The capacity of proteins to form aggregates has long been subjugated to create foods with diverse structural and textural distinctiveness. Soya storage proteins are extensively used in food as gelling agents as they can act as a surrounding substance for holding water, lipids and flavors, as well as for imparting desirable textural properties into products. Protein aggregation is a common problem associated with the protein products in the pharmaceutical and food industry. Protein aggregation is over and over again accompanied by the loss of activity of the product and in the case of therapeutic products can induce a toxic reaction. Protein aggregation can be triggered by heat, by definite chemicals used in the processing or may take place impulsively during storage.
Many models have been planned to explain the mechanism whereby proteins form heat-set gels. The sustaining facts for these models are, in some instances, light or of reduced quality, for the reason that the technological difficulties in working with aggregated proteins that are millions of daltons in size. In modern years our accepting of the nature of unprompted protein aggregation events has augmented significantly because of their consequence in the pathogenesis of conformational diseases, such as amyloidosis, Alzheimer's and the spongieform encephalopathies. (Walter, S. and Buchner, J. (2002)
Atomic force microscopy (AFM) is one of the methods that are been used with immense sensation in studying these aggregation processes. Scientists at the Institute of Food Research (IFR, Norwich Research Park, Colney, Norwich NR4 7UA, England, U.K.) have used AFM to follow the heat-induced arrangement of soluble aggregates of the soya globulin beta-conglycinin. Aggregates only begin forming once the protein is denatured and has a linear appearance. This indicates that the proteins stack in elongated cylinders. At high protein concentrations (1% w/v) the linear aggregates appear to form large macro aggregates, which may be the precursors of protein gel formation........
