title: Enzymatic Hydrolysis Does Not Reduce the Biological Reactivity of Soybean Proteins for All Allergic Subjects.
abstract: Many soybean protein products are processed by enzymatic hydrolysis to attain desirable functional food properties or in some cases to reduce allergenicity. However, few studies have investigated the effects of enzymatic hydrolysis on the allergenicity of soybean products. In this study the allergenicity of soybean protein isolates (SPI) hydrolyzed by Alcalase, trypsin, chymotrypsin, bromelain, or papain was evaluated by IgE immunoblots using eight soybean-allergic patient sera. The biological relevance of IgE binding was evaluated by a functional assay using a humanized rat basophilic leukemia (hRBL) cell line and serum from one subject. Results indicated that hydrolysis of SPI by the enzymes did not reduce the allergenicity, and hydrolysis by chymotrypsin or bromelain has the potential to increase the allergenicity of SPI. Two-dimensional (2D) immunoblot and liquid chromatography-tandem mass spectrometry (LC-MS/MS) analysis of the chymotrypsin-hydrolyzed samples indicated fragments of β-conglycinin protein are responsible for the apparent higher allergenic potential of digested SPI.
authors.affiliation: Food Allergy Research and Resource Program, Food Innovation Center, University of Nebraska , 1901 North 21st Street, Lincoln, Nebraska 68588-6207, United States.
authors.forename: Rakhi
authors.initials: R
authors.lastname: Panda
authors.affiliation: Food Allergy Research and Resource Program, Food Innovation Center, University of Nebraska , 1901 North 21st Street, Lincoln, Nebraska 68588-6207, United States.
authors.forename: Afua O
authors.initials: AO
authors.lastname: Tetteh
authors.affiliation: Department of Biochemistry, Kuvempu University , Shimoga 577203, Karnataka, India.
authors.forename: Siddanakoppalu N
authors.initials: SN
authors.lastname: Pramod
authors.affiliation: Food Allergy Research and Resource Program, Food Innovation Center, University of Nebraska , 1901 North 21st Street, Lincoln, Nebraska 68588-6207, United States.
authors.forename: Richard E
authors.initials: RE
authors.lastname: Goodman
mesh_terms: D002918:Chymotrypsin / Q000737:chemistry; D005512:Food Hypersensitivity / Q000276:immunology*; D006801:Humans; D006868:Hydrolysis; D007073:Immunoglobulin E / Q000032:analysis / Q000276:immunology; D030262:Soybean Proteins / Q000737:chemistry* / Q000276:immunology; D013025:Glycine max / Q000737:chemistry* / Q000276:immunology; D013381:Subtilisins / Q000737:chemistry; D014357:Trypsin / Q000737:chemistry
chemical_list: D030262:Soybean Proteins; D007073:Immunoglobulin E; D013381:Subtilisins; D002918:Chymotrypsin; D014357:Trypsin
keywords: IgE binding; enzymatic hydrolysis; functional assay; soybean