The soy protein-galactomannan conjugate prepared by the Maillard reaction removed the allergenicity of the 34 kDa protein which is frequently recognized by the IgE antibody in the sera of soybean-sensitive patients as a major allergen. Monitoring of polyclonal antibody titers by an indirect enzyme-linked immunosorbent assay and immunoblotting of rabbit sera, monoclonal antibody, and human allergic sera showed that soy protein-galactomannan conjugation was more effective in reducing the allergenicity of the soy protein than transglutaminase treatments and/or chymotrypsin. The soy protein-galactomannan conjugate was highly soluble at all pHs, while untreated soy protein was sparingly soluble at pH 4-6. Heat stability and emulsifying properties were greatly improved by conjugation with galactomannan.

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Insoluble gluten was solubilized by proteases (chymotrypsin, papain, Pronase, and pepsin) or mild acid (0.05 N HCl) treatments. The digests and hydrolysate are turbid, but after transglutaminase (TGase) treatment, the turbid mixture was converted to a transparent solution, which was found to be soluble at a wide range of pH. The hydrophobicity was greatly decreased after polymerization by TGase. SDS−PAGE patterns of the digests and hydrolysate with and without TGase treatment showed that the digests (except Pronase) were polymerized by TGase. The emulsifying properties of the polymerized peptides were greatly improved compared to those of the protease digests and acid hydrolysates. The foaming properties of the polymerized digests were also greatly improved. The digests and hydrolysate were found to have a bitter taste, but after polymerization the bitterness completely disappeared. Keywords: Functional properties; gluten; protease; hydrolysis; microbial transglutaminase

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