Bioinformatics Tools Assist in The Screening of Potential Porcine-Specific Peptide Biomarkers of Gelatin and Collagen For Halal Authentication
Keywords:
Gelatin, Collagen, Porcine, Peptide, BioinformaticsAbstract
Gelatin and collagen are two animal-derived ingredients that are widely used in various industries. Both have distinctive physico-chemical characteristic that made them ingredients of interest for many industrial players to be applied as there are vast arrays of usage in the food, cosmetic and biomedical fields. However, the origin of gelatin and collagen poses ethical and religious concerns, especially for Muslims and Jews who have restrictions on food consumption. Porcine by-products are of concern for religious and health reasons, and there is a demand for precise and reliable detection techniques. The limitation of DNA detection is due to extreme environment in food processing which results in low extractability of DNA. Therefore, peptide-based detection using mass spectrometry is required. However, identify the suitable marker is like searching needle in haystacks. Hence, combination of bioinformatics and mass spectrometry is proposed. This study aims to identify the specific peptide biomarkers by employing bioinformatics technique which can be applied to identify gelatin and collagen sources with the aid of mass spectrometry. In these approach, combination of Petunia Trans-Proteomic Pipeline (TPP, version 5.2.0) and sequence alignment ClustalW were applied to facilitate the MS data (LC-QTOF-MS) and peptide identification. As a result, 69 fasta file of protein sequence from both UniProtKB and NCBInr have been collected, 81 collagen peptides sequence and 118 gelatine peptides has been attainable that have the potential to distinguish different species. In conclusion, in silico protein sequence approaches helps to enable rapid screening of proteotypic peptides that can serve as species biomarkers proficiently.
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Amir, S.H., Yuswan, M.H., Aizat, W.M., Mansor, M.K., Desa, M.N.M., Yusof, Y.A., Song, L.K. & Mustafa, S. 2021. Comparative database search engine analysis on massive tandem mass spectra of pork-based food products for halal proteomics. Journal of Proteomics, 241: 2-7. DOI: https://doi.org/10.1016/j.jprot.2021.104240
Ballin, N.Z., Vogensen, F.K. & Karlsson, A.H. 2009. Species determination - Can we detect and quantify meat adulteration? Meat Science, 83(2): 165-174. DOI: https://doi.org/10.1016/j.meatsci.2009.06.003
Buckley, M. 2016. Species identification of bovine, ovine and porcine type 1 collagen; Comparing peptide mass fingerprinting and LC-based proteomics methods. International Journal of Molecular Sciences, 17(4): 445. DOI: https://doi.org/10.3390/ijms17040445
Calvano, C.D., Monopoli, A., Loizzo, P., Faccia, M. & Zambonin, C. 2013. Proteomic approach based on MALDI-TOF MS to detect powdered milk in fresh cow's milk. Journal of Agricultural and Food Chemistry, 61(8): 1609-1617. DOI: https://doi.org/10.1021/jf302999s
Cebi, N., Dogan, C.E., Mese, A.E., Ozdemir, D., Arici, M. & Sagdic, O. 2019. A rapid ATR-FTIR spectroscopic method for classification of gelatin gummy candies in relation to the gelatin source. Food Chemistry, 277: 373-381. DOI: https://doi.org/10.1016/j.foodchem.2018.10.125
