期刊
JOURNAL OF THE SCIENCE OF FOOD AND AGRICULTURE
卷 101, 期 3, 页码 1065-1075出版社
WILEY
DOI: 10.1002/jsfa.10715
关键词
legumin; oligochitosan; glycosylation; stability
资金
- National Natural Science Foundation of China [31972067]
- Tianjin Technical Expert Project, China [19JCTPJC50900]
- Science and Technology Planning Project of Tianjin City [19YFSLQY00100]
- Beijing Engineering and Technology Research Center of Food Additives, Beijing Technology & Business University (BTBU)
Oligochitosan glycosylation can alter the structure of pea legumin and enhance its emulsification stability, thermal stability, and in vitro digestive stability. This study demonstrates the potential for functionalizing legumin through glycosylation to create protein-oligochitosan complexes for food and nutritional applications.
BACKGROUND The functionality of pea proteins is relatively weak relative to that of soybean proteins, which limits the application of pea proteins in food and nutritional applications. Glycosylation is a promising approach to influence the protein structure and in turn change the functional properties of pea proteins. RESULTS In this study, the effect of transglutaminase-induced oligochitosan glycosylation on the structural and functional properties of pea seed legumin was studied. Different oligochitosan-modified legumin complexes (OLCs) were prepared by applying different molar ratios of legumin to oligochitosan (1:1 to 1:4) induced by transglutaminase (10 U g(-1)protein). Results of sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), glucosamine, and free amino analysis showed that the legumin could be covalently bonded with the oligochitosan and were influenced by the applying dose of the oligochitosan. Infrared spectroscopy, fluorescence, and scanning electron microscopy analysis indicated that the structure of the different OLC samples could be changed to different extents. Moreover, although the emulsifying activity decreased, the emulsification stability, thermal stability, andin vitrodigestive stability of the OLCs were remarkably improved relative to that of the untreated legumin. CONCLUSION Oligochitosan glycosylation could change the structure of the legumin and consequently improve its emulsification stability, thermal stability, andin vitrodigestive stability. This study will facilitate the legumin functionalization by the glycosylation approach to fabricate protein-oligochitosan complex for potential food and nutritional applications. (c) 2020 Society of Chemical Industry
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