Antiradical effect of low-molecular peptides in extracts and hydrolyzates from tissues of water organisms

Molecular-weight composition of peptides in extracts and hydrolyzates from soft tissues of the clams Corbicula japonica and Mercenaria mercenaria and liver of chum salmon is investigated. Antiradical activity is defined for low-molecular peptides, as well as for high-molecular proteins and free amino acids in the extracts. The maximum activity is detected for the extracts of salmon liver; all protein fractions in the water extract of the liver have antiradical activity. Low-molecular peptides and free amino acids have antiradical activity in all samples. The peptides with molecular weight 4.3 kDa have the highest activity in the water extract from C. japonica (43 units) and the peptides with molecular weight 4.7 kDa - in the water extract from M. mercenaria (5.6 units). After hydrolysis, the portion of low-molecular peptides increases for C. japonica , M. mercenaria , and salmon liver in 22.1, 14.5, and 11.1 %, respectively. Hence antiradical activity for hydrolyzates from C. japonica and M. mercen aria is in 1.9 times higher and for hydrolyzates from salmon liver - in 1.3 times higher than for water extracts from their tissues. Only the peptides with molecular weight 2.8-4.7 kDa have antiradical activity in the hydrolyzates; its value is 1-24 activity units for M. mercenaria ; 13-76 units for C. japonica and about 40 units for the chum salmon liver. Correlation is found between the content of peptides with molecular weight 3-4 kDa in hydrolyzates and their antiradical activity.

peptide, antiradical activity, Corbicula japonica, Mercenaria mercenaria, chum salmon, hydrolyzate, water extract

1. Морозов В.Г., Хавинсон В.Х., Малинин В.В. Пептидные тимомиметики : моногр. - СПб. : Наука, 2000. - 158 с.

2. Хавинсон В.Х., Кветная Т.В. Регуляторные пептиды и гомеостаз // Журн. российского хим. об-ва им. Д.И. Менделеева. - 2005. - Т. 49, № 1. - С. 112-117.

3. Чепкасова А.И., Аюшин Н.Б., Якуш Е.В. Состав и свойства водорастворимого препарата из печени лососей // Изв. ТИНРО. - 2014. - Т. 178. - С. 253-260.

4. Ahn Chang-Bum, Kim Jeong-Gyun, Je Jae-Young. Purification and antioxidant properties of octapeptide from salmon byproduct protein hydrolysate by gastrointestinal digestion // Food Chemistry. - 2014. - Vol. 147. - P. 78-83.

5. Chalamaiah M., Kumar D., Hemalatha R., Jyothirmayi T. Fish protein hydrolysates: Proximate composition, amino acid composition, antioxidant activities and applications // Review. Food Chem. - 2012. - Vol. 135. - P. 3020-3038.

6. Chijimatsu T., Tatsuguchi I., Oda H., Mochizuki S. Freshwater clam (Corbicula fluminea) extract reduces cholesterol level and hepatic lipids in normal rats and xenobiotics-induced hypercholesterolemic rats // J. Agric. Food. Chem. - 2009. - Vol. 57. - P. 3108-3112.

7. Girgih A.T., Udenigwe C.C., Hasan F.M. et al. Antioxidant properties of Salmon (Salmo salar) protein hydrolysate and peptide fractions isolated by reverse-phase HPLC // Food Research International. - 2013. - Vol. 52, № 1. - P. 315-322.

8. Harada K., Maeda T., Hasegawa Y. et al. Antioxidant activity of fish sauces including puffer (Lagocephalus wheeleri) fish sauce measured by the oxygen radical absorbance capacity method // Molecular Medicine Reports. - 2010. - Vol. 3, № 4. - P. 663-668.

9. Hartman R., Meisel H. Food derived peptides with biological activity: From research to food applications // Current Opinion in Biotechnology. - 2007. - Vol. 18. - P. 163-169.

10. Hsu C.L., Hsu C.C., Yen G.C. Hepatoprotection by freshwater clam extract against CCl4-induced hepatic damage in rats // Am. J. Chin. Med. - 2010. - Vol. 38. - P. 881-894.

11. Jia J., Zhou Y., Lu J. et al. Enzymatic hydrolysis of Alaska pollack (Theragra chalcogramma) skin and antioxidant activity of the resulting hydrolysate // J. Sci. Food and Agriculture. - 2010. - Vol. 90. - P. 635-640.

12. Ko J.Y., Lee J.H., Samarakoon K. et al. Purification and determination of two novel antioxidant peptides from flounder fish (Paralichthys olivaceus) using digestive proteases // Food and Chemical Toxicology. - 2013. - Vol. 52. - P. 113-120.

13. Korhonen H., Pihlanto-Leppala A., Rantamaki P., Tupasela T. Impact of processing on bioactive proteins and peptides // Trends in Food Science and Technology. - 1998. - Vol. 9. - P. 307-319.

14. Kumar N.S.S., Nazeer R.A., Jaiganesh R. Purification and biochemical characterization of antioxidant peptide from horse mackerel (Magalaspis cordyla) viscera protein // Peptides. - 2011. - Vol. 32. - P. 1496-1501.

15. Lee Y.S., Noguchi T., Naito H. Intestinal absorption of calcium in rats given diets containing casein: the role of casein phosphopeptides // Br. J. Nutr. - 1983. - Vol. 49. - P. 67-76.

16. Leng B., Liu X.D., Chen Q.X. et al. Inhibitory effects of anticancer peptide from Mercenaria on the BGC-823 cells and several enzymes // FEBS Lett. - 2005. - Vol. 579(5). - P. 1187-1190.

17. Maruyama S., Nakagomi K., Tomizuka N., Suzuki H. Angiotensin I-converting enzyme inhibitor derived from an enzymatic hydrolysate of casein // Agric Biol. Chem. - 1985. - Vol. 49. - P. 1405-1409.

18. Mendis E., Rajapakse N., Byun H.G., Kim S.K. Investigation of jumbo squid (Dosidicus gigas) skin gelatin peptides for their in vitro antioxidant effects // Life Sci. - 2005. - Vol. 17. - P. 2166-2178.

19. Nazeer R.A., Sampath Kumar N.S., Jai Ganesh R. In vitro and in vivo studies on the antioxidant activity of fish peptide isolated from the croaker (Otolithes ruber) muscle protein hydrolysate // Peptide. - 2012. - Vol. 35. - P. 261-268.

20. Qin L., Zhu B.W., Zhou D.Y. et al. Preparation and antioxidant activity of enzymatic hydrolysates from purple sea urchin (Strongylocentrotus nudus) gonad // LWT-Food Sci. Technol. - 2011. - Vol. 44. - P. 1113-1118.

21. Yashiro A., Oda S., Sugano M. Hypocholesterolemic effect of soybean protein in rats and mice after peptic digestion // J. Nutr. - 1985. - Vol. 115. - P. 1325-1336.

22. Zhou X., Wang C., Jiang A. Antioxiant peptides isolated from sea cucumber Stichopus japonicus // Eur. Food Res. Technol. - 2012. - Vol. 234. - P. 441-447.