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Food Structure

Authors

H. J. Swatland

Abstract

Techniques were developed to study the microdistribution of aerobic enzymes and myoglobin directly on the surfaces of slices of meat. Despite its solubility, the in vivo distribution of myoglobin was preserved post mortem and, in pork, the distribution of myoglobin followed the distribution of aerobic muscle fibers. Aerobic fibers were grouped centrally in their fasciculi. Differences in oxidative enzyme activity between central and peripheral fibers within fasciculi were detected by staining with methylene blue in an atmosphere with controlled levels of oxygen and nitrogen. Within individual aerobic fibers, there was a radial gradient of SOH (succinate dehydrogenase) activity with more intense activity in the subsarcolemmal region. However, the magnitude of the slope of the gradient in each fiber was a function of reaction time. Within individual aerobic fibers, myoglobin was distributed evenly across the fiber. By fiber optic spectrophotometry, myoglobin had an absorbance peak at 560 run and a low absorbance at 490 nm. When converted to nitrosylhemochrome in hams cured with sodium nitrite, there was a marked increase in absorbance at both 490 and 560 nm.

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