Possibilities of microscopic detection of isolated porcine proteins in model meat products
Keywords:collagen, isolated protein, light microscopy
In recent years, various protein additives intended for manufacture of meat products have increasing importance in the food industry. These ingredients include both, plant-origin as well as animal-origin proteins. Among animal proteins, blood plasma, milk protein or collagen are used most commonly. Collagen is obtained from pork, beef, and poultry or fish skin. Collagen does not contain all the essential amino acids, thus it is not a full protein in terms of essential amino acids supply for one's organism. However, it is rather rich in amino acids of glycine, hydroxyproline and proline which are almost absent in other proteins and their synthesis is very energy intensive. Collagen, which is added to the soft and small meat products in the form of isolated porcine protein, significantly affects the organoleptic properties of these products. This work focused on detection of isolated porcine protein in model meat products where detection of isolated porcine protein was verified by histological staining and light microscopy. Seven model meat products from poultry meat and 7 model meat products from beef and pork in the ratio of 1:1, which contained 2.5% concentration of various commercially produced isolated porcine proteins, were examined. These model meat products were histologically processed by means of cryosections and stained with hematoxylin-eosin staining, toluidine blue staining and Calleja. For the validation phase, Calleja was utilized. To determine the sensitivity and specificity, five model meat products containing the addition of isolated porcine protein and five model meat products free of it were used. The sensitivity was determined for isolated porcine protein at 1.00 and specificity was determined at 1.00. The detection limit of the method was at the level of 0.001% addition. Repeatability of the method was carried out using products with addition as well as without addition of isolated porcine protein and detection was repeated 10 times. Repeatability in both, positive and negative samples, for isolated porcine protein was determined at 100%. The results show that the histological processing of cryosections stained using Calleja is suitable for detecting isolated porcine protein in meat products.
Bailey, A. J., Light, N. D. 1989. Connective tissue in meat and meat products. London: Elsevier Science Publishers Ltd, 355 p. ISBN-1 85166 284 7. https://doi.org/10.1016/S0309-1740(03)00082-2
Budig, J. Mathauser, P. 2007. Technicko-technologické aspekty výroby díla mělněných masných výrobků v minulosti a v současnosti. Maso, vol. 4, p. 21.
Doerscher, D. R., Briggs, J. L., Lonergan, S. M. 2004. Effects of pork collagen on thermal and viscoelastic properties of purified porcine myofibrillar protein gels. Meat Science, vol. 66, no. 1, p. 181-188.
European Commision. Commission Decision 2002/657/EC of 12 August 2002 implementing Council Directive 96/23/EC concerning the performance of analytical methods and the interpretation of results. Official Journal of European Commission. L, 2002 vol. 221, p. 8-36.
Gillett, T. A. 1987. Gelatin gels. In: A. M. Pearson, et al. Collagen as a food. Van Nostrand Reinhold Company, New York, N.Y., p. 223-249.
Khiari, Z. 2014. Poultry protein isolate prepared using an acid solubilization/precipitation extraction influences the microstructure, the functionality and the consumer acceptability of a processed meat product. Food Structure, vol. 2, no. 1, p. 49-60. https://doi.org/10.1016/j.foostr.2014.08.002
Khoshnoodi, J., Cartailler, J. P., Alvares, K., Veis, A., Hudson, G. B. 2006. Molecular Recognition in the Assembly of Collagens: Terminal Noncollagenous Domains Are Key Recognition Modules in the Formation of Triple Helical Protomers. Journal of Biological Chemistry, vol. 281, no. 50, p. 38117-38121. https://doi.org/10.1074/jbc.R600025200
Lát, J., Beneš, J., Blanka, R., Gola, J., Hlavinka, J., Klíma, D., Mareček, S., Petříček, M., Pokorný, V., Rusz, J. 1976. Technologie masa (Meat technology). Praha: SNTL, 635 s. ISBN- 978-80-8069-861-4. PMid:941647
European Food Safety Authority. 2004. Opinion of the Scientific Panel on Dietetic Products, Nutrition and Allergies on a request from the Commission relating to the evaluation of allergenic foods for labelling purposes. The EFSA Journal, vol. 32, p. 1-197.
Massart, D. L., Vandeginste, B. G. M., Buydens, L. M. C., De Jong, G. J., Lewi, P. J., Smeyers-Verbeke, J. 1997. Handbook of Chemometrics and Qualimetrics (Data Handling in Science and Technology), vol. 20, Elsevier, Amsterdam. ISBN- 978-0-444-82853-8.
O'rangers, J. J., Condon, R. J. 2000. Current Issues in Regulatory Chemistry, AOAC Int., Gaithersburg, Maryland, USA, p. 207.
Petracci, M., Bianchi, M., Mudalal, S., Cavani, C. 2013. Functional ingredients for poultry meat products. Trends in Food Science & Technology, vol. 33, no. 1, p. 27-39. https://doi.org/10.1016/j.tifs.2013.06.004
Prabhu, G. A., Doerscher, D. R., Hull, D. H. 2004. Utilization of pork collagen protein in emulsified and whole muscle meat products. Journal of Food Science, vol. 69, p. C388-389. https://doi.org/10.1111/j.1365-2621.2004.tb10703.x
Straka, I., Malota, L. 2006. Chemické vyšetření masa: klasické laboratorní metody (Chemical determination of meat: classic laboratory methods). Tábor, Czech Republic : OSSIS, 94 s. ISBN-80-86659-09-7.
Suchánek, M. 1999. Qualimetry 9. The appropriateness of the analytical methods for a particular purpose. p. 61. ISBN- 80-901868-7-4.
Tarté, R. 2010. Ingredients in meat products: properties, functionality and applications. Springer Science & Business Media, 129 p. ISBN-978-1-4419-2436-0. PMCid:PMC3317889
Trullols, E., Ruisanchez, I., Rius, F. X. 2004. Validation of qualitative analytical methods. TrAC Trends in Analytical Chemistry, vol. 23, no. 2, p. 137-145. https://doi.org/10.1016/S0165-9936(04)00201-8
Vognarová, I., Vrchlabský, J. 1984. Technologie masa (Meat technology). 2 nd ed. Praha, Czech Republic : SNTL - Nakladatelství technické literatury. ISBN- 04-846-46.
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