Proteomic analysis ofLupinus angustifolius(var. Zeus and Bojar) andLupinus luteus(var. Lord and Parys) seed proteins and their hydrolysates
| Autor: | Magdalena Montowska, Jaroslaw Czubinski, Eleonora Lampart-Szczapa, Edward Pospiech |
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| Rok vydání: | 2017 |
| Předmět: |
0301 basic medicine
Gel electrophoresis chemistry.chemical_classification 030109 nutrition & dietetics Nutrition and Dietetics biology 04 agricultural and veterinary sciences biology.organism_classification Trypsin 040401 food science Hydrolysate 03 medical and health sciences Hydrolysis Lupinus angustifolius 0404 agricultural biotechnology Enzyme chemistry Biochemistry Enzymatic hydrolysis medicine Digestion Agronomy and Crop Science Food Science Biotechnology medicine.drug |
| Zdroj: | Journal of the Science of Food and Agriculture. 97:5423-5430 |
| ISSN: | 0022-5142 |
| DOI: | 10.1002/jsfa.8436 |
| Popis: | BACKGROUND Proteins enzymatic digestion is a very complex process, during which some components are degraded, while others remain in an unchanged form. Moreover, the enzymatic hydrolysis is one of the most popular methods used to reduce the allergenicity of food proteins. In this study, the efficiency of enzymatic hydrolysis of lupin seeds proteins was assessed by proteomic analysis performed by two-dimensional gel electrophoresis (2-DE) coupled with mass spectrometry identification. Two digestion systems were used, namely, oriented digestion carried out by trypsin and the model in vitro digestion mimicking conditions present in the gastrointestinal tract. RESULTS The comparisons of 2-DE maps of proteins isolated form different lupin seeds species revealed that the differences in proteins expression were observed mainly in the central parts of gels, i.e., in the molecular weight range from 20 to 70 kDa, and the pH range 5–7. A total number of 27 differentially expressed proteins spots were successfully identified by mass spectrometry analysis. An important reduction in the number of proteins spots on 2-DE maps was observed when trypsin, and the in vitro digestion model were applied. The protein spot insensitive to digestion in both hydrolysis systems was identified as β-conglutin. CONCLUSIONS The results provide insight into the nature of the digestion process that may take place after lupin seed proteins intake and highlight the important fact that some of the proteins are insensitive to digestive enzymes activity. Moreover, evaluation of digestion activity of trypsin towards lupin seed proteins may be used for the development of specific processes of hypoallergenic food production. |
| Databáze: | OpenAIRE |
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