Obtaining peptides from aquatic organisms of the Antarctic region

N. Raksha, T. Maievska, O. Savchuk
NGO "Ukraine's fishing industry cluster of innovations", Kyiv; NGO "Ukraine's fishing industry cluster of innovations", Kyiv; NGO "Ukraine's fishing industry cluster of innovations", Kyiv


The rapid growth in demand for peptide drugs is actualizing the search for new natural and economically viable sources of raw materials. The
wide variety of biologically active compounds, including peptide nature, inherent in marine aquatic organisms allows us to consider their promising raw material resource. However, the use of marine objects as a source for the production of target molecules requires some optimization of existing methodological approaches to their isolation and ensure the appropriate degree of purification. The problem of optimization of the method of obtaining peptides from hydrobionts of the Antarctic region on the example of the hydrobiont Nacellaconcinna is solved in the work. The proposed three-step approach allows to isolate fractions of peptides of different molecular weight. The first step involved the precipitation of high molecular weight protein material first with perchloric acid and then with 80% ethyl alcohol. The result was a fraction of peptide molecules with a molecular weight of up to 6.5 kDa, which contained a small amount of high molecular weight protein impurities. Further purification of the obtained fraction was performed by
ultrafiltration using membranes with a pore size of 10 kDa. Control of the protein-peptide composition of the sample at all stages of production was performed by disk electrophoresis under denaturing conditions in plates of 18% polyacrylamide gel. Analysis using 2D electrophoresis found that the isoelectric points of most peptides are in the pH range from 8.0 to 10.0. Only a small proportion of the peptides had isoelectric points at 4.0 and 5.0 pH. The final step of obtaining the peptide fraction involved fractionation of the sample by gel chromatography. As a result of chromatographic separation, four peaks were obtained, corresponding to the fractions with peptides, the molecular weight of which is about 2.3 kDa (1 peak), 1.9 kDa (2 peak), 1.4 kDa (3 peak) and 0.7 kDa (4 peak).


hydrobionts, peptide fraction, production method

Full Text:



Lovejoy D.A., Hogg D.W., Dodsworth T.L., Jurado F.R., Read C.C., D'Aquila A.L., Barsyte-Lovejoy D. Synthetic Peptides as Therapeutic Agents: Lessons Learned From Evolutionary Ancient Peptides and Their Transit Across Blood-Brain Barriers // Front Endocrinol (Lausanne). 2019; 10; 730.

Cheng S., Yu X., Zhang Y. Extraction of polysaccharides from Mytilusedulis and their antioxidant activity in vitro. ShipinGongyeKeji. 2010; 31 ;132–134.

Lordan S., Ross R.P., Stanton C. Marine bioactives as functional food ingredients: Potential to reduce the incidence of chronic diseases. Mar. Drugs. 2011;9;1056–1100. doi: 10.3390/md9061056.

Ganesan P., Noda K., Manabe Y., Ohkubo T., Tanaka Y., Maoka T., et al. Siphonaxanthin, a marine carotenoid from green algae, effectively induces apoptosis in human leukemia (HL-60) cells. Biochim. Biophys. Acta. 2011;1810;497–503. doi: 10.1016/j.bbagen.2011.02.008

Mayer A., Rodríguez A., Taglialatela-Scafati O., Fusetani N. Marine Pharmacology in 2009–2011: Marine Compounds with Antibacterial, Antidiabetic, Antifungal, Anti-Inflammatory, Antiprotozoal, Antituberculosis, and Antiviral Activities; Affecting the Immune and Nervous Systems, and other Miscellaneous Mechanisms of Action.Mar. Drugs. 2013;11;2510–2573; doi:10.3390/md11072510

Se-KwonKima, IsuruWijesekaraa. Development and biological activities of marine-derived bioactive peptides: A review. J Functional Foods. 2010;2;1–9.

Bougatef N. Nedjar-Arroume L. Manni. Purification and identification of novel antioxidant peptides from enzymatic hydrolysates of sardinelle (Sardinellaaurita) by-products proteins. Food Chemistry. 2010;118(3);559–565.

Su Y. Isolation and identification of pelteobagrin, a novel antimicrobial peptide from the skin mucus of yellow catfish (Pelteobagrusfulvidraco). Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology. 2011;158(2);149–154.

Wu H., He H.-L., Chen X.-L., Sun C.-Y., Zhang Y.-Z., Zhou B.-C. Purification and identification of novel angiotensin-I-converting enzyme inhibitory peptides from shark meat hydrolysate. Process Biochemistry. 2008;43(4);457–461.

Rajapakse N., Jung W.-K., Mendis E., Moon S.-H., Kim S.-K. A novel anticoagulant purified from fish protein hydrolysate inhibits factor XIIa and platelet aggregation. Life Sciences. 2005;76(22);2607–2619.

Nikolajchik V., Moin V., Kirkovskij, V. Sposob opredeleniya srednih molekul. Laboratornoe delo. 1991;10;13–18.

Laemmli K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970;227(1);680-685.

2-D Electrophoresis Principles and Methods Amersham Biosciences UK Limited Amersham Place Little Chalfont. 2004;168.

Shen Y, Ai HX, Song R, Liang ZN, Li JF, Zhang SQ. Expression and purification of moricin CM4 and human beta-defensins 4 in Escherichia coli using a new technology. Microbiol Res. 2010;165(8);713-8. doi: 10.1016/j.micres.2010.01.002. Epub 2010 Jan 20.

Duan X., Ocen D., Wu F.F., Li M., Yang N., Xu J., Chen H.Y., Huang L.Q., Jin Z.Y., Xu X.M. Purification and characterization of a natural antioxidant peptide from fertilized eggs. Food Res. 2014;56;18–24.

Scott M.G., Hancock R.E. Cationic antimicrobial peptides and their multifunctional role in the immune system. Crit Rev Immunol. 2000;20;407–431.

Hilpert K., Fjell C.D., Cherkasov A. Short linear cationic antimicrobial peptides: screening, optimizing, and prediction. Methods Mol Biol. 2008;494;127–159.

Received: 05.01.2021

Revised: 02.02.2021

Signed for the press: 02.02.2021

DOI: http://dx.doi.org/10.17721/1728_2748.2021.84.38-43


  • There are currently no refbacks.

Лицензия Creative Commons
This journal is available according to the Creative Commons License «Attribution» («Атрибуція») 4.0 Global (CC-BY).