Extraction and Characterization of Myofibrillar Proteins from Different Meat Sources: A Comparative Study
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 p...
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KeAi Communications Co., Ltd.
2021-11-01
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author | Pavan Kumar Dara Anjana Geetha Upasana Mohanty Mahadevan Raghavankutty Suseela Mathew Ravishankar Chandragiri Nagarajarao Anandan Rangasamy |
author_facet | Pavan Kumar Dara Anjana Geetha Upasana Mohanty Mahadevan Raghavankutty Suseela Mathew Ravishankar Chandragiri Nagarajarao Anandan Rangasamy |
author_sort | Pavan Kumar Dara |
collection | DOAJ |
description | 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. |
first_indexed | 2024-04-09T21:57:51Z |
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institution | Directory Open Access Journal |
issn | 2369-9698 |
language | English |
last_indexed | 2024-04-09T21:57:51Z |
publishDate | 2021-11-01 |
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record_format | Article |
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spelling | doaj.art-ca25436592284417b5a1188c91487a302023-03-24T04:22:38ZengKeAi Communications Co., Ltd.Journal of Bioresources and Bioproducts2369-96982021-11-0164367378Extraction and Characterization of Myofibrillar Proteins from Different Meat Sources: A Comparative StudyPavan Kumar Dara0Anjana Geetha1Upasana Mohanty2Mahadevan Raghavankutty3Suseela Mathew4Ravishankar Chandragiri Nagarajarao5Anandan Rangasamy6Biochemistry and Nutrition Division, ICAR-Central Institute of Fisheries Technology, Cochin 682029, Kerala, IndiaDepartment of Food and Nutrition, Mody University, Lakshmangarh 332311, Rajasthan, IndiaCollege of fisheries, Central Agricultural University, Tripura 799210, IndiaBiochemistry and Nutrition Division, ICAR-Central Institute of Fisheries Technology, Cochin 682029, Kerala, IndiaBiochemistry and Nutrition Division, ICAR-Central Institute of Fisheries Technology, Cochin 682029, Kerala, India; Corresponding author.Biochemistry and Nutrition Division, ICAR-Central Institute of Fisheries Technology, Cochin 682029, Kerala, IndiaBiochemistry and Nutrition Division, ICAR-Central Institute of Fisheries Technology, Cochin 682029, Kerala, IndiaIn 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.http://www.sciencedirect.com/science/article/pii/S2369969821000360Myofibrillar proteinsSodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE)Rheological and surface-active property |
spellingShingle | 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 Journal of Bioresources and Bioproducts Myofibrillar proteins Sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE) Rheological and surface-active property |
title | Extraction and Characterization of Myofibrillar Proteins from Different Meat Sources: A Comparative Study |
title_full | Extraction and Characterization of Myofibrillar Proteins from Different Meat Sources: A Comparative Study |
title_fullStr | Extraction and Characterization of Myofibrillar Proteins from Different Meat Sources: A Comparative Study |
title_full_unstemmed | Extraction and Characterization of Myofibrillar Proteins from Different Meat Sources: A Comparative Study |
title_short | Extraction and Characterization of Myofibrillar Proteins from Different Meat Sources: A Comparative Study |
title_sort | extraction and characterization of myofibrillar proteins from different meat sources a comparative study |
topic | Myofibrillar proteins Sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE) Rheological and surface-active property |
url | http://www.sciencedirect.com/science/article/pii/S2369969821000360 |
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