Nuclear chemistry

Chromatography

Biochemistry

Food science

Myofibril

Extraction (chemistry)

Tropomyosin

Myosin

Chemistry

Denaturation (fissile materials)

Journal of Bioresources and Bioproducts

In the present study, myofibrillar proteins were extracted from the meat proteins of beef, lamb, chicken, tuna and emperor fish using non-denaturation method, and their physico-chemical and rheological properties were assessed. The myofibrillar proteins of beef, emperor and lamb samples had higher percentage of protein extractability than tuna and chicken samples. The tuna sample showed significantly higher bound bromophenol blue (BPB) value while lamb samples showed lower value ( P < 0.05). The myofibrillar protein of chicken sample was found to have more ionic and hydrogen bonds than all other myofibrillar samples. The disulphide bonds in tuna and lamb myofibrillar protein samples were significantly higher than other three samples ( P < 0.05). The myofibrillar protein samples showed major bands myosin heavy chain, α -actinin, desimin, actin, troponin, tropomyosin and myosin light chain with wider molecular weight distribution in the range of 20–200 ku. The myofibrillar proteins exhibited Newtonian and shear thickening nature behaviour at lower protein concentration (1 mg/mL) as revealed by flow profile and visco-elastic analysis using rheometer.

Extraction and Characterization of Myofibrillar Proteins from Different Meat Sources: A Comparative Study