Allergenicity reduction of cow's milk proteins using latex peptidases

OLIVEIRA JOAO; CANDREVA ANGELA; RIZZO GASTON; RAMOS MARCIO; OLIVEIRA JEFFERSON; OLIVEIRA HERMOGENES; ARY MARIA; DOCENA GUILLERMO H.; FREITAS CLEVERSON

FOOD CHEMISTRY

ELSEVIER SCI LTD

Lugar: Amsterdam; Año: 2019

0308-8146

The present study evaluated four laticifer fluids as new source of peptidases able to hydrolyze cow?s milk proteins. 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, confirmed by a significant reduction in the residual antigenicity. Casein hydrolysis by Plumeria rubra latex peptidases (PrLP) was negligible. On the other hand, whey proteins were more resistant to proteolysis by latex peptidases. However, the heat pretreatment of the whey proteins enhanced the degree of hydrolysis and reduced the residual antigenicity of the hydrolysates. The in vivo assays showed that the cow?s milk proteins hydrolyzed by CgLP and CapLP did not exhibit immune reactions in mice allergenic to cow?s milk, similar to a commercial partially hydrolyzed formula. Thus, these peptidases are promising enzymes to develop novel hypoallergenic formulas for children with milk allergy.