Allergenicity reduction of cow’s milk proteins using latex peptidases

• Autores: Oliveira, João P.B.; Candreva, Ángela María; Rizzo, Gastón; Ramos, Márcio V.; Oliveira, Jefferson S.; Oliveira, Hermógenes D.; Ary, Maria B.; Docena, Guillermo; Freitas, Cleverson D.T.
• Año de publicación: 2019
• Idioma: inglés
• Tipo de recurso: artículo
• Materia: Ciencias Químicas; Allergy; Laticifer; Protein; Protease
• Institución: Comisión de Investigaciones Científicas de la Provincia de Buenos Aires

The present study evaluated four laticifer fluids as a novel source of peptidases capable of hydrolyzing proteins in cow’s milk. The latex peptidases from Calotropis procera (CpLP), Cryptostegia grandiflora (CgLP), and Carica papaya (CapLP) were able to perform total hydrolysis of caseins after 30 min at pH 6.5, as confirmed by a significant reduction in the residual antigenicity. Casein hydrolysis by Plumeria rubra latex peptidases (PrLP) was negligible. Moreover, whey proteins were more resistant to proteolysis by latex peptidases; however, heat pretreatment of the whey proteins enhanced the degree of hydrolysis and reduced the residual antigenicity of the hydrolysates. The in vivo assays show that the cow’s milk proteins hydrolysed by CgLP and CapLP exhibited no immune reactions in mice allergic to cow’s milk, similar to a commercial partially hydrolysed formula. Thus, these peptidases are promising enzymes for the development of novel hypoallergenic formulas for children with a milk allergy.