Dehydrogenase Enzymes Associated to Glycolysis in Beef Carcasses Stored at 0 °C

Cristian A. Acevedo, María J. Cornejo, Yusser A. Olguín, Ronny Vallejos, Donald I. Brown

Resultado de la investigación: Article

1 Cita (Scopus)

Resumen

After the death of an animal, cell metabolism is controlled locally. The post-mortem oxygen depletion increases the glycolytic activity and lactate production. However, many mechanisms of post-mortem metabolic regulation have not been fully investigated in beef carcasses. In this work, we studied the post-mortem glycolytic behavior (including lactate dehydrogenase) and three dehydrogenase associated to glycolysis (glycerophosphate dehydrogenase, glucose 6-phosphate dehydrogenase, and glycerol dehydrogenase) by using cytochemistry techniques in three fast-twitch muscles (M. longissimus dorsi, M. semimembranosus, and M. cutaneus trunci) of carcasses stored at 0 °C. Our results indicate that glycolysis depends on the type of muscle. The post-mortem glycolytic flux and lactate dehydrogenase activity of M. cutaneus trunci was the lowest of the three muscles studied. Of the other dehydrogenases analyzed, only glycerophosphate and glycerol dehydrogenase showed clear cytochemical reaction. Glucose 6-phosphate dehydrogenase was not used by muscles very much. The glycerophosphate dehydrogenase was the strongest enzymatic activity correlated to the post-mortem glycolytic flux. In addition, a relationship between glycerophosphate dehydrogenase and glycerol dehydrogenase was detected by using a multiple regression model. This phenomenon was studied by using bioinformatics tools, suggesting that glycerophosphate dehydrogenase could oxidize the glycerol in bovine fast-twitch muscles.

Idioma originalEnglish
Páginas (desde-hasta)1696-1702
Número de páginas7
PublicaciónFood and Bioprocess Technology
Volumen6
N.º7
DOI
EstadoPublished - 1 jul 2013

Huella dactilar

Glycerolphosphate Dehydrogenase
Beef
glycerol dehydrogenase
beef carcasses
glycolysis
Glycolysis
Muscle
Oxidoreductases
Enzymes
Muscles
muscles
enzymes
Glucosephosphate Dehydrogenase
glucose-6-phosphate 1-dehydrogenase
lactate dehydrogenase
L-Lactate Dehydrogenase
Glycerol
Fluxes
cytochemistry
Histocytochemistry

ASJC Scopus subject areas

  • Food Science
  • Process Chemistry and Technology
  • Safety, Risk, Reliability and Quality
  • Industrial and Manufacturing Engineering

Citar esto

Acevedo, C. A., Cornejo, M. J., Olguín, Y. A., Vallejos, R., & Brown, D. I. (2013). Dehydrogenase Enzymes Associated to Glycolysis in Beef Carcasses Stored at 0 °C. Food and Bioprocess Technology, 6(7), 1696-1702. https://doi.org/10.1007/s11947-012-0814-9
Acevedo, Cristian A. ; Cornejo, María J. ; Olguín, Yusser A. ; Vallejos, Ronny ; Brown, Donald I. / Dehydrogenase Enzymes Associated to Glycolysis in Beef Carcasses Stored at 0 °C. En: Food and Bioprocess Technology. 2013 ; Vol. 6, N.º 7. pp. 1696-1702.
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abstract = "After the death of an animal, cell metabolism is controlled locally. The post-mortem oxygen depletion increases the glycolytic activity and lactate production. However, many mechanisms of post-mortem metabolic regulation have not been fully investigated in beef carcasses. In this work, we studied the post-mortem glycolytic behavior (including lactate dehydrogenase) and three dehydrogenase associated to glycolysis (glycerophosphate dehydrogenase, glucose 6-phosphate dehydrogenase, and glycerol dehydrogenase) by using cytochemistry techniques in three fast-twitch muscles (M. longissimus dorsi, M. semimembranosus, and M. cutaneus trunci) of carcasses stored at 0 °C. Our results indicate that glycolysis depends on the type of muscle. The post-mortem glycolytic flux and lactate dehydrogenase activity of M. cutaneus trunci was the lowest of the three muscles studied. Of the other dehydrogenases analyzed, only glycerophosphate and glycerol dehydrogenase showed clear cytochemical reaction. Glucose 6-phosphate dehydrogenase was not used by muscles very much. The glycerophosphate dehydrogenase was the strongest enzymatic activity correlated to the post-mortem glycolytic flux. In addition, a relationship between glycerophosphate dehydrogenase and glycerol dehydrogenase was detected by using a multiple regression model. This phenomenon was studied by using bioinformatics tools, suggesting that glycerophosphate dehydrogenase could oxidize the glycerol in bovine fast-twitch muscles.",
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Acevedo, CA, Cornejo, MJ, Olguín, YA, Vallejos, R & Brown, DI 2013, 'Dehydrogenase Enzymes Associated to Glycolysis in Beef Carcasses Stored at 0 °C', Food and Bioprocess Technology, vol. 6, n.º 7, pp. 1696-1702. https://doi.org/10.1007/s11947-012-0814-9

