Effect of ultimate pH and ageing on thermal denaturation of bovine muscle proteins

Juan D. Rios-Mera; Jair Sebastião da Silva Pinto; Carmen J. Contreras-Castillo

doi:10.1016/j.meatsci.2017.04.017

Effect of ultimate pH and ageing on thermal denaturation of bovine muscle proteins

Juan D. Rios-Mera, Jair Sebastião da Silva Pinto, Carmen J. Contreras-Castillo

Research output: Contribution to journal › Article › peer-review

9 Scopus citations

Abstract

The thermal denaturation of proteins was evaluated in the natural state of bovine muscle using differential scanning calorimetry (DSC). The Longissimus lumborum muscle was selected according to ultimate pH (pH_u) values classified into two groups: low pH_u with values between 5.4 and 5.8, and intermediate pH_u with values between 5.81 and 6.19. The muscles were cut and aged at 2 °C up to 21 d post mortem. The three maximum temperatures of denaturation (T_max1, T_max2, T_max3) found in muscle were evaluated, showing higher thermal stability in the intermediate pH_u group, which could be an indicator of protection of proteins against aggregation or enzymatic activity. The thermal behavior of muscle proteins could be defined by biochemical factors that are affected by pH_u of the muscle, however, further studies are necessary to explain this process, which could have a great impact on the understanding of the final tenderness achieved in meat.

Original language	English
Pages (from-to)	25-27
Number of pages	3
Journal	Meat Science
Volume	131
DOIs	https://doi.org/10.1016/j.meatsci.2017.04.017
State	Published - 1 Sep 2017
Externally published	Yes

Bibliographical note

Publisher Copyright:
© 2017

Keywords

DSC
Muscle proteins
Protein degradation

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10.1016/j.meatsci.2017.04.017

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title = "Effect of ultimate pH and ageing on thermal denaturation of bovine muscle proteins",

abstract = "The thermal denaturation of proteins was evaluated in the natural state of bovine muscle using differential scanning calorimetry (DSC). The Longissimus lumborum muscle was selected according to ultimate pH (pHu) values classified into two groups: low pHu with values between 5.4 and 5.8, and intermediate pHu with values between 5.81 and 6.19. The muscles were cut and aged at 2 °C up to 21 d post mortem. The three maximum temperatures of denaturation (Tmax1, Tmax2, Tmax3) found in muscle were evaluated, showing higher thermal stability in the intermediate pHu group, which could be an indicator of protection of proteins against aggregation or enzymatic activity. The thermal behavior of muscle proteins could be defined by biochemical factors that are affected by pHu of the muscle, however, further studies are necessary to explain this process, which could have a great impact on the understanding of the final tenderness achieved in meat.",

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AU - da Silva Pinto, Jair Sebastião

AU - Contreras-Castillo, Carmen J.

PY - 2017/9/1

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N2 - The thermal denaturation of proteins was evaluated in the natural state of bovine muscle using differential scanning calorimetry (DSC). The Longissimus lumborum muscle was selected according to ultimate pH (pHu) values classified into two groups: low pHu with values between 5.4 and 5.8, and intermediate pHu with values between 5.81 and 6.19. The muscles were cut and aged at 2 °C up to 21 d post mortem. The three maximum temperatures of denaturation (Tmax1, Tmax2, Tmax3) found in muscle were evaluated, showing higher thermal stability in the intermediate pHu group, which could be an indicator of protection of proteins against aggregation or enzymatic activity. The thermal behavior of muscle proteins could be defined by biochemical factors that are affected by pHu of the muscle, however, further studies are necessary to explain this process, which could have a great impact on the understanding of the final tenderness achieved in meat.

AB - The thermal denaturation of proteins was evaluated in the natural state of bovine muscle using differential scanning calorimetry (DSC). The Longissimus lumborum muscle was selected according to ultimate pH (pHu) values classified into two groups: low pHu with values between 5.4 and 5.8, and intermediate pHu with values between 5.81 and 6.19. The muscles were cut and aged at 2 °C up to 21 d post mortem. The three maximum temperatures of denaturation (Tmax1, Tmax2, Tmax3) found in muscle were evaluated, showing higher thermal stability in the intermediate pHu group, which could be an indicator of protection of proteins against aggregation or enzymatic activity. The thermal behavior of muscle proteins could be defined by biochemical factors that are affected by pHu of the muscle, however, further studies are necessary to explain this process, which could have a great impact on the understanding of the final tenderness achieved in meat.

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KW - Protein degradation

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JO - Meat Science

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ER -

Effect of ultimate pH and ageing on thermal denaturation of bovine muscle proteins

Abstract

Bibliographical note

Keywords

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