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http://krishi.icar.gov.in/jspui/handle/123456789/47247
Title: | Extraction and characterization of myofibrillar proteins from different meat sources: A comparative study |
Other Titles: | Not Available |
Authors: | Dara, P. K. Anjana Geetha Upasana Mohanty Mahadevan, R. Suseela Mathew Ravishankar, C. N. Anandan, R. |
ICAR Data Use Licennce: | http://krishi.icar.gov.in/PDF/ICAR_Data_Use_Licence.pdf |
Author's Affiliated institute: | ICAR::Central Institute of Fisheries Technology Department of Food and Nutrition, Mody University, Lakshmangarh 332311, Rajasthan, India College of fisheries, Central Agricultural University, Tripura 799210, India |
Published/ Complete Date: | 2021-04-07 |
Project Code: | Not Available |
Keywords: | Myofibrillar proteins Sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE) Rheological and surface-active property |
Publisher: | Elsevier |
Citation: | Dara, P. K., Anjana Geetha, Upasana Mohanty, Mahadevan R., Suseela Mathew, Ravishankar, C. N. and Anandan, R. (2021). Extraction and characterization of myofibrillar proteins from different meat sources: a comparative study. Journal of Bioresources and Bioproducts. https://doi.org/10.1016/j.jobab.2021.04.004 |
Series/Report no.: | Not Available; |
Abstract/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. |
Description: | Not Available |
ISSN: | 2369-9698 |
Type(s) of content: | Research Paper |
Sponsors: | Not Available |
Language: | English |
Name of Journal: | Journal of Bioresources and Bioproducts |
Journal Type: | International |
Volume No.: | Not Available |
Page Number: | Not Available |
Name of the Division/Regional Station: | Not Available |
Source, DOI or any other URL: | https://doi.org/10.1016/j.jobab.2021.04.004 |
URI: | http://krishi.icar.gov.in/jspui/handle/123456789/47247 |
Appears in Collections: | FS-CIFT-Publication |
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