The effect of storage on protein solubility and heat-induced gelation properties of chicken hen breast and leg myofibrils was investigated. Myofibrils suspended in 0.6M NaC1, pH 6.0, showed increasing protein solubility, viscosity, gel strength and water holding capacity with storage at 4°C. However, the effect of storage was most dramatic only during the initial 10 hr for all of the parameters studied. The relative distribution of the proteins comprising the salt soluble protein (SSP) extract changed during storage. Although storage had little effect on breast SSP, it was detrimental to leg SSP gelation. Breast myofibril suspensions, for all storage times, contained a greater amount of SSP and had better gelation properties than leg myofibril suspensions.

Pea protein isolates were acylated with succinic and acetic anhydride at 1.0, 3.0, and 5.0 mmol anhydride/g protein. The chemically modified isolates showed increased emulsifying capacity, emulsion stability, foam capacity and stability, and water adsorption compared to untreated pea protein isolate. In general, the greater the extent of acylation, the greater the improvement in emulsification properties compared to the untreated protein isolate; however, improvement at greater than 3.0 mmol anhydride/g protein was slight, Acetylation at 3 mmol/g increased foam capacity to the greatest extent. Water adsorption was enhanced to the greatest extent in protein isolates acetylated at 5 mmol/g. Acylation lowered the isoelectric point of protein isolates compared to untreated isolate, In vitro enzyme hydrolysis of the protein isolates, as determined by a multienzyme system of trypsin, chymotrypsin and peptidase, was not impaired by acylation.

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Purified chicken myofibrils were suspended in 0.6M NaCl at various pH values to study gelation properties of the myofibrils. Postrigor breast myofibrils showed a greater protein extractability and gel strength than prerigor breast myofibrils, but the reverse was found for leg myofibrils. Salt-soluble protein was least extractable at pH 5.50 for both breast and leg myofibrils. The pH for optimum gelation, indicated bv increased nenetration force. was 6.00 for breast and 5.50 for leg myofibrils. Heiting at l"C/min f;om 20 to 70°C produced stronger breast but weaker leg myofibril gels than isothermal heating at 70°C for 20 min. Muscle rigor state showed a greater effect on protein extractability and gel strength for breast myofibrils than for leg myofibrils.

Mixed globulins (MG) were extracted from ground dry peas (Pisum sntivum, B-160) with 0.5M NaCl, 50 mM potassium phosphate, pH 7.2, and isolated by precipitation at pH 4.5. Crude vicilin and legumin were fractionated from the MG by dialysis against 0.2M NaCl, pH 4.8, and centrifugation, then further purified using DEAE-cellulose chromatography. Conditions for maximum gel hardness of heat induced MG gel, as determined with an Instron Universal Testing Machine, were heating for 20 min at pH 7.1 at 87°C. Purified vicilin, but not legumin, formed heat induced gels. The relationship was linear between protein (globulin) concentration and log gel hardness. At all protein concentrations studied, as proportion of legumin decreased, gel hardness increased.