EFFECT OF SMOKING PROCESS ON SOLUBILITY AND ELECTROPHORETIC BEHAVIOR OF MEAT PROTEINS

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Abstract
SUMMARY: The solubility characteristics and starch gel electrophoretic properties of untreated, heated, and heated and smoked pork longissimus dorsi muscle samples were investigated. The percentages of the low ionic strength fraction, the sarcoplasmic and the soluble fibrillar protein nitrogen fractions decreased in the heated and heated and smoked samples when compared to the untreated samples. The myofibrillar protein nitrogen fraction increased in the heated samples and decreased in the heated and smoked samples. The stroma fraction from the untreated to the heated state remained almost constant, but increased considerably in the heated and smoked samples. Electrophoretic studies of the sarcoplasmic fraction indicated numerous changes in the heated and heated and smoked samples. The electropherograms of the heated and smoked samples from the Weber‐Edsall and meat‐urea extracts showed definite changes in protein components. These studies indicated that smoke definitely caused changes in protein solubility and the electrophoretic behavior of meat proteins.