The degree to which lipid and myoglobin (Mb) oxidation processes interact in meat can be species-specific. We investigated the effects of beef and pork sarcoplasmic extracts containing different Mb concentrations on lipid oxidation in a liposome system. Sarcoplasm was extracted from beef and pork longissimus dorsi and psoas major muscles. Beef sarcoplasm was diluted with 0.1 M phosphate buffer to obtain a Mb concentration equivalent to that in pork sarcoplasm. Conversely, equine heart Mb was added to pork sarcoplasm to match the myoglobin concentration of beef sarcoplasm. This resulted in beef and pork sarcoplasms, each with 2 different Mb concentrations for the longissimus (0.02 mM and 0.07 mM) and psoas (0.05 and 0.12 mM). Sarcoplasm (or phosphate buffer control) was incorporated within a phosphatidylcholine liposome preparation and incubated at 25 degrees C. Thiobarbituric acid reactive substances (TBARS) were measured at 0, 30, 60, 90, and 120 min of incubation. Regardless of species, greater Mb concentration within the sarcoplasm increased lipid oxidation (P < 0.05). Across muscles, pork sarcoplasm had lower TBARS values than beef sarcoplasm (P < 0.05). Our results suggest that pork sarcoplasm has a lesser effect on lipid oxidation than beef sarcoplasm for a common Mb concentration. However, increased myoglobin concentration within sarcoplasm promotes lipid oxidation regardless of species.
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http://dx.doi.org/10.1111/j.1750-3841.2008.01021.x | DOI Listing |
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