Reducing the allergenicity of pea protein based on the enzyme action of alcalase
| Autor: | Na Sun, Libo Qi, Huapeng Ju, Jie Ding, Songyi Lin, Limin Zhong |
|---|---|
| Rok vydání: | 2021 |
| Předmět: |
0301 basic medicine
Enzyme-Linked Immunosorbent Assay Peptide Immunoglobulin E Cell Degranulation Hydrolysate Mice 03 medical and health sciences 0404 agricultural biotechnology Enzymatic hydrolysis Animals Amino Acid Sequence Subtilisins EC50 chemistry.chemical_classification Mice Inbred BALB C 030109 nutrition & dietetics biology Chemistry Hydrolysis Pea protein Hypoallergenic 04 agricultural and veterinary sciences General Medicine Allergens 040401 food science Ultrafiltration (renal) Biochemistry Immunoglobulin G biology.protein Female Pea Proteins Food Science |
| Zdroj: | Food & Function. 12:5940-5948 |
| ISSN: | 2042-650X 2042-6496 |
| Popis: | Enzymatic hydrolysis could be one of the crucial means to limit the allergenicity of allergens. The allergenicity of pea peptides was evaluated using indirect ELISA and RBL-2H3 cell assay, thereby obtaining hypoallergenic pea peptide sequences. Results indicated that pea protein-sensitized mice produced higher levels of total IgG1 and IgE antibodies than the mice in the control group (P < 0.05). Moreover, the allergenicity of hydrolysates decreased significantly after enzymolysis, and the allergenicity of ultrafiltration component F1 and purified component F1–2 was significantly lower than that of other isolated and purified components (P < 0.05). Furthermore, ADLYNPR identified from F1–2 had lower binding capacity to specific IgE and IgG1 and lower degree of cell degranulation with a higher EC50 value of 6.63 ng mL−1, which was about 36.83 times that of pea protein (P < 0.05). Based on the above results, ADLYNPR might be a potential source of hypoallergenic peptides. |
| Databáze: | OpenAIRE |
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