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The influence of ultrasound and adenosine 5′-monophosphate marination on tenderness and structure of myofibrillar proteins of beef

OBJECTIVE: The aim was to investigate the influence of ultrasound and adenosine 5′-monophosphate (AMP) marination (UAMP) on tenderness and structure of myofibrillar proteins of beef. METHODS: Five groups, the untreated meat (Control), deionized water marination (DW), ultrasound followed by DW (UDW),...

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Detalles Bibliográficos
Autores principales: Zou, Ye, Yang, Heng, Zhang, Muhan, Zhang, Xinxiao, Xu, Weimin, Wang, Daoying
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Asian-Australasian Association of Animal Production Societies (AAAP) and Korean Society of Animal Science and Technology (KSAST) 2019
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6718909/
https://www.ncbi.nlm.nih.gov/pubmed/31010995
http://dx.doi.org/10.5713/ajas.18.0780
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author Zou, Ye
Yang, Heng
Zhang, Muhan
Zhang, Xinxiao
Xu, Weimin
Wang, Daoying
author_facet Zou, Ye
Yang, Heng
Zhang, Muhan
Zhang, Xinxiao
Xu, Weimin
Wang, Daoying
author_sort Zou, Ye
collection PubMed
description OBJECTIVE: The aim was to investigate the influence of ultrasound and adenosine 5′-monophosphate (AMP) marination (UAMP) on tenderness and structure of myofibrillar proteins of beef. METHODS: Five groups, the untreated meat (Control), deionized water marination (DW), ultrasound followed by DW (UDW), AMP marination (AMP), and ultrasound followed by AMP (UAMP) were studied. Myofibrillar fragmentation, cooking loss, shear force, thermograms, histological observation of meats and myofibrillar proteins properties were investigated in these different treatments. RESULTS: The results showed that UAMP significantly increased myofibrillar fragmentation index from 152 (Control), 231 (AMP), and 307 (UDW) to 355 (p<0.05), respectively. The lowest cooking loss, shear force and peak denaturation temperature were observed in UAMP. In histological observation, UDW and UAMP had more fragmented muscular bundles than the others. Furthermore, a drastic increase in α-helix and decrease in β-sheet of myofibrillar proteins was observed in UAMP, implying the disaggregation of protein samples. The synchronous fluorescence spectra of myofibrillar proteins in UAMP suggested the combination of ultrasound and AMP could accelerate the unfolding molecular structure and destroying hydrophobic interactions. The results of circular dichroism and synchronous fluorescence spectra for myofibrillar proteins coincided with the microstructures of beef. CONCLUSION: The results indicate that ultrasound combined with AMP improved meat tenderness not only by disruption in muscle integrity, increasing water retention, but also altering their spatial structure of myofibrillar proteins.
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spelling pubmed-67189092019-10-01 The influence of ultrasound and adenosine 5′-monophosphate marination on tenderness and structure of myofibrillar proteins of beef Zou, Ye Yang, Heng Zhang, Muhan Zhang, Xinxiao Xu, Weimin Wang, Daoying Asian-Australas J Anim Sci Article OBJECTIVE: The aim was to investigate the influence of ultrasound and adenosine 5′-monophosphate (AMP) marination (UAMP) on tenderness and structure of myofibrillar proteins of beef. METHODS: Five groups, the untreated meat (Control), deionized water marination (DW), ultrasound followed by DW (UDW), AMP marination (AMP), and ultrasound followed by AMP (UAMP) were studied. Myofibrillar fragmentation, cooking loss, shear force, thermograms, histological observation of meats and myofibrillar proteins properties were investigated in these different treatments. RESULTS: The results showed that UAMP significantly increased myofibrillar fragmentation index from 152 (Control), 231 (AMP), and 307 (UDW) to 355 (p<0.05), respectively. The lowest cooking loss, shear force and peak denaturation temperature were observed in UAMP. In histological observation, UDW and UAMP had more fragmented muscular bundles than the others. Furthermore, a drastic increase in α-helix and decrease in β-sheet of myofibrillar proteins was observed in UAMP, implying the disaggregation of protein samples. The synchronous fluorescence spectra of myofibrillar proteins in UAMP suggested the combination of ultrasound and AMP could accelerate the unfolding molecular structure and destroying hydrophobic interactions. The results of circular dichroism and synchronous fluorescence spectra for myofibrillar proteins coincided with the microstructures of beef. CONCLUSION: The results indicate that ultrasound combined with AMP improved meat tenderness not only by disruption in muscle integrity, increasing water retention, but also altering their spatial structure of myofibrillar proteins. Asian-Australasian Association of Animal Production Societies (AAAP) and Korean Society of Animal Science and Technology (KSAST) 2019-10 2019-03-07 /pmc/articles/PMC6718909/ /pubmed/31010995 http://dx.doi.org/10.5713/ajas.18.0780 Text en Copyright © 2019 by Asian-Australasian Journal of Animal Sciences This is an open-access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Article
Zou, Ye
Yang, Heng
Zhang, Muhan
Zhang, Xinxiao
Xu, Weimin
Wang, Daoying
The influence of ultrasound and adenosine 5′-monophosphate marination on tenderness and structure of myofibrillar proteins of beef
title The influence of ultrasound and adenosine 5′-monophosphate marination on tenderness and structure of myofibrillar proteins of beef
title_full The influence of ultrasound and adenosine 5′-monophosphate marination on tenderness and structure of myofibrillar proteins of beef
title_fullStr The influence of ultrasound and adenosine 5′-monophosphate marination on tenderness and structure of myofibrillar proteins of beef
title_full_unstemmed The influence of ultrasound and adenosine 5′-monophosphate marination on tenderness and structure of myofibrillar proteins of beef
title_short The influence of ultrasound and adenosine 5′-monophosphate marination on tenderness and structure of myofibrillar proteins of beef
title_sort influence of ultrasound and adenosine 5′-monophosphate marination on tenderness and structure of myofibrillar proteins of beef
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6718909/
https://www.ncbi.nlm.nih.gov/pubmed/31010995
http://dx.doi.org/10.5713/ajas.18.0780
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