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Extrusion Chemistry of Wheat Flour Proteins: II. Sulfhydryl-Disulfide Content and Protein Structural Changes

¹Department of Food Science, Rutgers University, 65 Dudley Rd., New Brunswick, NJ 08901-8520. ²Current address: Campbell Soup Company, Campbell Place, Camden, NJ 08103. ³Corresponding author. Phone: 732/932-9611, ext. 233; Fax: 609/497-9313; E-mail: schaich@aesop.rutgers.edu.

Effects of twin-screw extrusion conditions on wheat flour proteins were studied, using a two-level fractional factorial experimental design (11 and 14% protein content, 160 and 185°C, 16 and 20% moisture, 300 and 500 rpm screw speed, mass flow rate of 225 and 400 g/min). Total protein detectable by solid-phase bicinchoninic acid assay decreased slightly after extrusion, with greatest protein loss at 16% moisture and 160°C. Sulfhydryl content of both flours increased after extrusion at 185°C and 16% moisture with moderate specific mechanical energy (SME ≈ 400–600 kJ/kg) or 160°C and 16% moisture with high SME (SME > 1,000 kJ/kg). Disulfide bonds increased under comparable conditions but with moderate shear (SME = 510–540 kJ/kg). At 20% moisture and either temperature, sulfhydryl and total thiol contents decreased without corresponding increases in disulfides. Reversed-phase HPLC indicated gliadins were the fractions most affected by extrusion; high molecular weight glutenin subunits also were affected. Changes in gliadins were extensive at 185°C and 16% moisture and were minimal at 160°C and 20% moisture. SDS-PAGE confirmed the disappearance of protein bands and appearance of new material at low and high molecular weights, presumably resulting from polypeptide fragmentation followed by random radical recombination. Both protein fragmentation and cross-linking appeared to involve free radicals.