The structure and stability analysis of the pea seed legumin glycosylated by oligochitosan
- PMID: 32767558
- DOI: 10.1002/jsfa.10715
The structure and stability analysis of the pea seed legumin glycosylated by oligochitosan
Abstract
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, and in vitro digestive 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, and in vitro digestive stability. This study will facilitate the legumin functionalization by the glycosylation approach to fabricate protein-oligochitosan complex for potential food and nutritional applications. © 2020 Society of Chemical Industry.
Keywords: glycosylation; legumin; oligochitosan; stability.
© 2020 Society of Chemical Industry.
Similar articles
-
Structure and property modification of an oligochitosan-glycosylated and crosslinked soybean protein generated by microbial transglutaminase.Food Chem. 2014 Nov 15;163:114-9. doi: 10.1016/j.foodchem.2014.04.089. Epub 2014 May 4. Food Chem. 2014. PMID: 24912705
-
Composition, physicochemical properties of pea protein and its application in functional foods.Crit Rev Food Sci Nutr. 2020;60(15):2593-2605. doi: 10.1080/10408398.2019.1651248. Epub 2019 Aug 20. Crit Rev Food Sci Nutr. 2020. PMID: 31429319 Review.
-
Proteomic analysis of albumin and globulin fractions of pea (Pisum sativum L.) seeds.Acta Sci Pol Technol Aliment. 2014 Apr-Jun;13(2):181-90. doi: 10.17306/j.afs.2014.2.7. Acta Sci Pol Technol Aliment. 2014. PMID: 24876313
-
Modified properties of a glycated and cross-linked soy protein isolate by transglutaminase and an oligochitosan of 5 kDa.J Sci Food Agric. 2017 Jan;97(1):58-64. doi: 10.1002/jsfa.7682. Epub 2016 Mar 23. J Sci Food Agric. 2017. PMID: 26916835
-
Pea protein composition, functionality, modification, and food applications: A review.Adv Food Nutr Res. 2022;101:71-127. doi: 10.1016/bs.afnr.2022.02.002. Epub 2022 Mar 17. Adv Food Nutr Res. 2022. PMID: 35940709 Review.
Cited by
-
The Hydrolysis of Pigment-Protein Phycoerythrin by Bromelain Enhances the Color Stability.Foods. 2023 Jun 30;12(13):2574. doi: 10.3390/foods12132574. Foods. 2023. PMID: 37444311 Free PMC article.
References
REFERENCES
-
- Barilli E, Sillero JC, Prats E and Rubiales D, Resistance to rusts (Uromyces pisi and U. viciae-fabae) in pea. Czech J Genet Plant 50:135-143 (2014).
-
- Schwenke KD, Zirwer D, Cast K, Gornitz E, Linow KJ and Gueguen J, Changes of the oligomeric structure of legumin from pea (Pisum sativum L.) after succinylation. Eur J Biochem 194:621-627 (1990).
-
- Lycett GW, Croy RRD, Shirsat AH and Boulter D, The complete nucleotide sequence of a legumin gene from pea (Pisum sativum L.). Nucleic Acids Res 12:4493-4496 (1984).
-
- Mession JL, Sok N, Assifaoui A and Saurel R, Thermal denaturation of pea globulins (Pisum sativum L.)-molecular interactions leading to heat-induced protein aggregation. J Agric Food Chem 61:1196-1204 (2013).
-
- Kimura A, Fukuda T, Zhang M, Motoyama S, Maruyama N and Utsumi S, Comparison of physicochemical properties of 7S and 11S globulins from pea, fava bean, cowpea, and French bean with those of soybean-French bean 7S globulin exhibits excellent properties. J Agric Food Chem 56:10273-10279 (2008).
MeSH terms
Substances
Grants and funding
- 31972067/National Natural Science Foundation of China
- 19JCTPJC50900/Tianjin Technical Expert Project, China
- 19YFSLQY00100/Science and Technology Planning Project of Tianjin City
- the fund of the Beijing Engineering and Technology Research Center of Food Additives, Beijing Technology & Business University (BTBU)
LinkOut - more resources
Full Text Sources