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Title of article Analysis of myofibrillar and sarcoplasmic proteins in pork meat by capillary gel electrophoresis
Authors

Grujić R., University of East Sarajevo , University of East Sarajevo

Savanović D., University of Banja Luka , University of Banja Luka

Section: STANDARDIZATION, CERTIFICATION, QUALITY AND SAFETY
Year 2018 Issue 2 DOI 10.21603/2308-4057-2018-2-421-428
Annotation Myofibrillar and sarcoplasmic proteins were extracted from pork meat (M. Longissimus dorsi) and then separated by capillary gel electrophoresis (CGE). Migration time and peak areas of individual protein molecules in the electropherogram were analysed. The electropherograms obtained after the separation of myofibrillar proteins contained 53 well-separated peaks, of which the following were identified: thymosin, myosin light chain-3 (MLC-3), myosin light chain-2 (MLC-2), troponin C, troponin I, myosin light chain-1 (MLC-1), tropomyosin 1, tropomyosin 2, troponin T, actin, desmin, troponin, C protein, and myosin heavy chain (MHC). The relative concentration of the identified myofibrillar proteins was 74.5%. Of the 56 separated sarcoplasmic proteins the following were identified: myoglobin, myokinase, triosephosphate isomerase, phosphoglycerate mutase, lactate dehydrogenase, glyceraldehyde phosphate dehydrogenase, aldolase, creatine kinase, enolase, phosphoglucose isomerase, pyruvate kinase, phosphoglucomutase, and phosphorylase b. The relative concentration of the identified sarcoplasmic proteins was 83.6% of all sarcoplasmic proteins extracted from the pork meat.
Keywords Myofibrillar proteins, sarcoplasmic proteins, capillary gel electrophoresis
Artice information Received June 18, 2017
Accepted October 25, 2018
Available online December 20, 2018
Imprint article Grujić R. and Savanović D. Analysis of myofibrillar and sarcoplasmic proteins in pork meat by capillary gel electrophoresis. Foods and Raw Materials, 2018, vol. 6, no. 2, pp. 421–428.
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Bibliography
  • Vallejo-Cordoba B., Rodríguez-Ramírez R., and González-Córdova A.F. Capillary electrophoresis for bovine and ostrich meat characterization. Food Chemistry, 2010, vol. 120, no. 1, pp. 304–307. DOI: https://doi.org/10.1016/j.foodchem.2009.09.080.
  • Matarneh S.K., England E.M., Scheffler T.L., and Gerrard D.E. The Conversion of Muscle to Meat. In Toldra F. (ed) Lawrie’s Meat Science. Cambridge, UK: Woodhead Publ., 2017. pp. 159–185.
  • Ssrensen H., Ssrensen S., Bjergegaard C., and Michaelsen S. Chromatography and capillary electrophoresis in food analysis. London, UK: The Royal Society of Chemistry, 1999. pp.198–276.
  • Porzio M.A. and Pearson A.M. Improved resolution of myofibrillar proteins with sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Biochimica et Biophysica Acta (BBA) – Protein Structure, 1977, vol. 490, no. 1, pp. 27–34. DOI: https://doi.org/10.1016/0005-2795(77)90102-7.
  • Grujić R., Petrović L., Pikula B., and Amidžić Lj. Definition of the optimum freezing rate—1. Investigation of structure and ultrastructure of beef M. longissimus dorsi frozen at different freezing rates. Meat Science, 1993, vol. 33, no. 3, pp. 301–318. DOI: https://doi.org/10.1016/0309 1740(93)90003-Z.
  • Claeys E., Uytterhaegen L., Buts B., and Demmeyer D. Quantification of beef myofibrillar proteins by SDS–PAGE. Meat Science, 1995, vol. 39, no. 2, pp. 177–193. DOI: https://doi.org/10.1016/0309-1740(94)P1819-H.
  • Ahmed N.S., Abd El-Gawad M.A.M, El-Abd M.M., and Abd-Rabou N.S. Properties of buffalo Mozzarella cheese as affected by type of coagulante. Acta Scientiarum Polonorum Technologia Alimentaria, 2011, vol. 10, no. 3, pp. 339–357.
  • Gallego M., Mora L., Aristoy M.C., and Toldrá F. Optimisation of a simple and reliable label-free methodology for the relative quantitation of raw pork meat proteins. Food Chemistry, 2015, vol. 182, pp. 74–80. DOI: 10.1016/j.foodchem.2015.02.114
