Studies on Myoglobin

YASUI Tsutomu

doi:10.2508/chikusan.29.163

In order to investigate the state of cooked myoglobin which has beeen known as the main constituent of meat color in cooked cured meat, experiments on heat denaturation or coagulation of myoglobin were carried out by using cristallized metmyoglobin as a sample. From these experiments, the following facts were found out. (1) Myoglobin was hardly denatured in 1/10M NaOH in which hemoglobin was denatured. (2) When beat-coagulated myoglobin was dissolved in 1/10M NaOH solution and then neutralized, a native myoglobin-like substance, which showed photometrically the characteristics identical with those of native myoglobin, was obtained. The yields were about 80% after 5 minutes, and 40-50% after 30 minutes, heating at 100° in distilled water, 60-70% after 5 minutes, and 40-50% after 30 minutes, heating at 100° in 1/10M phosphate buffer (pH 7.0), and about 20% after 5 minutes, and 10-18% after 30 minutes, heating at 100° in 3% NaCl solution (3) Heat-coagulated nitric-oxide myoglobin dissolved in 1/10M NaOH solution showed a spectral curve similar to that of native myoglobin. Myoglobin derivatives dissolved in the same solution gave the same results. (4) Myoglobin recovered from heat-coagulated metmyoglobin could form various derivatives as native myoglobin could and the spectral characteristics of each derivative showed good agreement with those of native myoglobin. (5) From these results, it is supposed theat the heat-denaturation of myoglobin consists of two processes; that is, the reversible and the irreversible one.

Studies on Myoglobin

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