Enzymatic Hydrolysis of Sweet Lupin, Chickpea, and Lentil 11S Globulins Decreases their Antigenic Activity

We investigated the effects of treatments with the enzymes pepsin and trypsin on the in vitro immunological reactivity of the major globulins found in the seeds of sweet lupin, chickpea, and lentil. Polyclonal major globulin-specific antiserum was obtained by immunization of rabbits with a solution...

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Bibliographic Details
Published in:	Journal of agricultural and food chemistry Vol. 57; no. 3; pp. 1070 - 1075
Main Authors:	Sormus de Castro Pinto, Silvia Elaine, Neves, Valdir Augusto, Machado de Medeiros, Beatriz Maria
Format:	Journal Article
Language:	English
Published:	Washington, DC American Chemical Society 11-02-2009
Subjects:	allergenicity allergens Antigens, Plant - chemistry Antigens, Plant - immunology Antigens, Plant - metabolism Biological and medical sciences chickpeas Cicer - chemistry Confectionery products and chocolate industries, honey enzymatic hydrolysis enzymatic treatment food allergies Food Chemistry/Biochemistry Food industries Fundamental and applied biological sciences. Psychology globulins Hydrolysis Lens Plant - chemistry lentils Lupinus - chemistry Lupinus albus pepsin Pepsin A - metabolism Plant Proteins - immunology Plant Proteins - metabolism proteolysis seeds Seeds - chemistry trypsin Trypsin - metabolism Sweet lupin lentil antigenic activity enzymatic hydrolysis chickpea Hydrolysis Lentil Decrease Lupin Sweets Confectionery product Globulin Enzymatic reaction
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Summary:	We investigated the effects of treatments with the enzymes pepsin and trypsin on the in vitro immunological reactivity of the major globulins found in the seeds of sweet lupin, chickpea, and lentil. Polyclonal major globulin-specific antiserum was obtained by immunization of rabbits with a solution of the 11S globulin of each legume. The globulins were hydrolyzed with pepsin and trypsin for 1, 5, 15, and 30 min. The native globulins and their hydrolysates were analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and immunoblotting to identify the polypeptide bands with antigenic activity, and the hypoantigenicity of the hydrolysates was analyzed by enzyme-linked immunosorbent assay. Our results show that enzymatic treatment of the major storage protein (11S globulin) of sweet lupin, chickpea, and lentil with pepsin or trypsin lead to the formation of large amounts of short peptides and free amino acids that do not allow antibody binding, resulting in a weakened immunoreactivity.
Bibliography:	http://dx.doi.org/10.1021/jf803108c ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23
ISSN:	0021-8561 1520-5118
DOI:	10.1021/jf803108c