Details

Autor(en) / Beteiligte

• Kim, Y.H.
• Keeton, J.T.
• Smith, S.B.
• Berghman, L.R.
• Savell, J.W.

Titel

Role of lactate dehydrogenase in metmyoglobin reduction and color stability of different bovine muscles

Ist Teil von

• Meat science, 2009-11, Vol.83 (3), p.376-382

Ort / Verlag

Kidlington: Elsevier Ltd

Erscheinungsjahr

2009

Link zum Volltext

Quelle

Elsevier ScienceDirect Journals Complete

Beschreibungen/Notizen

• The role of lactate dehydrogenase (LDH) in metmyoglobin reducing activity (MRA) and color stability of different bovine muscles was studied in two consecutive experiments. In experiment 1, three different bovine muscles – M. longissimus lumborum (LL), M. semimembranosus (SM), and M. psoas major (PM) – were obtained ( n = 7, respectively), cut into steaks, PVC packaged, and then displayed for 7 days at 1 °C. The LL was the most red over display time and had more ( P < 0.05) LDH-B activity (catalyzing toward NADH generation), LDH1 isoform expression, NADH, and higher ( P < 0.05) MRA than the other two muscles studied. The PM had the least color stability and lowest MRA. In experiment 2, LL steaks ( n = 8) were cut in half, one side syringe-injected with oxamate, and the other injected with distilled water. Inclusion of oxamate decreased ( P < 0.05) LDH-B activity, NADH, and a* values after 10 days display at 1 °C. These results suggest that variation in color stability of physiologically different muscles is regulated by different replenishment rates of NADH via different LDH isozymes.