Proteomic analysis of Lupinus angustifolius (var. Zeus and Bojar) and Lupinus luteus (var. Lord and Parys) seed proteins and their hydrolysates

• Published in: Journal of the science of food and agriculture Vol. 97; no. 15; pp. 5423 - 5430
• Main Authors: Czubinski, Jaroslaw, Montowska, Magdalena, Pospiech, Edward, Lampart‐Szczapa, Eleonora
• Format: Journal Article
• Language: English
• Published: Chichester, UK John Wiley & Sons, Ltd 01.12.2017; John Wiley and Sons, Limited
• Subjects: Allergenicity; Allergens - chemistry; Allergens - immunology; Digestion; Digestive system; Electrophoresis, Gel, Two-Dimensional; Enzymatic activity; Enzyme activity; Food allergies; Food production; Gastrointestinal tract; Gel electrophoresis; Gels; Hydrolysates; Hydrolysis; in vitro digestion; lupin seeds; Lupinus - chemistry; Lupinus - immunology; Mass Spectrometry; Mass spectroscopy; Mimicry; Molecular weight; pH effects; Plant Proteins - chemistry; Plant Proteins - immunology; Protein Hydrolysates - chemistry; Protein Hydrolysates - immunology; Proteins; proteins hydrolysis; Proteomics; Scientific imaging; Seeds - chemistry; Seeds - immunology; Spectroscopy; Spots; storage proteins; Trypsin; Two dimensional analysis; two‐dimensional electrophoresis; proteins hydrolysis; storage proteins; two-dimensional electrophoresis; lupin seeds; in vitro digestion
• ISSN: 0022-5142; 1097-0010
• DOI: 10.1002/jsfa.8436

BACKGROUND Proteins enzymatic digestion is a very complex process, during which some components are degraded, whereas others remain in an unchanged form. Moreover, enzymatic hydrolysis is one of the most popular methods used to reduce the allergenicity of food proteins. In the present study, the efficiency of enzymatic hydrolysis of lupin seed proteins was assessed by proteomic analysis as performed by two‐dimensional gel electrophoresis (2‐DE) coupled with mass spectrometry identification. Two digestion systems were used: oriented digestion carried out by trypsin and model in vitro digestion mimicking the conditions present in the gastrointestinal tract. RESULTS The comparisons of 2‐DE maps of proteins isolated form different lupin seed 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). In total, 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 of the present study provide insight into the nature of the digestion process that may take place after lupin seed protein intake and highlight the important fact that some of the proteins are insensitive to digestive enzyme activity. Moreover, evaluation of digestion activity of trypsin towards lupin seed proteins may be used for the development of specific processes with respect to hypoallergenic food production. © 2017 Society of Chemical Industry