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 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.
Sormus de Castro Pinto
Silvia Elaine
SE
Department of Biological Sciences, School of Pharmaceutical Sciences, Sao Paulo State UniversityUNESP, Araraquara, SP, Brazil.
Neves
Valdir Augusto
VA
Machado de Medeiros
Beatriz Maria
BM
D052179:Antigens, Plant / Q000737:chemistry / Q000276:immunology* / Q000378:metabolism; D029863:Cicer / Q000737:chemistry*; D006868:Hydrolysis; D027806:Lens Plant / Q000737:chemistry*; D031297:Lupinus / Q000737:chemistry*; D010434:Pepsin A / Q000378:metabolism; D010940:Plant Proteins / Q000276:immunology* / Q000378:metabolism*; D012639:Seeds / Q000737:chemistry; D014357:Trypsin / Q000378:metabolism
D052179:Antigens, Plant; D010940:Plant Proteins; D014357:Trypsin; D010434:Pepsin A