Journal
MEAT SCIENCE
Volume 137, Issue -, Pages 85-91Publisher
ELSEVIER SCI LTD
DOI: 10.1016/j.meatsci.2017.11.009
Keywords
Mitochondrial F-1-ATPase; Glycolytic flux; Ultimate pH; Acid meat
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Funding
- National Institute of Food and Agriculture, U.S. Department of Agriculture [2014-67017-21654]
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The experiment was conducted to identify the mitochondrial protein responsible for enhancing glycolytic flux. We hypothesized that mitochondrial F-1-ATPase promotes ATP hydrolysis and thereby the flux through glycolysis. Porcine longissimus muscle mitochondria were incorporated into an in vitro system designed to recapitulate postmortem glycolysis with or without Na-azide to specifically inhibit the beta-subunit of mitochondrial F-1-ATPase that catalyzes ATP hydrolysis. Addition of mitochondria enhanced ATP hydrolysis, glycogen degradation, lactate accumulation, and pH decline in the in vitro system. However, the majority of mitochondria-mediated enhancement in glycolytic flux was abolished in the presence of Na-azide. To investigate further, myofibrillar and mitochondrial proteins were added to the in vitro system after 240 min from the initiation of the reaction. Greater pH decline and lactate accumulation were observed in system containing mitochondrial protein compared to their myofibrillar counterpart. In conclusion, mitochondrial F-1-ATPase is capable of increasing glycolytic flux through promoting greater ATP hydrolysis at lower pH.
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