Myofibrillar protein profile of Pectoralis major muscle in broiler chickens subjected to different freezing and thawing methods

The study examined the protein profile of Pectoralis major muscle in broiler chickens subjected to different freezing and thawing methods. Pectoralis major muscle was excised from the carcasses of twenty broiler chickens and split into left and right halves. The left half was subjected to slow freez...

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Main Authors: Dauda, Adeyemi Kazeem, Mislan, Noraida, Aghwan, Zeiad Amjad Abdulrazzak, Zainal Abidin, Siti Aimi Sarah, Sazili, Awis Qurni
Format: Article
Language:English
Published: Faculty of Food Science and Technology, Universiti Putra Malaysia 2014
Online Access:http://psasir.upm.edu.my/id/eprint/40783/1/41%20IFRJ%2021%20%2803%29%202014%20Aqis%20613.pdf
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author Dauda, Adeyemi Kazeem
Mislan, Noraida
Aghwan, Zeiad Amjad Abdulrazzak
Zainal Abidin, Siti Aimi Sarah
Sazili, Awis Qurni
author_facet Dauda, Adeyemi Kazeem
Mislan, Noraida
Aghwan, Zeiad Amjad Abdulrazzak
Zainal Abidin, Siti Aimi Sarah
Sazili, Awis Qurni
author_sort Dauda, Adeyemi Kazeem
collection UPM
description The study examined the protein profile of Pectoralis major muscle in broiler chickens subjected to different freezing and thawing methods. Pectoralis major muscle was excised from the carcasses of twenty broiler chickens and split into left and right halves. The left half was subjected to slow freezing (-20°C) while the right half was rapidly frozen (-80°C). The samples were stored at their respective temperature for 2 weeks and assigned to either of tap water (27°C, 30 min), room temperature (26°C, 60 min), microwave (750W, 10 min) or chiller (4°C, 6 h) thawing. Changes in myofibrillar proteins following the thawing methods were monitored through sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE). The electrophoretic profile indicated differences (p < 0.05) in intensities of the components of myofibrillar proteins among the thawing methods in both slow and rapidly frozen samples. Chiller thawing had significantly higher (p < 0.05) protein concentration than other methods in rapidly frozen samples. However, in slow freezing, there were no significant differences in protein concentration among the thawing methods. In rapidly frozen samples, the protein optical densities at molecular weight of 21, 27, 55 and 151kDa in tap water, chiller and room temperature thawing did not differ (p < 0.05). Similarly, in slowly frozen samples, protein optical densities at molecular weight of 21, 27, 85 and 151 kDa were not significantly different among chill, tap water and room temperature thawing. Microwave thawing consistently caused higher protein degradation resulting in significantly lower (p < 0.05) protein quality and quantity in both freezing methods.
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spelling upm.eprints-407832015-10-08T08:24:10Z http://psasir.upm.edu.my/id/eprint/40783/ Myofibrillar protein profile of Pectoralis major muscle in broiler chickens subjected to different freezing and thawing methods Dauda, Adeyemi Kazeem Mislan, Noraida Aghwan, Zeiad Amjad Abdulrazzak Zainal Abidin, Siti Aimi Sarah Sazili, Awis Qurni The study examined the protein profile of Pectoralis major muscle in broiler chickens subjected to different freezing and thawing methods. Pectoralis major muscle was excised from the carcasses of twenty broiler chickens and split into left and right halves. The left half was subjected to slow freezing (-20°C) while the right half was rapidly frozen (-80°C). The samples were stored at their respective temperature for 2 weeks and assigned to either of tap water (27°C, 30 min), room temperature (26°C, 60 min), microwave (750W, 10 min) or chiller (4°C, 6 h) thawing. Changes in myofibrillar proteins following the thawing methods were monitored through sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE). The electrophoretic profile indicated differences (p < 0.05) in intensities of the components of myofibrillar proteins among the thawing methods in both slow and rapidly frozen samples. Chiller thawing had significantly higher (p < 0.05) protein concentration than other methods in rapidly frozen samples. However, in slow freezing, there were no significant differences in protein concentration among the thawing methods. In rapidly frozen samples, the protein optical densities at molecular weight of 21, 27, 55 and 151kDa in tap water, chiller and room temperature thawing did not differ (p < 0.05). Similarly, in slowly frozen samples, protein optical densities at molecular weight of 21, 27, 85 and 151 kDa were not significantly different among chill, tap water and room temperature thawing. Microwave thawing consistently caused higher protein degradation resulting in significantly lower (p < 0.05) protein quality and quantity in both freezing methods. Faculty of Food Science and Technology, Universiti Putra Malaysia 2014 Article PeerReviewed application/pdf en http://psasir.upm.edu.my/id/eprint/40783/1/41%20IFRJ%2021%20%2803%29%202014%20Aqis%20613.pdf Dauda, Adeyemi Kazeem and Mislan, Noraida and Aghwan, Zeiad Amjad Abdulrazzak and Zainal Abidin, Siti Aimi Sarah and Sazili, Awis Qurni (2014) Myofibrillar protein profile of Pectoralis major muscle in broiler chickens subjected to different freezing and thawing methods. International Food Research Journal, 21 (3). pp. 1125-1129. ISSN 1985-4668; ESSN: 2231-7546 http://www.ifrj.upm.edu.my/21%20%2803%29%202014/41%20IFRJ%2021%20%2803%29%202014%20Aqis%20613.pdf
spellingShingle Dauda, Adeyemi Kazeem
Mislan, Noraida
Aghwan, Zeiad Amjad Abdulrazzak
Zainal Abidin, Siti Aimi Sarah
Sazili, Awis Qurni
Myofibrillar protein profile of Pectoralis major muscle in broiler chickens subjected to different freezing and thawing methods
title Myofibrillar protein profile of Pectoralis major muscle in broiler chickens subjected to different freezing and thawing methods
title_full Myofibrillar protein profile of Pectoralis major muscle in broiler chickens subjected to different freezing and thawing methods
title_fullStr Myofibrillar protein profile of Pectoralis major muscle in broiler chickens subjected to different freezing and thawing methods
title_full_unstemmed Myofibrillar protein profile of Pectoralis major muscle in broiler chickens subjected to different freezing and thawing methods
title_short Myofibrillar protein profile of Pectoralis major muscle in broiler chickens subjected to different freezing and thawing methods
title_sort myofibrillar protein profile of pectoralis major muscle in broiler chickens subjected to different freezing and thawing methods
url http://psasir.upm.edu.my/id/eprint/40783/1/41%20IFRJ%2021%20%2803%29%202014%20Aqis%20613.pdf
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