| Autor: |
Chen S; Food Allergy Research and Resource Program, Department of Food Science and Technology, University of Nebraska-Lincoln, Lincoln, Nebraska 68588, United States., Downs ML; Food Allergy Research and Resource Program, Department of Food Science and Technology, University of Nebraska-Lincoln, Lincoln, Nebraska 68588, United States. |
| Jazyk: |
angličtina |
| Zdroj: |
Journal of proteome research [J Proteome Res] 2022 Jul 01; Vol. 21 (7), pp. 1694-1706. Date of Electronic Publication: 2022 Jun 03. |
| DOI: |
10.1021/acs.jproteome.2c00095 |
| Abstrakt: |
Cashews are one of the most prevalent causes of tree nut allergies. However, the cashew proteome is far from complete, which limits the quality of peptide identification in mass spectrometric analyses. In this study, bioinformatics tools were utilized to construct a customized cashew protein database and improve sequence quality for proteins of interest, based on a publicly available cashew genome database. As a result, two additional isoforms for cashew 2S albumins and five other isoforms for cashew 11S proteins were identified, along with several other potential allergens. Using the optimized protein database, the protein profiles of cashew nuts subjected to different oil-roasting conditions (139 and 166 °C for 2-10 min) were analyzed using discovery LC-MS/MS analysis. The results showed that the cashew 2S protein is most heat-stable, followed by 11S and 7S proteins, though protein isoforms might be affected differently. Preliminary target peptide selection indicated that out of the 29 potential targets, 18 peptides were derived from the newly developed database. In the evaluation of thermal processing effects on cashew proteins, several Maillard reaction adducts were also identified. The cashew protein database developed in this study allows for comprehensive analyses of cashew proteins and development of high-quality allergen detection methods. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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