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Pavan Kumar Dara, Anjana Geetha, Upasana Mohanty, Mahadevan Raghavankutty, Suseela Mathew, Ravishankar Chandragiri Nagarajarao, Anandan Rangasamy. Extraction and characterization of myofibrillar proteins from different meat sources: A comparative study[J]. Journal of Bioresources and Bioproducts. doi: 10.1016/j.jobab.2021.04.004
Citation: Pavan Kumar Dara, Anjana Geetha, Upasana Mohanty, Mahadevan Raghavankutty, Suseela Mathew, Ravishankar Chandragiri Nagarajarao, Anandan Rangasamy. Extraction and characterization of myofibrillar proteins from different meat sources: A comparative study[J]. Journal of Bioresources and Bioproducts. doi: 10.1016/j.jobab.2021.04.004

Extraction and characterization of myofibrillar proteins from different meat sources: A comparative study

doi: 10.1016/j.jobab.2021.04.004
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  • Corresponding author: Corresponding author Biochemistry and Nutrition Division, ICAR-Central Institute of Fisheries Technology, Cochin 682029, Kerala, India
    Email address: suseela1962@gmail.com (Suseela Mathew).
  • Received Date: 2020-06-24
  • Accepted Date: 2020-08-29
  • Rev Recd Date: 2020-08-19
  • 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.


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