Functional properties of proteins in foods

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Abstract
The measurement of functionality of protein food ingredients has developed somewhat haphazardly, probably due to the wide range of proteins used as ingredients and the diversity of foods. Studies of the physiochemical properties of proteins should enable prediction of a proteins response to process environments and prove more fruitful than many of the empirical measurements of functionality. The effects of pH, salt type and concentration on the phase behaviour of the oilseed globulin and arachin, demonstrates the complexity of protein solubility and the inadequacies of simple tests that have arisen. Studies of the effects of salts and conditioning on meat fibres, coupled with measurement of the location of water in pellets from water holding tests enable the latter to be applied with increased confidence. Comparison of the endothermic transitions observed on heating with the development of storage and loss moduli allow the contributions of domains of skeletal muscle myosin to gel structure to be investigated.

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