Preview

Izvestiya TINRO

Advanced search

Study on biological activity of tissues from bivalve mollusks

https://doi.org/10.26428/1606-9919-2018-195-253-264

Abstract

Biological activity of tissues and enzyme hydrolyzates is investigated for three species of bivalve mollusks: Corbicula japonica, Mercenaria mercenaria, and Anadara broughtonii. Antiradical activity of all samples has increased signifcantly during their enzymatic hydrolysis: in eight times for C. japonica, in three times for M. mercenaria, and in 2.5 times for A. broughtonii. The highest anti-trombolitic activity (0.0823 units) is found for the hydrolyzate of C. japonica in concentration of 10 mg/mL. Angiotensin I-converting enzyme inhibitory activity is found only for the hydrolyzate of M. mercenaria in concentration of 10–100 mg/mL. The maximum inhibitory activity for alpha-amylase and alpha-glycosidase (7.5 and 7.2 %, respectively) is observed for the hydrolyzate of M. mercenaria in concentration 1 mg/mL. Hepatoprotective activity, measured by survival rate of HepG2 hepatocytes, is detected for the hydrolyzate of tissues for all species in weak concentrations: 0.1 mg/mL for C. japonica and M. mercenaria and 0.2 mg/mL for A. broughtonii.

About the Authors

E. P. Karaulova
Тихоокеанский научно-исследовательский рыбохозяйственный центр
Russian Federation

Karaulova Ekaterina P., Ph.D., senior researcher



H. D. Yoon
Биологическая пищевая компания
Korea, Republic of

Yoon Ho Dong, Ph.D., director



J. G. Kim
Кенгсанский национальный университет
Korea, Republic of

Kim Jeong Gyun, professor



S. H. Park
Кенгсанский национальный университет
Korea, Republic of

Park Si Hyang, Ph.D., head of department



T. N. Slutskaya
Тихоокеанский научно-исследовательский рыбохозяйственный центр
Russian Federation

Slutskaya Tatiana N., D.Sc., professor, head of department



E. V. Yakush
Тихоокеанский научно-исследовательский рыбохозяйственный центр
Russian Federation

Yakush Eugeny V., Ph.D., deputy director



References

1. Ayushin, N.B., Petrova, I.P., and Epshtein, L.M., Taurine and carnosine in tissues of Pacifc mollusks, Vopr. Pitaniya, 1997, no. 6, pp. 6–8.

2. Voronina, T.A., Antioxidant Mexidol. The basic neuropsychotropic effects and mechanism of action, Psychopharmakol. Biol. Narkol., 2001, vol. 1, no. 1, pp. 2–12.

3. Karaulova, E.P. and Chepkasova, A.I., Peptides of marine animals as a potential source of natural antioxidants, Izv. Tikhookean. Nauchno–Issled. Inst. Rybn. Khoz. Okeanogr., 2017, vol. 189, pp. 192–203.

4. Karaulova, E.P., Chepkasova, A.I., Slutskaya, T.N., Shulgina, L.V., and Yakush, E.V., Antiradical effect of low-molecular peptides in extracts and hydrolyzates from tissues of water organisms, Izv. Tikhookean. Nauchno–Issled. Inst. Rybn. Khoz. Okeanogr., 2015, vol. 182, pp. 269–276.

5. Kupina, N.M., The main results of the study of bivalve mollusks in the coastal zone of the Japan Sea, Izv. Tikhookean. Nauchno–Issled. Inst. Rybn. Khoz. Okeanogr., 2015, vol. 182, pp. 249–257.

6. Ovodova, R.G., Molchanova, V.I., Mikeiskaya, L.V., and Ovodov, Yu.S., General characteristics of immunomodulator bioglycans from invertebrates of the Sea of Japan, Chem. Nat. Compd., 1990, no. 6, pp. 738–742.

7. Apostolidis, E., Kwon, Y.I., and Shetty, K., Potential of cranberry-based herbal synergies for diabetes and hypertension management, Asia Pac. J. Clin. Nutr., 2006, vol. 15, no. 3, pp. 433–441.

8. Bolignano, D., Cernaro, V., Gembillo, G., Baggetta, R., Buemi, M., and D’Arrigo, G., Antioxidant agents for delaying diabetic kidney disease progression: A systematic review and metaanalysis, PLoS One, 2017, vol. 12, no. 6, art. ID e0178699. doi 10.1371/journal.pone.0178699

9. Chalamaiah, M., Dinesh Kumar, B., Hemalatha, R., and Jyothirmayi, T., Fish protein hydrolysates: Proximate composition, amino acid composition, antioxidant activities and applications: a review, Food Chem., 2012, vol. 135, no. 4, pp. 3020–3038. doi 10.1016/j.foodchem.2012.06.100

10. Chang, G.T., Min, S.Y., Kim, J.H., Kim, S.H., Kim, J.K., and Kim, C.H., Anti-thrombic activity of Korean herbal medicine, Dae-Jo-Whan and its herbs, Vasc. Pharmacol., 2005, vol. 43, no. 4, pp. 283–288. doi 10.1016/j.vph.2005.08.014

11. Chijimatsu, T., Tatsuguchi, I., Oda, H., and Mochizuki, S., A 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, no. 8, pp. 3108–3112. doi 10.1021/jf803308h

12. Degirolamo, C., Modica, S., Vacca, M., Di Tullio, G., Morgano, A., D’Orazio, A., Kannisto, K., Parini, P., and Moschetta, A., Prevention of spontaneous hepatocarcinogenesis in farnesoid X receptor-null mice by intestinal-specifc farnesoid X receptor reactivation, Hepatology, 2015, vol. 61, no. 1, pp. 161–170. doi 10.1002/hep.27274

