Abstract

The enzymatic hydrolysis of soybean protein isolate (SPI) was investigated using commercially available Bacillus sp. proteases for reduction of soybean allergenicity. An alkaline protease, Proleather FG-F, was found to be useful for degradation of the major soybean allergens (Gly m Bd 30 K, Gly m Bd 28 K and α-subunit of β-conglycinin), whereas all proteases tested so far preferentially degrade β-conglycinin in native SPI at 70°C. The hydrolysate prepared using Proleather FG-F retained gel-forming ability, while the reactivity with IgE in serum of soybean-sensitive patients was markedly reduced. Thus, this hydrolysate may be especially useful as an ingredient in hypoallergenic foods.

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