145703 20260217205537.0 doi 10.1039/D4FO03052D sideral 140544 ART-2024-140544 eng Tobajas, Ana Pilar Universidad de Zaragoza (orcid)0000-0002-2646-5733 Enzymatic treatment to decrease the allergenicity of Pru p 3 from peach 2024 Access copy available to the general public Unrestricted Pru p 3, a member of the Lipid Transfer Protein family, is considered a major allergen from peach and it often induces serious allergic reactions in peach allergic individuals. The high resistance of Pru p 3 to processing treatments and to digestion or enzymatic hydrolysis is probably the cause of the severity of this fruit allergy. The aim of this study was to determine the effect of treatment with a high number of proteases from different origins (vegetal, animal and microbial) on the degradation and allergenicity of Pru p 3. To perform this study, Pru p 3 was previously isolated using cation exchange chromatography and ultrafiltration, and the purified protein was incubated with proteases under different conditions. Results showed that only two of fifteen proteases assayed were able to degrade efficiently the protein at acid pH, as determined by SDS-PAGE. These two commercial acid proteases, derived from Aspergillus niger, decreased more than 95% the immunoreactivity of Pru p 3 by ELISA using specific rabbit IgG, giving peptides lower than 3.2 kDa as determined by MALDI-TOF mass spectrometry. The hydrolysates obtained showed a decrease in reactivity of IgE respect to untreated Pru p 3 higher than 70% using three pools of sera from peach allergic individuals. Furthermore, when hydrolysates were tested by the prick test, more than 90% of peach allergic patients significantly decreased the average size of the wheal between 72% and 85%. Results suggest that acid protease from Aspergillus niger could be used to obtain novel hypoallergenic products more tolerable for peach sensitized individuals. info:eu-repo/grantAgreement/ES/DGA/A20-23R info:eu-repo/semantics/openAccess by-nc https://creativecommons.org/licenses/by-nc/4.0/deed.es 5.4 2024 FOOD SCIENCE & TECHNOLOGY 38 / 182 = 0.209 2024 Q1 T1 BIOCHEMISTRY & MOLECULAR BIOLOGY 61 / 320 = 0.191 2024 Q1 T1 1.194 2024 Medicine (miscellaneous) 2024 Q1 Food Science 2024 Q1 10.5 2024 info:eu-repo/semantics/article info:eu-repo/semantics/acceptedVersion Agulló-García, Ana Cubero, Jose Luis Universidad de Zaragoza (orcid)0000-0002-5232-685X Colás Sanz, Carlos Universidad de Zaragoza (orcid)0000-0001-8959-6784 Civera, Alba (orcid)0000-0001-7719-6388 Esteban, Clara Universidad de Zaragoza (orcid)0009-0005-0336-7582 Sánchez, L. Universidad de Zaragoza (orcid)0000-0001-5964-823X Pérez, M. D. Universidad de Zaragoza (orcid)0000-0003-2555-8425 1007 610 Universidad de Zaragoza Dpto. Medicina, Psiqu. y Derm. Area Medicina 1002 060 Universidad de Zaragoza Dpto. Bioq.Biolog.Mol. Celular Área Bioquímica y Biolog.Mole. 2008 780 Universidad de Zaragoza Dpto. Produc.Animal Cienc.Ali. Área Tecnología de Alimentos (2024), [11 pp.] FOOD & FUNCTION FOOD & FUNCTION 2042-6496 2323289 http://zaguan.unizar.es/record/145703/files/texto_completo.pdf Postprint 1504525 http://zaguan.unizar.es/record/145703/files/texto_completo.jpg?subformat=icon icon Postprint oai:zaguan.unizar.es:145703 articulos driver 2026-02-17-20:34:55 ARTICLE