13. Dunehoo, A.L., Anderson, M., Majumdar, S., Kobayashi, N., Berkland, C., and Siahaan, T.J., Cell adhesion molecules for targeted drug delivery, J. Pharm. Sci., 2006, vol. 95, no. 9, pp. 1856–1872. doi 10.1002/jps.20676

14. Evran, B., Karpuzoğlu, H., Develi, S., Kalaz, E.B., Soluk-Tekkeşin, M., Olgaç, V., DoğruAbbasoğlu, S., and Uysal, M., Effects of carnosine on prooxidant-antioxidant status in heart tissue, plasma and erythrocytes of rats with isoproterenol-induced myocardial infarction, Pharmacol. Rep., 2014, vol. 66, no. 1, pp. 81–86. doi 10.1016/j.pharep.2013.08.008

15. FitzGerald, R.J. and Meisel, Н., Milk protein-derived peptide inhibitors of angiotensin-Iconverting enzyme, Br. J. Nutr., 2000, vol. 84, suppl. 1, pp. 33–37.

16. Hansawasdi, C., Kawabata, J., and Kasai, T., Alpha-amylase inhibitors from roselle (Hibiscus sabdariffa Linn.) tea, Biosci., Biotechnol., Biochem., 2000, vol. 64, no. 5, pp. 1041–1043. doi 10.1271/bbb.64.1041

17. Hartmann, R. and Meisel, H., Food-derived peptides with biological activity: from research to food applications, Curr. Opin. Biotechnol., 2007, vol. 18, no. 2, pp. 163–169. doi 10.1016/j.copbio.2007.01.013

18. Hsu, C.L., Hsu, C.C., and Yen, G.C., Hepatoprotection by freshwater clam extract against CCl 4-induced hepatic damage in rats, Am. J. Chin. Med., 2010, vol. 38, no. 5, pp. 881–894. doi 10.1142/S0192415X10008329

19. Je, J.Y., Lee, K.H., Lee, M.H., and Ahn, C.B., Antioxidant and antihypertensive protein hydrolysates produced from tuna liver by enzymatic hydrolysis, Food Res. Int., 2009, vol. 42, no. 9, pp. 1266–1272.

20. Wanasundara, P.K., Ross, A.R.S., Amarowicz, R., Ambrose, S.J., Pegg, R.B., and Shand, P.J., Peptides with angiotensin I-converting enzyme (ACE) inhibitory activity from defbrinated, hydrolyzed bovine plasma, J. Agric. Food Chem., 2002, vol. 50, no. 24, pp. 6981–6988.

21. Leng, B., Liu, X.D., and Chen, Q.X., Inhibitory effects of anticancer peptide from Mercenaria on the BGC-823 cells and several enzymes, FEBS Lett., 2005, vol. 579, no. 5, pp. 1187–1190. doi 10.1016/j.febslet.2004.12.089

22. Molyneux, P., The use of the stable free radical diphenylpicrylhydrazyl (DPPH) for estimating antioxidant activity, Songklanakarin J. Sci. Technol., 2004, vol. 26, no. 2, pp. 211–219.

23. Souza, S.R.G., Miranda Neto, M.H., Martins Perles, J.V.C., Vieira Frez, F.C., Zignani, I., Ramalho, F.V., Hermes-Uliana, C., Bossolani, G.D., and Zanoni, J.N., Antioxidant effects of the quercetin in the jejunal myenteric innervation of diabetic rats, Front. Med. (Lausanne), 2017, vol. 4. doi 10.3389/fmed.2017.00008

24. Sui, X. and Gao, С., Huperzine A ameliorates damage induced by acute myocardial infarction in rats through antioxidant, anti-apoptotic and anti-inflammatory mechanisms, Int. J. Mol. Med., 2014, vol. 33, no. 1, pp. 227–233. doi 10.3892/ijmm.2013.1546

25. Tundis, R., Loizzo, M.R., Menichini, F., Bonesi, M., Conforti, F., Statti, G., De Luca, D., de Cindio B., and Menichini, F., Comparative study on the chemical composition, antioxidant properties and hypoglycaemic activities of two Capsicum annuum L. cultivars (Acuminatum small and Cerasiferum), Plant Foods Hum. Nutr., 2011, vol. 66, no. 3, pp. 261–269. doi 10.1007/s11130-011-0248-y

26. Turcic, P., Stambuk, N., Konjevoda, P., Kelava, T., Gabricevic, M., Stojkovic, R., Aralica, G., Modulation of γ2-MSH hepatoprotection by antisense peptides and melanocortin subtype 3 and 4 receptor antagonists, Med. Chem., 2015, vol. 11, no. 3, pp. 286–295. doi 10.2174/1573406410666140914161421

27. Xia, E.Q., Zhu, S.S., He, M.J., Luo, F., Fu, C.Z., and Zou, T.B., Marine peptides as potential agents for the management of type 2 diabetes mellitus-A prospect, Mar. Drugs, 2017, vol. 15, no. 4. doi 10.3390/md15040088

28. You, L., Zhao, M., Cui, C., Zhao, H., and Yang, B., Effect of degree of hydrolysis on the antioxidant activity of loach (Misgurnus anguillicaudatus) protein hydrolysates, Innovative Food Sci. Emerging Technol., 2009, vol. 10, no. 2, pp. 235–240.


Review

For citations:


Karaulova E.P., Yoon H.D., Kim J.G., Park S.H., Slutskaya T.N., Yakush E.V. Study on biological activity of tissues from bivalve mollusks. Izvestiya TINRO. 2018;195(4):253-264. (In Russ.) https://doi.org/10.26428/1606-9919-2018-195-253-264

Views: 614


Creative Commons License
This work is licensed under a Creative Commons Attribution 4.0 License.


ISSN 1606-9919 (Print)
ISSN 2658-5510 (Online)