide from pork that could be used as peptide biomarker in raw pork meat. Two peptides from haemoglobin subunit beta (F1RII7) protein heat stable peptide biomarkers were not previously reported. The method is proven for fast analysis, simple protein extraction, and rapid identification of specific pork peptides in raw meat and processed pork products.
Significance
The authenticity of halal meat is a global issue because pork adulteration occurs. Certain religions, such as Islam and Judaism, prohibit the use of pork in food products. Pork is frequently used as an adulterant in high-quality, high-priced meats such as beef, fish meat slices, lamb, or other meat to increase profits because pork is less expensive than the other meats. The purpose of this study was to evaluate the volume of trypsin and the digestion time to establish a fast and straightforward procedure on proteomic analysis for halal authentication of meat and meat products. The results show that 30 min digestion time and 50 μL of trypsin could detect specific peptides from pork. The proteins such as L-lactate dehydrogenase (D2SW96), haemoglobin subunit beta (F1RII7), carbonic anhydrase (A0A4XIUCS1), and myosin-1 (A0A481AX92) could be the alternative protein that contains specific peptide from pork that could be used as peptide biomarker in raw pork meat. To the best of our knowledge, this is the first report that studied on fast analysis, simple protein extraction, and rapid identification of specific pork peptides in raw meat and processed pork products.
期刊介绍:
Journal of Proteomics is aimed at protein scientists and analytical chemists in the field of proteomics, biomarker discovery, protein analytics, plant proteomics, microbial and animal proteomics, human studies, tissue imaging by mass spectrometry, non-conventional and non-model organism proteomics, and protein bioinformatics. The journal welcomes papers in new and upcoming areas such as metabolomics, genomics, systems biology, toxicogenomics, pharmacoproteomics.
Journal of Proteomics unifies both fundamental scientists and clinicians, and includes translational research. Suggestions for reviews, webinars and thematic issues are welcome.