Effects of twin-screw extrusion of peanut flour on in vitro digestion of potentially allergenic peanut proteins.

Partially defatted peanut flour was processed in a twin-screw extruder. Resulting extrudates were dried, ground, and incubated with simulated gastric fluid for various time periods. Soluble protein content of the resulting digesta was measured after 10% trichloroacetic acid treatment to evaluate the digestibility. In vitro digestion using pepsin increased the solubility of peanut protein in 10% trichloroacetic acid solution from 2 to 6% to 65 to 75%. Four strong IgE-binding subunits (65, 22, 17, and 14 kDa) were found with immunoblotting in peanut proteins extracted from unextruded peanut flour; no IgE-binding bands were observed in extrudates. The 65-kDa (putative Ara h 1) subunit was insolubilized during extrusion, and its IgE-binding property was susceptible to in vitro digestion. Following extrusion cooking, no IgE-binding bands were detected by immunoblotting, including the strongly IgE-binding 14-kDa fraction, a strong IgE-binding band from native peanut protein that is stable in pepsin. The 22- and 17-kDa (putative Ara h 2) subunits retained a small amount of IgE-binding potential and became susceptible to pepsin hydrolysis after extrusion.