Skip to content
2000
image of Evaluation of Functional Properties and the Lipase Inhibitory Activity of Proteins from Amaranthus cruentus Seeds

Abstract

Aims / Background

Obesity is characterized by excessive body fat and is a chronic and complex disease. The medications used to date for the treatment of obesity have exhibited various side effects. Thus, new substances must be sought from alternative sources as anti-obesity drugs. Recently, there has been increased interest in the study of bioactive peptides generated from plant proteins for functional food development. Plant proteins have exhibited pancreatic lipase inhibitory activity and can be potentially studied as sources of anti-obesity drugs for long-term use. seeds are very nutritious, with high protein content and medicinal properties. Hence, this study focuses on pancreatic lipase inhibitory activity and functional properties of Amaranthus cruentus seed protein isolates.

Materials and Methods

Proteins were isolated using conventional and thermal isoelectric precipitation methods. The protein's ability to inhibit lipases was assessed using both synthetic and natural substrates. The functional properties, such as nitrogen solubility, foaming test, emulsification test, and water and oil holding abilities, were evaluated. The protein isolates were characterized by SDS-PAGE and DSC. Cell line studies were performed on 3T3-L1 cell lines to determine the cytotoxicity and anti-adipogenic activity of protein isolates.

Results

Proteins 1, 2, 3, and 4 were found to have high protein yield and protein content. SDS-PAGE characterization showed protein bands at different molecular weights (kDa). Protein isolates demonstrated good functional properties and antilipase activity as compared to flour. In the cell line experiments, protein 1 exhibited a dose-dependent reduction in the lipid content.

Conclusion

seed protein could pave the way for the development of nutraceutical formulation in the treatment of obesity.

Loading

Article metrics loading...

/content/journals/rafna/10.2174/012772574X346300241111055324
2024-12-09
2025-05-31
Loading full text...

Full text loading...

