Hydrophobic and Electrostatic Interactions on Extrusion of Protein Isolates

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Abstract
Lung protein isolates previously defatted by solvents of increasing polarity were extruded. Water monolayer values of these isolates, calculated from water vapor isotherms, showed a maximum when solvents of intermediate polarity were used. Shear resistance of the extruded products presented a similar behavior, with maximum values attained when the same solvents were employed to defat the isolates prior to extrusion. Phospholipid percentage in lipid fraction of the solvent extracts showed that minimum phospholipids were removed from the isolates when these solvents were used. The results suggested that the presence of phospholipid in the isolates after defatting could be important in improving the extrusion of these systems. Hydrophobic and electrostatic interactions between the macromolecules involved seemed therefore, to be relevant for the final texture obtained by extrusion.