A proteomic based assessment on changes in myofirbrillar proteins of goat longissimus muscle as affected by heat treatments
The present study examined the effect of different heat treatments; (1) chilled, (2) boiled at 100°C for 30 min, and (3) autoclaved at 121°C at 15 psi for 20 min, on the expression of goat skeletal muscle proteins using two-dimensional gel electrophoresis. The molecular weight (MW) and isoelectric p...
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| Format: | Article |
| Language: | English |
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Pakistan Agricultural Scientists Forum
2014
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| Online Access: | http://psasir.upm.edu.my/id/eprint/36235/ http://psasir.upm.edu.my/id/eprint/36235/1/A%20proteomic%20based%20assessment%20on%20changes%20in%20myofirbrillar%20proteins%20of%20goat%20longissimus%20muscle%20as%20affected%20by%20heat%20treatments.pdf |
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| author | Zainal Abidin, Siti Aimi Sarah Karsani, Saiful Anuar Ismail, Amin Khairil Mokhtar, Nur Fadhilah Sazili, Awis Qurni |
| author_facet | Zainal Abidin, Siti Aimi Sarah Karsani, Saiful Anuar Ismail, Amin Khairil Mokhtar, Nur Fadhilah Sazili, Awis Qurni |
| author_sort | Zainal Abidin, Siti Aimi Sarah |
| building | UPM Institutional Repository |
| collection | Online Access |
| description | The present study examined the effect of different heat treatments; (1) chilled, (2) boiled at 100°C for 30 min, and (3) autoclaved at 121°C at 15 psi for 20 min, on the expression of goat skeletal muscle proteins using two-dimensional gel electrophoresis. The molecular weight (MW) and isoelectric point (pI) of heat stable proteins were characterised followed by identification of the proteins by MALDI-TOF/TOF mass spectrometry. There were 153 protein spots obtained in the boiled samples, while only 46 protein spots were observed in the autoclaved samples. Thirteen spots that exhibited high intensity of protein were chosen from the autoclaved sample for MALDI-TOF/TOF mass spectrometry analysis. The putative heat stable proteins identified were myosin light chain (MLC), actin, tropomyosin (TPM), troponin T (TnT), myoglobin, and creatine kinase. The Proc-GLM analysis revealed that the heat treatments have resulted in significant differences in spot intensities of actin, troponin T (TnT), myoglobin, and creatine kinase with no significant changes noted in other proteins. |
| first_indexed | 2025-11-15T09:31:55Z |
| format | Article |
| id | upm-36235 |
| institution | Universiti Putra Malaysia |
| institution_category | Local University |
| language | English |
| last_indexed | 2025-11-15T09:31:55Z |
| publishDate | 2014 |
| publisher | Pakistan Agricultural Scientists Forum |
| recordtype | eprints |
| repository_type | Digital Repository |
| spelling | upm-362352015-11-11T07:04:05Z http://psasir.upm.edu.my/id/eprint/36235/ A proteomic based assessment on changes in myofirbrillar proteins of goat longissimus muscle as affected by heat treatments Zainal Abidin, Siti Aimi Sarah Karsani, Saiful Anuar Ismail, Amin Khairil Mokhtar, Nur Fadhilah Sazili, Awis Qurni The present study examined the effect of different heat treatments; (1) chilled, (2) boiled at 100°C for 30 min, and (3) autoclaved at 121°C at 15 psi for 20 min, on the expression of goat skeletal muscle proteins using two-dimensional gel electrophoresis. The molecular weight (MW) and isoelectric point (pI) of heat stable proteins were characterised followed by identification of the proteins by MALDI-TOF/TOF mass spectrometry. There were 153 protein spots obtained in the boiled samples, while only 46 protein spots were observed in the autoclaved samples. Thirteen spots that exhibited high intensity of protein were chosen from the autoclaved sample for MALDI-TOF/TOF mass spectrometry analysis. The putative heat stable proteins identified were myosin light chain (MLC), actin, tropomyosin (TPM), troponin T (TnT), myoglobin, and creatine kinase. The Proc-GLM analysis revealed that the heat treatments have resulted in significant differences in spot intensities of actin, troponin T (TnT), myoglobin, and creatine kinase with no significant changes noted in other proteins. Pakistan Agricultural Scientists Forum 2014 Article PeerReviewed application/pdf en http://psasir.upm.edu.my/id/eprint/36235/1/A%20proteomic%20based%20assessment%20on%20changes%20in%20myofirbrillar%20proteins%20of%20goat%20longissimus%20muscle%20as%20affected%20by%20heat%20treatments.pdf Zainal Abidin, Siti Aimi Sarah and Karsani, Saiful Anuar and Ismail, Amin and Khairil Mokhtar, Nur Fadhilah and Sazili, Awis Qurni (2014) A proteomic based assessment on changes in myofirbrillar proteins of goat longissimus muscle as affected by heat treatments. The Journal of Animal and Plant Sciences, 24 (2). pp. 406-412. ISSN 1018-7081 http://www.thejaps.org.pk/Volume/2014/24-2/index.php |
| spellingShingle | Zainal Abidin, Siti Aimi Sarah Karsani, Saiful Anuar Ismail, Amin Khairil Mokhtar, Nur Fadhilah Sazili, Awis Qurni A proteomic based assessment on changes in myofirbrillar proteins of goat longissimus muscle as affected by heat treatments |
| title | A proteomic based assessment on changes in myofirbrillar proteins of goat longissimus muscle as affected by heat treatments |
| title_full | A proteomic based assessment on changes in myofirbrillar proteins of goat longissimus muscle as affected by heat treatments |
| title_fullStr | A proteomic based assessment on changes in myofirbrillar proteins of goat longissimus muscle as affected by heat treatments |
| title_full_unstemmed | A proteomic based assessment on changes in myofirbrillar proteins of goat longissimus muscle as affected by heat treatments |
| title_short | A proteomic based assessment on changes in myofirbrillar proteins of goat longissimus muscle as affected by heat treatments |
| title_sort | proteomic based assessment on changes in myofirbrillar proteins of goat longissimus muscle as affected by heat treatments |
| url | http://psasir.upm.edu.my/id/eprint/36235/ http://psasir.upm.edu.my/id/eprint/36235/ http://psasir.upm.edu.my/id/eprint/36235/1/A%20proteomic%20based%20assessment%20on%20changes%20in%20myofirbrillar%20proteins%20of%20goat%20longissimus%20muscle%20as%20affected%20by%20heat%20treatments.pdf |