Abstract
Surface proteins, both soluble and insoluble, extracted from chicken breast and thigh meat chunks with water or 3% NaCl solution were studied. Soluble proteins were separated by an ammonium sulfate gradient precipitation method, quantified, and characterized using sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The quantities of both soluble and insoluble proteins from chicken breast meat chunk surfaces were higher than those of the thigh meat. The 3% NaCl solution extracted more soluble proteins, particularly those of molecular weight greater than 66,000 daltons, than that extracted by plain water. Most of these higher molecular weight proteins were satisfactorily precipitated by the addition of 20% ammonium sulfate. The amount of extracted water and salt soluble proteins from blended meat chunks were 3.00 and 4.75 times higher than those from washed suspensions, respectively. An increase in mixing time also enhanced the exudation of proteins to the meat surfaces.
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