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

Radoslav Grujić ^a

Danica Savanović ^b

Affiliation

a University of East Sarajevo, Lukavica, Bosnia and Herzegovina

b University of Banja Luka, Banja Luka, Bosnia and Herzegovina

Copyright ©Grujić et al. This is an open access article distributed under the terms of the Creative Commons Attribution 4.0. (http://creativecommons.org/licenses/by/4.0/), allowing third parties to copy and redistribute the material in any medium or format and to remix, transform, and build upon the material for any purpose, even commercially, provided the original work is properly cited and states its license.

DOI: http://doi.org/10.21603/2308-4057-2018-2-421-428

Abstract

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

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