References

  1. Acosta C. Carpio C. Vilcacundo R. Carrillo W. Identification of proteins isolate from amaranth (Amaranthus caudatus) by sodium dodecyl sulfate-polyacrylamide gel electrophoresis with water and NaCl 0.1 m solvents. Asian J. Pharm. Clin. Res. 2016 1 33 1 4
    [Google Scholar]
  2. Tovar-Pérez E.G. Guerrero-Legarreta I. Farrés-González A. Soriano-Santos J. Angiotensin I-converting enzyme-inhibitory peptide fractions from albumin 1 and globulin as obtained of amaranth grain. Food Chem. 2009 116 2 437 444 10.1016/j.foodchem.2009.02.062
    [Google Scholar]
  3. Bell C.G. Walley A.J. Froguel P. The genetics of human obesity. Nat. Rev. Genet. 2005 6 3 221 234 10.1038/nrg1556 15703762
    [Google Scholar]
  4. Kang J.G. Park C.Y. Anti-obesity drugs: A review about their effects and safety. Diabetes Metab. J. 2012 36 1 13 25 10.4093/dmj.2012.36.1.13 22363917
    [Google Scholar]
  5. Liu T.T. Liu X.T. Chen Q.X. Shi Y. Lipase inhibitors for obesity: A review. Biomed. Pharmacother. 2020 128 110314 10.1016/j.biopha.2020.110314 32485574
    [Google Scholar]
  6. Heck A.M. Yanovski J.A. Calis K.A. Orlistat, a new lipase inhibitor for the management of obesity. Pharmacotherapy 2000 20 3 270 279 10.1592/phco.20.4.270.34882 10730683
    [Google Scholar]
  7. Mhatre S Bhagit A Yadav R.P. In vitro studies of some edible spices on pancreatic lipase inhibitory activity. Ind. Drugs. 2017 54 2 62 10.53879/id.54.02.10815
    [Google Scholar]
  8. Bustanji Y. Mohammad M. Hudaib M. Tawaha K. Al-Masri I.M. AlKhatib H.S. Issa A. Alali F.Q. Screening of some medicinal plants for their pancreatic lipase inhibitory potential. Jordan J. Pharm. Sci. 2011 4 2 81 88
    [Google Scholar]
  9. de la Garza A. Milagro F. Boque N. Campión J. Martínez J. Natural inhibitors of pancreatic lipase as new players in obesity treatment. Planta Med. 2011 77 8 773 785 10.1055/s‑0030‑1270924 21412692
    [Google Scholar]
  10. Mhatre S.V. Bhagit A.A. Yadav R.P. Proteinaceous pancreatic lipase inhibitor from the seed of Litchi chinensis. Food Technol. Biotechnol. 2019 57 1 113 118 10.17113/ftb.57.01.19.5909 31316283
    [Google Scholar]
  11. Satouchi K. Kodama Y. Murakami K. Tanaka T. Iwamoto H. Ishimoto M. A lipase-inhibiting protein from lipoxygenase-deficient soybean seeds. Biosci. Biotechnol. Biochem. 2002 66 10 2154 2160 10.1271/bbb.66.2154 12450126
    [Google Scholar]
  12. Chapman G.W. Jr A proteinaceous competitive inhibitor of lipase isolated from Helianthus annuus seeds. Phytochemistry 1987 26 12 3127 3131 10.1016/S0031‑9422(00)82455‑3
    [Google Scholar]
  13. Hayes M. Measuring protein content in food: An overview of methods. Foods 2020 9 10 1340 10.3390/foods9101340 32977393
    [Google Scholar]
  14. Adebiyi A.P. Adebiyi A.O. Ogawa T. Muramoto K. Preparation and characterization of high‐quality rice bran proteins. J. Sci. Food Agric. 2007 87 7 1219 1227 10.1002/jsfa.2819
    [Google Scholar]
  15. Fidantsi A. Doxastakis G. Emulsifying and foaming properties of amaranth seed protein isolates. Colloids Surf. B Biointerfaces 2001 21 1-3 119 124 10.1016/S0927‑7765(01)00165‑5 11377941
    [Google Scholar]
  16. Alarcón-García M.A. Perez-Alvarez J.A. López-Vargas J.H. Pagán-Moreno M.J. Techno-functional properties of new Andean ingredients: Maca (Lepidium meyenii) and Amaranth (Amaranthus caudatus) Proceedings 2020 70 1 74
    [Google Scholar]
  17. Stoytcheva M. Montero G. Zlatev R.A. Leon J. Gochev V. Analytical methods for lipases activity determination: A review. Curr. Anal. Chem. 2012 8 3 400 407 10.2174/157341112801264879
    [Google Scholar]
  18. Jafar S. Kamal H. Mudgil P. Hassan H.M. Maqsood S. Camel whey protein hydrolysates displayed enhanced cholesteryl esterase and lipase inhibitory, anti-hypertensive and anti-haemolytic properties. Lebensm. Wiss. Technol. 2018 98 212 218 10.1016/j.lwt.2018.08.024
    [Google Scholar]
  19. Hengpratom T. Ngernsoungnern A. Ngernsoungnern P. Lowe G.M. Eumkeb G. Antiadipogenesis of Oroxylum indicum (L.) Kurz extract via PPAR γ 2 in 3T3‐L1 adipocytes. Evid. Based Complement. Alternat. Med. 2020 2020 1 6720205 10.1155/2020/6720205 31998399
    [Google Scholar]
  20. Zhang X. Shi J. Fu Y. Zhang T. Jiang L. Sui X. Structural, nutritional, and functional properties of amaranth protein and its application in the food industry: A review. Sustain. Food. Proteins. 2023 1 1 45 55 10.1002/sfp2.1002
    [Google Scholar]
  21. Jain A. Prakash M. Radha C. Extraction and evaluation of functional properties of groundnut protein concentrate. J. Food Sci. Technol. 2015 52 10 6655 6662 10.1007/s13197‑015‑1758‑7 26396413
    [Google Scholar]
  22. Dachmann E. Nobis V. Kulozik U. Dombrowski J. Surface and foaming properties of potato proteins: Impact of protein concentration, pH value and ionic strength. Food Hydrocoll. 2020 107 105981 10.1016/j.foodhyd.2020.105981
    [Google Scholar]
  23. Burger T.G. Zhang Y. Recent progress in the utilization of pea protein as an emulsifier for food applications. Trends Food Sci. Technol. 2019 86 25 33 10.1016/j.tifs.2019.02.007
    [Google Scholar]
  24. Branch S. Maria S. Evaluation of the functional properties of mung bean protein isolate for development of textured vegetable protein. Int. Food Res. J. 2017 24 4 1595 1605
    [Google Scholar]
/content/journals/rafna/10.2174/012772574X346300241111055324
Loading
/content/journals/rafna/10.2174/012772574X346300241111055324
Loading

Data & Media loading...


  • Article Type:
    Research Article
Keywords: A. cruentus ; functional properties ; anticipated activity ; Amaranthus cruentus ; obesity ; proteins
This is a required field
Please enter a valid email address
Approval was a Success
Invalid data
An Error Occurred
Approval was partially successful, following selected items could not be processed due to error
Please enter a valid_number test