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Changes in proteolytic enzyme activities, tenderness-related traits, and quality properties of spent hen meat affected by adenosine 5′-monophosphate during cold storage
A mechanism of postmortem tenderization by adenosine 5′-monophosphate (AMP) on spent hen meat was investigated. Breast meat samples were made into a rectangular size of 7.5 × 5 × 2 cm and grouped into 5 different treatments, followed by immersion for 24 h at 4 ± 2°C in AMP marinade solutions of 0, 1...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Elsevier
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8005812/ https://www.ncbi.nlm.nih.gov/pubmed/33744615 http://dx.doi.org/10.1016/j.psj.2021.101056 |
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author | Barido, Farouq Heidar Lee, Sung Ki |
author_facet | Barido, Farouq Heidar Lee, Sung Ki |
author_sort | Barido, Farouq Heidar |
collection | PubMed |
description | A mechanism of postmortem tenderization by adenosine 5′-monophosphate (AMP) on spent hen meat was investigated. Breast meat samples were made into a rectangular size of 7.5 × 5 × 2 cm and grouped into 5 different treatments, followed by immersion for 24 h at 4 ± 2°C in AMP marinade solutions of 0, 15, 30, 45, and 60 mmol/L that dissolved in 0.9% (w/v) saline solution. To investigate the enzymatic changes and tenderness-related traits, samples were stored until day 5 at a temperature of 2 ± 2°C. Result showed that each increase of 15 mmol/L AMP within marinade solution remarkably improved the myofibril fragmentation index and texture properties. The upregulation of tenderness-related enzymes was found for caspase-3 at 1 to 20.4 fold and 1 to 1.2 fold higher for the cathepsin-B, while a slight effect on calpains enzyme was observed. When compared with day 0 as a reference sample, the activity of the caspase-3 enzyme was more stable, as was cathepsin-B on the ultimate storage day, while the calpains enzyme showed a declining activity even after treatment. The flavor enhancement of 2.16- to 5.10-fold seemed to be a consequence of the AMP conversion into IMP that was responsible for the intensification of the umami-like flavor. No adverse effect was observed for instrumental surface color during the postmortem period. Therefore, this study suggested that the synergistic results after AMP treatment strongly contributed to postmortem tenderization mainly through cathepsin-B and caspase-3 enzyme upregulation, which led to more myofibrillar fragmentation and structural alteration of myofibrillar protein. |
format | Online Article Text |
id | pubmed-8005812 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | Elsevier |
record_format | MEDLINE/PubMed |
spelling | pubmed-80058122021-04-01 Changes in proteolytic enzyme activities, tenderness-related traits, and quality properties of spent hen meat affected by adenosine 5′-monophosphate during cold storage Barido, Farouq Heidar Lee, Sung Ki Poult Sci PROCESSING AND PRODUCT A mechanism of postmortem tenderization by adenosine 5′-monophosphate (AMP) on spent hen meat was investigated. Breast meat samples were made into a rectangular size of 7.5 × 5 × 2 cm and grouped into 5 different treatments, followed by immersion for 24 h at 4 ± 2°C in AMP marinade solutions of 0, 15, 30, 45, and 60 mmol/L that dissolved in 0.9% (w/v) saline solution. To investigate the enzymatic changes and tenderness-related traits, samples were stored until day 5 at a temperature of 2 ± 2°C. Result showed that each increase of 15 mmol/L AMP within marinade solution remarkably improved the myofibril fragmentation index and texture properties. The upregulation of tenderness-related enzymes was found for caspase-3 at 1 to 20.4 fold and 1 to 1.2 fold higher for the cathepsin-B, while a slight effect on calpains enzyme was observed. When compared with day 0 as a reference sample, the activity of the caspase-3 enzyme was more stable, as was cathepsin-B on the ultimate storage day, while the calpains enzyme showed a declining activity even after treatment. The flavor enhancement of 2.16- to 5.10-fold seemed to be a consequence of the AMP conversion into IMP that was responsible for the intensification of the umami-like flavor. No adverse effect was observed for instrumental surface color during the postmortem period. Therefore, this study suggested that the synergistic results after AMP treatment strongly contributed to postmortem tenderization mainly through cathepsin-B and caspase-3 enzyme upregulation, which led to more myofibrillar fragmentation and structural alteration of myofibrillar protein. Elsevier 2021-02-16 /pmc/articles/PMC8005812/ /pubmed/33744615 http://dx.doi.org/10.1016/j.psj.2021.101056 Text en © 2021 The Authors http://creativecommons.org/licenses/by-nc-nd/4.0/ This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/). |
spellingShingle | PROCESSING AND PRODUCT Barido, Farouq Heidar Lee, Sung Ki Changes in proteolytic enzyme activities, tenderness-related traits, and quality properties of spent hen meat affected by adenosine 5′-monophosphate during cold storage |
title | Changes in proteolytic enzyme activities, tenderness-related traits, and quality properties of spent hen meat affected by adenosine 5′-monophosphate during cold storage |
title_full | Changes in proteolytic enzyme activities, tenderness-related traits, and quality properties of spent hen meat affected by adenosine 5′-monophosphate during cold storage |
title_fullStr | Changes in proteolytic enzyme activities, tenderness-related traits, and quality properties of spent hen meat affected by adenosine 5′-monophosphate during cold storage |
title_full_unstemmed | Changes in proteolytic enzyme activities, tenderness-related traits, and quality properties of spent hen meat affected by adenosine 5′-monophosphate during cold storage |
title_short | Changes in proteolytic enzyme activities, tenderness-related traits, and quality properties of spent hen meat affected by adenosine 5′-monophosphate during cold storage |
title_sort | changes in proteolytic enzyme activities, tenderness-related traits, and quality properties of spent hen meat affected by adenosine 5′-monophosphate during cold storage |
topic | PROCESSING AND PRODUCT |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8005812/ https://www.ncbi.nlm.nih.gov/pubmed/33744615 http://dx.doi.org/10.1016/j.psj.2021.101056 |
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