Dehydrogenase Enzymes Associated to Glycolysis in Beef Carcasses Stored at 0 °C. / Acevedo, Cristian A.; Cornejo, María J.; Olguín, Yusser A.; Vallejos, Ronny; Brown, Donald I.

En: Food and Bioprocess Technology, Vol. 6, N.º 7, 01.07.2013, p. 1696-1702.

Resultado de la investigación: Article

TY - JOUR

T1 - Dehydrogenase Enzymes Associated to Glycolysis in Beef Carcasses Stored at 0 °C

AU - Acevedo, Cristian A.

AU - Cornejo, María J.

AU - Olguín, Yusser A.

AU - Vallejos, Ronny

AU - Brown, Donald I.

PY - 2013/7/1

Y1 - 2013/7/1

N2 - After the death of an animal, cell metabolism is controlled locally. The post-mortem oxygen depletion increases the glycolytic activity and lactate production. However, many mechanisms of post-mortem metabolic regulation have not been fully investigated in beef carcasses. In this work, we studied the post-mortem glycolytic behavior (including lactate dehydrogenase) and three dehydrogenase associated to glycolysis (glycerophosphate dehydrogenase, glucose 6-phosphate dehydrogenase, and glycerol dehydrogenase) by using cytochemistry techniques in three fast-twitch muscles (M. longissimus dorsi, M. semimembranosus, and M. cutaneus trunci) of carcasses stored at 0 °C. Our results indicate that glycolysis depends on the type of muscle. The post-mortem glycolytic flux and lactate dehydrogenase activity of M. cutaneus trunci was the lowest of the three muscles studied. Of the other dehydrogenases analyzed, only glycerophosphate and glycerol dehydrogenase showed clear cytochemical reaction. Glucose 6-phosphate dehydrogenase was not used by muscles very much. The glycerophosphate dehydrogenase was the strongest enzymatic activity correlated to the post-mortem glycolytic flux. In addition, a relationship between glycerophosphate dehydrogenase and glycerol dehydrogenase was detected by using a multiple regression model. This phenomenon was studied by using bioinformatics tools, suggesting that glycerophosphate dehydrogenase could oxidize the glycerol in bovine fast-twitch muscles.

AB - After the death of an animal, cell metabolism is controlled locally. The post-mortem oxygen depletion increases the glycolytic activity and lactate production. However, many mechanisms of post-mortem metabolic regulation have not been fully investigated in beef carcasses. In this work, we studied the post-mortem glycolytic behavior (including lactate dehydrogenase) and three dehydrogenase associated to glycolysis (glycerophosphate dehydrogenase, glucose 6-phosphate dehydrogenase, and glycerol dehydrogenase) by using cytochemistry techniques in three fast-twitch muscles (M. longissimus dorsi, M. semimembranosus, and M. cutaneus trunci) of carcasses stored at 0 °C. Our results indicate that glycolysis depends on the type of muscle. The post-mortem glycolytic flux and lactate dehydrogenase activity of M. cutaneus trunci was the lowest of the three muscles studied. Of the other dehydrogenases analyzed, only glycerophosphate and glycerol dehydrogenase showed clear cytochemical reaction. Glucose 6-phosphate dehydrogenase was not used by muscles very much. The glycerophosphate dehydrogenase was the strongest enzymatic activity correlated to the post-mortem glycolytic flux. In addition, a relationship between glycerophosphate dehydrogenase and glycerol dehydrogenase was detected by using a multiple regression model. This phenomenon was studied by using bioinformatics tools, suggesting that glycerophosphate dehydrogenase could oxidize the glycerol in bovine fast-twitch muscles.

KW - Beef

KW - Carcasses

KW - Dehydrogenases

KW - Enzymes

KW - Glycolysis

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U2 - 10.1007/s11947-012-0814-9

DO - 10.1007/s11947-012-0814-9

M3 - Article

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SN - 1935-5130

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