Cifuentes, A. 2017. Foodomics, foodome and modern food analysis. TrAC Trends in Analytical Chemistry, 96: 1. DOI: https://doi.org/10.1016/j.trac.2017.09.001
Deutsch, E.W., Mendoza, L., Shteynberg, D., Farrah, T., Lam, H., Tasman, N., Sun, Z., Nilsson, E., Pratt, B., Prazen, B., Eng, J.K., Martin, D.B., Nesvizhskii, A.I. & Aebersold, R. 2010. A guided tour of the Trans-Proteomic Pipeline. Proteomics, 10(6): 1150-1159. DOI: https://doi.org/10.1002/pmic.200900375
Gallardo, J.M., Ortea, I. & Carrera, M. 2013. Proteomics and its applications for food authentication and food-technology research. TrAC Trends in Analytical Chemistry, 52: 135-141. DOI: https://doi.org/10.1016/j.trac.2013.05.019
Grundy, H.H., Reece, P., Buckley, M., Solazzo, C.M., Dowle, A.A., Ashford, D., Charlton, A.J., Wadsley, M.K. & Collins, M. J. 2016. A mass spectrometry method for the determination of the species of origin of gelatine in foods and pharmaceutical products. Food Chemistry, 190: 276-284. DOI: https://doi.org/10.1016/j.foodchem.2015.05.054
Hashim, D.M., Man, Y.B.C., Norakasha, R., Shuhaimi, M., Salmah, Y. & Syahariza, Z. A. 2010. Potential use of Fourier transform infrared spectroscopy for differentiation of bovine and porcine gelatins. Food Chemistry, 118(3): 856-860. DOI: https://doi.org/10.1016/j.foodchem.2009.05.049
Husin, M.M. 2022. Gula-gula bergelatin babi tular semula. Sinar Harian [WWW Document]. Sinar Harian. URL https://www.sinarharian.com.my/article/215261/berita/semasa/gula-gula-bergelatin-babi-tular-semula (accessed 12.19.2023).
Jagadeesh, D.S., Kannegundla, U. & Reddy, R.K. 2017. Application of proteomic tools in food quality and safety. Advances in Animal and Veterinary Sciences, 5(5): 213-225.
Jannat, B., Ghorbani, K., Kouchaki, S., Sadeghi, N., Eslamifarsani, E., Rabbani, F. & Beyramysoltan, S. 2020. Distinguishing tissue origin of bovine gelatin in processed products using LC/MS technique in combination with chemometrics tools. Food Chemistry, 319: 2-6. DOI: https://doi.org/10.1016/j.foodchem.2020.126302
Jaswir, I., Mirghani, M.E.S., Salleh, H.M., Ramli, N., Octavianti, F. & Hendri, R. 2016. An overview of the current analytical methods for halal testing. In: Contemporary Issues and Development in the Global Halal Industry. Springer, Singapore. pp. 291-300. DOI: https://doi.org/10.1007/978-981-10-1452-9_27
Kariduraganavar, M.Y., Kittur, A.A. & Kamble, R.R. 2014. Polymer synthesis and processing. In: Natural and Synthetic Biomedical Polymers. G. Sangamesh, Kumbar, T. Cato, Laurencin and M. Deng (Eds.). Elsevier, Oxford. pp. 1-31. DOI: https://doi.org/10.1016/B978-0-12-396983-5.00001-6
Korte R. & Brockmeyer, J. 2017. Novel mass spectrometry approaches in food proteomics. TrAC Trends in Analytical, 96: 99-106. DOI: https://doi.org/10.1016/j.trac.2017.07.010
Manning, L. & Soon, J.M. 2016. Food safety, food fraud, and food defense: A fast evolving literature. Journal of Food Science, 81(4): 823-834. DOI: https://doi.org/10.1111/1750-3841.13256
Nugraha, R., Rahayu, F. & Nurilmala, M. 2022. Identification of peptide biomarkers for halal gelatin using bioinformatics techniques. IOP Conference Series: Earth and Environmental Science, 10333: 2-7. DOI: https://doi.org/10.1088/1755-1315/1033/1/012063
Orduna, R., Husby, E., Yang, C.T., Ghosh, D. & Beaudry, F. 2015. Assessment of meat authenticity using bioinformatics, targeted peptide biomarkers and high-resolution mass spectrometry. Food Additives & Contaminants: Part A, 32(10): 1709-1717. DOI: https://doi.org/10.1080/19440049.2015.1064173
