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Comparing the effect of heat on tropomyosin isoforms patterns from water buffalo and wild boar meat by two-dimensional gel electrophoresis

Tropomyosin is one of the most abundant proteins in meat; however, very little is known about it due to the lack of scientific literature. In this study, the spot volume of tropomyosin (TPM) isoforms, TPM2 and TPM1, in meat from water buffalo and wild boar subjected to various cook treatments were...

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Main Authors: Nadiah Mat Junoh,, Mohd Hafis Yuswan,, Shuhaimi Mustafa,, Amalia Mohd Hashim,, Rozi Mohamed,, Lee, Shiou Yih, Nazia Abdul Majid,, Siti Aimi Sarah,, Dhilia Udie Lamasudin,
Format: Article
Language:English
Published: Penerbit Universiti Kebangsaan Malaysia 2019
Online Access:http://journalarticle.ukm.my/14677/1/48_02_19.pdf
http://journalarticle.ukm.my/14677/
http://www.mabjournal.com/index.php?option=com_content&view=article&id=921&catid=59:current-view&Itemid=56
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spelling my-ukm.journal.146772020-05-27T01:04:07Z http://journalarticle.ukm.my/14677/ Comparing the effect of heat on tropomyosin isoforms patterns from water buffalo and wild boar meat by two-dimensional gel electrophoresis Nadiah Mat Junoh, Mohd Hafis Yuswan, Shuhaimi Mustafa, Amalia Mohd Hashim, Rozi Mohamed, Lee, Shiou Yih Nazia Abdul Majid, Siti Aimi Sarah, Dhilia Udie Lamasudin, Tropomyosin is one of the most abundant proteins in meat; however, very little is known about it due to the lack of scientific literature. In this study, the spot volume of tropomyosin (TPM) isoforms, TPM2 and TPM1, in meat from water buffalo and wild boar subjected to various cook treatments were compared. We hypothesized that primary structures of the tropomyosin isoforms from both species would remain stable despite the application of heat. Proteins extracted from the treated meats were analyzed using two-dimensional gel electrophoresis and mass spectrometry. A Kruskal-Wallis test showed that there were no significant differences in protein spot volumes for all treatments; however, a significant difference was observed between species. Changes in the amino acid sequence of TPM1 were observed between the two species, indicating that the isoforms could be used as thermostable proteins or peptide markers for species identification because of their resistance to high temperatures. Penerbit Universiti Kebangsaan Malaysia 2019-05 Article PeerReviewed application/pdf en http://journalarticle.ukm.my/14677/1/48_02_19.pdf Nadiah Mat Junoh, and Mohd Hafis Yuswan, and Shuhaimi Mustafa, and Amalia Mohd Hashim, and Rozi Mohamed, and Lee, Shiou Yih and Nazia Abdul Majid, and Siti Aimi Sarah, and Dhilia Udie Lamasudin, (2019) Comparing the effect of heat on tropomyosin isoforms patterns from water buffalo and wild boar meat by two-dimensional gel electrophoresis. Malaysian Applied Biology, 48 (2). pp. 131-139. ISSN 0126-8643 http://www.mabjournal.com/index.php?option=com_content&view=article&id=921&catid=59:current-view&Itemid=56
institution Universiti Kebangsaan Malaysia
building Tun Sri Lanang Library
collection Institutional Repository
continent Asia
country Malaysia
content_provider Universiti Kebangsaan Malaysia
content_source UKM Journal Article Repository
url_provider http://journalarticle.ukm.my/
language English
description Tropomyosin is one of the most abundant proteins in meat; however, very little is known about it due to the lack of scientific literature. In this study, the spot volume of tropomyosin (TPM) isoforms, TPM2 and TPM1, in meat from water buffalo and wild boar subjected to various cook treatments were compared. We hypothesized that primary structures of the tropomyosin isoforms from both species would remain stable despite the application of heat. Proteins extracted from the treated meats were analyzed using two-dimensional gel electrophoresis and mass spectrometry. A Kruskal-Wallis test showed that there were no significant differences in protein spot volumes for all treatments; however, a significant difference was observed between species. Changes in the amino acid sequence of TPM1 were observed between the two species, indicating that the isoforms could be used as thermostable proteins or peptide markers for species identification because of their resistance to high temperatures.
format Article
author Nadiah Mat Junoh,
Mohd Hafis Yuswan,
Shuhaimi Mustafa,
Amalia Mohd Hashim,
Rozi Mohamed,
Lee, Shiou Yih
Nazia Abdul Majid,
Siti Aimi Sarah,
Dhilia Udie Lamasudin,
spellingShingle Nadiah Mat Junoh,
Mohd Hafis Yuswan,
Shuhaimi Mustafa,
Amalia Mohd Hashim,
Rozi Mohamed,
Lee, Shiou Yih
Nazia Abdul Majid,
Siti Aimi Sarah,
Dhilia Udie Lamasudin,
Comparing the effect of heat on tropomyosin isoforms patterns from water buffalo and wild boar meat by two-dimensional gel electrophoresis
author_facet Nadiah Mat Junoh,
Mohd Hafis Yuswan,
Shuhaimi Mustafa,
Amalia Mohd Hashim,
Rozi Mohamed,
Lee, Shiou Yih
Nazia Abdul Majid,
Siti Aimi Sarah,
Dhilia Udie Lamasudin,
author_sort Nadiah Mat Junoh,
title Comparing the effect of heat on tropomyosin isoforms patterns from water buffalo and wild boar meat by two-dimensional gel electrophoresis
title_short Comparing the effect of heat on tropomyosin isoforms patterns from water buffalo and wild boar meat by two-dimensional gel electrophoresis
title_full Comparing the effect of heat on tropomyosin isoforms patterns from water buffalo and wild boar meat by two-dimensional gel electrophoresis
title_fullStr Comparing the effect of heat on tropomyosin isoforms patterns from water buffalo and wild boar meat by two-dimensional gel electrophoresis
title_full_unstemmed Comparing the effect of heat on tropomyosin isoforms patterns from water buffalo and wild boar meat by two-dimensional gel electrophoresis
title_sort comparing the effect of heat on tropomyosin isoforms patterns from water buffalo and wild boar meat by two-dimensional gel electrophoresis
publisher Penerbit Universiti Kebangsaan Malaysia
publishDate 2019
url http://journalarticle.ukm.my/14677/1/48_02_19.pdf
http://journalarticle.ukm.my/14677/
http://www.mabjournal.com/index.php?option=com_content&view=article&id=921&catid=59:current-view&Itemid=56
_version_ 1669008496731881472
score 13.211869

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