  • Kim G-D., Seo J.-K., Yum H.-W., Jeong J-Y., Yang H-S. Protein markers for discrimination of meat species in raw beef, pork and poultry and their mixtures. Food Chemistry, 2017, vol. 217, pp. 163–170. DOI: https://doi.org/10.1016/j.foodchem.2016.08.100.
  • Dziuba J., Szerszunowicz I., Nałęcz D., and Dziuba M. Proteomic analysis of albumin and globulin fractions of pea (Pisum sativum L.) seeds. Acta Scientiarum Polonorum Technologia Alimentaria, 2014, vol. 13, no. 2, pp. 181–190. DOI: https://doi.org/10.17306/J.AFS.2014.2.7.
  • Cota-Rivas M. and Vallejo-Cordoba B. Capillary electrophoresis for meat species differentiation. Journal of Capillary Electrophoresis, 1997, vol. 4, no. 4, pp. 195–199.
  • Hajba L. and Guttman A. Recent advances in column coatings for capillary electrophoresis of proteins. Trends in Analytical Chemistry, 2017, vol. 90, pp. 38–44. DOI: https://doi.org/10.1016/j.trac.2017.02.013.
  • Sirén H. Capillary Electrophoresis in Food Analysis. In: Nollet L.M.L and Toldra F.. Handbook of Food Analysis – Two Volume Set, 3rd Edition. Boca Raton, Florida: CRC Press, 2015. pp. 493–519.
  • Weinberger R. Practical Capillary Electrophoresis. Chappaqua, New York: Academic Press, 2000. pp. 1–24.
  • Zhu Z., Lu J.J., and Liu S. Protein Separation by Capillary Gel Electrophoresis: A Review. Analytica Chimica Acta, 2012, vol. 709, pp. 21–31. DOI: https://doi.org/10.1016/j.aca.2011.10.022.
  • Stepanova S. and Kasicka V. Recent applications of capillary electromigration methods to separation and analysis of proteins. Analytica Chimica Acta, 2016, vol. 933, pp. 23–42. DOI: https://doi.org/10.1016/j.aca.2016.06.006.
  • Bonczar G., Walczycka M., and Duda I. The changes of proteins fractions shares in milk and fermented milk drinks. Acta Scientiarum Polonorum Technologia Alimentaria, 2016, vol. 15, no. 4, pp. 379–389. DOI: https://doi.org/10.17306/J.AFS.2016.4.36.
  • Wenz C. Performance of commercially available gels for protein characterization by capillary gel electrophoresis with UV detection on the Agilent 7100 CE System. Application Note. Agilent Technologies, 2011.
  • Toldra F., Rico E., and Flores J. Cathepsin B, D, H and L activities in the processing of dry-cured ham. Journal of the Science of Food and Agriculture, 1993, vol. 62, no. 2, pp. 157–161. DOI: https://doi.org/10.1002/jsfa.2740620208.
  • Sotelo G.C., Pineiro C., Perez-Martin I.R., and Gallardo M.J. Analysis of fish and squid myofibrillar proteins by capillary sodium dodecyl sulfate gel electrophoresis: actin and myosin quantification. European Food Research and Technology, 2000, vol. 211, no. 6, pp. 443–448. DOI:https://doi.org/10.1007/s002170000176.
  • Ngapo T.M. and Alexander M. Capillary gel electrophoresis versus SDS PAGE of exudate from fresh pork. Meat Science, 1999, vol. 53, no. 3, pp. 145–148. DOI: https://doi.org/10.1016/S0309-1740(99)00049-2.
  • Purslow P.P. The Structure and Growth of Muscle. In Toldra F. (ed) Lawrie’s Meat Science. Cambridge, UK: Woodhead Publ, 2017. pp 49–97.
  • Marino R., Albenzio M., della Malva A., et al. Changes in meat quality traits and sarcoplasmic proteins during aging in three different cattle breeds. Meat Science, 2014, vol. 98, no. 2, pp. 178–186. DOI: https://doi.org/10.1016/j.meatsci.2014.05.024.
  • Wu G., Farouk M.M., Clerens S., and Rosenvold K. Effect of beef ultimate pH and large structural protein changes with aging on meat tenderness. Meat Science, 2014, vol. 98, no. 4, pp. 637–645. DOI: https://doi.org/10.1016/j.meatsci.2014.06.010.
  • Jia G., Liu H., Nirasawa S., and Liu H. Effects of high-voltage electrostatic field treatment on the thawing rate and post-thawing quality of frozen rabbit meat. Innovative Food Science and Emerging Technologies, 2017, vol. 41, pp. 348–356. DOI: https://doi.org/10.1016/j.ifset.2017.04.011.

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