Allergenicity of roasted peanuts treated with a non-human digestive protease. (March 2015)

• Record Type: Journal Article
• Authors: Yu, Jianmei; Hernandez, Michelle; Li, Hao; Goktepe, Ipek; Robinette, Carole; Auerbach, Amy; Peden, David; Ahmedna, Mohamed
• Is Part Of: Food research international. Volume 69(2015)
• Page Start: 341
• Page End: 347
• Publication Date: 2015-03
• Subjects: Peanut allergens -- Ara h 1 -- Ara h 2 -- Alcalase -- Enzyme treatment -- IgE-binding -- Skin prick test; Food -- Analysis -- Periodicals; Food industry and trade -- Periodicals; Food industry and trade -- Canada -- Periodicals; Food Technology -- Periodicals; Food -- Periodicals; Food-Processing Industry -- Periodicals; Aliments -- Industrie et commerce -- Périodiques; Aliments -- Industrie et commerce -- Canada -- Périodiques; Aliments -- Recherche -- Périodiques; Food industry and trade; Canada; Periodicals; Electronic journals; 664.005
• DOI: 10.1016/j.foodres.2015.01.007
• Languages: English
• ISSNs: 0963-9969

Abstract

Abstract: Peanut allergy is a severe and lifelong type of food allergy triggered by allergenic proteins and peptides in peanuts. This study investigated the effects of ultrasound-assisted alcalase treatment on the concentrations of major allergenic proteins (Ara h 1 and Ara h 2) in roasted peanut kernels and the allergenicity of treated peanut extracts. Peanut kernels were sonicated for 1 h in buffer solution, incubated with different amount of alcalase for various time, then vacuum dried. The variations of Ara h 1 and Ara h 2 contents in soluble and insoluble portions of peanuts treatments were evaluated by sandwich ELISA and SDS-PAGE, respectively. The in vitro IgE-binding capacity of treated peanut extracts was determined by a competitive inhibition ELISA using pooled plasma of 10 peanut allergic patients. Samples with lower in vitro IgE-binding were used for human skin prick tests (SPTs) in peanut allergic individuals. Results indicate that alcalase digestion of sonicated peanuts significantly increased protein solubility while decreasing Ara h 1 and Ara h 2 concentrations in both soluble and insoluble portions of peanuts relative to untreated peanuts. The maximum reductions of Ara h 1 and Ara h 2 levels were obtained following 3 hour digestion with alcalase at concentrations of 4.54 and 6.05 U/100 g. Samples obtained under these conditions showed the lowest in vitro IgE-binding and caused the least allergic response in human SPTs. The current study suggests that the allergenic potential of peanuts could be reduced by postharvest processing such as ultrasound-assisted enzymatic treatment of peanuts kernels. Highlights: Peanut allergy is a severe food allergy and difficult to outgrow. Peanut allergy is caused by allergenic proteins. Alcalase effectively reduced the allergenic protein content in this study. IgE-binding tests showed reduced in vitro allergenicity of alcalase treated peanuts. The in vivo skin prick test results agreed well with that of in vitro tests.