Malays. Appl. Biol. (2019) 48(2): 131–139
COMPARING THE EFFECT OF HEAT ON TROPOMYOSIN
ISOFORMS PATTERNS FROM WATER BUFFALO AND WILD
BOAR MEAT BY TWO-DIMENSIONAL GEL ELECTROPHORESIS
NADIAH MAT JUNOH1, MOHD HAFIS YUSWAN1, SHUHAIMI MUSTAFA1, AMALIA MOHD HASHIM1,2,
ROZI MOHAMED4, SHIOU YIH LEE4, NAZIA ABDUL MAJID5, SITI AIMI SARAH6
and DHILIA UDIE LAMASUDIN1,3*
1Laboratory of Halal Science Research, Halal Products Research Institute, Universiti Putra Malaysia,
43400 UPM Serdang, Selangor, Malaysia
2Department of Microbiology, Faculty of Biotechnology and Biomolecular Sciences,
Universiti Putra Malaysia, 43400 Serdang, Selangor, Malaysia
3Department of Cell & Molecular Biology, Faculty of Biotechnology and Biomolecular Sciences,
Universiti Putra Malaysia, 43400 UPM Serdang, Selangor, Malaysia
4Department of Forest Management, Faculty of Forestry, Universiti Putra Malaysia,
43400 UPM Serdang, Selangor, Malaysia
5Institute of Biological Science, University of Malaya, 50603 Kuala Lumpur,
Wilayah Persekutuan Kuala Lumpur, Malaysia
6Food Science and Technology Program, Faculty of Applied Sciences, Universiti Teknologi MARA,
40450 Shah Alam, Selangor, Malaysia
*E-mail: This e-mail address is being protected from spambots. You need JavaScript enabled to view it
Accepted 7 May 2019, Published online 31 May 2019
ABSTRACT
Tropomyosin is one of the most abundant proteins in meat; however, very little is known about it due to the lack of scientific literature. In this study, the spot volume of tropomyosin (TPM) isoforms, TPM2 and TPM1, in meat from water buffalo and wild boar subjected to various cook treatments were compared. We hypothesized that primary structures of the tropomyosin isoforms from both species would remain stable despite the application of heat. Proteins extracted from the treated meats were analyzed using two-dimensional gel electrophoresis and mass spectrometry. A Kruskal-Wallis test showed that there were no significant differences in protein spot volumes for all treatments; however, a significant difference was observed between species. Changes in the amino acid sequence of TPM1 were observed between the two species, indicating that the isoforms could be used as thermostable proteins or peptide markers for species identification because of their resistance to high temperatures.
Key words: Meat, tropomyosin isoforms, spot volume, proteomic approaches