Ortea, I., O'Connor, G. & Maquet, A. 2016. Review on proteomics for food authentication. Journal of Proteomics, 147: 212-225. DOI: https://doi.org/10.1016/j.jprot.2016.06.033
Sha, X.M., Hu, Z.Z., Ye, Y.H., Xu, H. & Tu, Z.C. 2019. Effect of extraction temperature on the gelling properties and identification of porcine gelatin. Food Hydrocolloids, 92: 163-172. DOI: https://doi.org/10.1016/j.foodhyd.2019.01.059
Sha, X.M., Zhang, L.J., Tu, Z.C., Zhang, L.Z., Hu, Z.Z., Li, Z., Li, X., Huang, T., Wang, H., Zhang, L. & Xiao, H. 2018. The identification of three mammalian gelatins by liquid chromatography-high resolution mass spectrometry. Lwt Food science and Technology, 89: 74-86. DOI: https://doi.org/10.1016/j.lwt.2017.10.001
Silva, T.H., Moreira-Silva, J., Marques, A.L., Domingues, A., Bayon, Y. & Reis, R.L. 2014. Marine origin collagens and its potential applications. Marine Drugs, 12(12): 5881-5901. DOI: https://doi.org/10.3390/md12125881
Silvipriya, K., Kumar, K., Bhat, A., Kumar, B., John, A. & Lakshmanan, P. 2015. Collagen: Animal Sources and Biomedical Application. Journal of Applied Pharmaceutical Science, 5(3): 123-127. DOI: https://doi.org/10.7324/JAPS.2015.50322
Stadler, R.H., Tran, L.A., Cavin, C., Zbinden, P. & Konings, E.J. 2016. Analytical Approaches to Verify Food Integrity: Needs and Challenges. Journal of AOAC International, 99(5): 1135-1144. DOI: https://doi.org/10.5740/jaoacint.16-0231
Tighe, P.J., Ryder, R.R., Todd, I. & Fairclough, L.C. 2015. ELISA in the multiplex era: Potentials and pitfalls. Proteomics Clinical Application, 9(3-4): 406-422. DOI: https://doi.org/10.1002/prca.201400130
Yang, C.T., Ghosh, D. & Beaudry, F. 2018. Detection of gelatin adulteration using bio-informatics, proteomics and high-resolution mass spectrometry. Food Additives and Contaminants: Part A, 35(4): 599-608. DOI: https://doi.org/10.1080/19440049.2017.1416680
Yilmaz, M.T., Kesmen, Z., Baykal, B., Sagdic, O., Kulen, O., Kacar, O., Yetim, H. & Baykal, A.T. 2013. A novel method to differentiate bovine and porcine gelatins in food products: nanoUPLC-ESI-Q-TOF-MS(E) based data independent acquisition technique to detect marker peptides in gelatin. Food Chemistry, 141(3): 2450-2458. DOI: https://doi.org/10.1016/j.foodchem.2013.05.096
Yuswan, M.H., Jalil, N.H.A., Mohamad, H., Keso, S., Mohamad, N.A., Yusoff, T.S.T.M., Ismail, N.F., Manaf, Y.N.A., Hashim, A.M., Desa, M.N.M., Yusof, Y.A. & Mustafa, S. 2021. Hydroxyproline determination for initial detection of halal-critical food ingredients (gelatin and collagen). Food Chemistry, 337: 127762. DOI: https://doi.org/10.1016/j.foodchem.2020.127762
Zhang, Q., Tu, Z., Wang, H., Huang, X., Shi, Y., Sha, X. & Xiao, H. 2014. Improved glycation after ultrasonic pretreatment revealed by high-performance liquid chromatography-linear ion trap/Orbitrap high-resolution mass spectrometry. Journal of Agricultural and Food Chemistry, 62(12): 2522-2530. DOI: https://doi.org/10.1021/jf5002765
Zhang, T., Shi, X. & Netto, J. 2019. Determination of Animal Species Origin from Gelatin in Food and Pharmaceutical Products by LC-MS/MS [WWW Document]. Sciex. URL https://sciex.com/content/dam/SCIEX/pdf/posters/Food-Fraud-Authenticity.pdf (accessed 12.19.2023)
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