Enzymatic Production of Sarotherodon galillaeus Muscle Protein Hydrolysates and Assessment of its Alpha-Amylase Inhibitory and Antioxidant Potential

Author(s): Oludele Olayemi ODEKANYIN, Abideen Oyinlola Ayangbemi, Aanuoluwapo Joy Jerome

The study was carried out to evaluate the antioxidant activity and α-amylase activity inhibitory potential of Sarotherodon galillaeus muscle protein hydrolysates. Sarotherodon galillaeus muscle protein isolate was hydrolysed with three digestive proteases namely trypsin, chymotrypsin and pepsin. Degree of hydrolysis was determined. The antioxidative potential of the hydrolysates was investigated using DPPH radical scavenging, ferric reducing power, hydrogen peroxide scavenging and metal chelating activity. The ability of the hydrolysates to inhibit the activity of sugar-hydrolysing enzyme was also evaluated. Highest degree of hydrolysis was obtained with pepsin (55.86%) followed by trypsin (47.11%) and chymotrypsin (42.36%) after 6 hrs of hydrolysis. The half maximal inhibitory concentration (IC50) of hydrolysates produced by trypsin, chymotrypsin and pepsin for DPPH radical scavenging activity were 1.26 ± 0.95, 0.98 ± 0.07 and 1.18 ± 0.34 mg/ml respectively. Trypsin-produced hydrolysates displayed highest metal chelating activity and ferric reducing power while hydrolysates obtained with pepsin showed highest hydrogen peroxide scavenging activity. Amylase activity inhibitory potential of all the hydrolysates was low with pepsin-produced hydrolysates shown highest inhibitory effect of 18.46 ± 1.51%. The hydrolysates showed antioxidative potential that can be used in prevention of food oxidation.

Sarotherodon galillaeus, Hydrolysate, Amylase, Antioxidant, Degree of Hydrolysis

1. Ajibola, C.F., Fashakin, J.B., Fagbemi, T.N., Aluko, R.E. (2011). Effect of peptide size on antioxidant properties of African yam bean seed (Sphenostylis stenocarpa) protein hydrolysate fractions. Int. J. Mol. Sci., 12: 6685–6702.
2. Babu, D., Gurumurthy, P., Borra, S. K., and Cherian, K. M. (2013). Antioxidant and free radical scavenging activity of triphala determined by using different in vitro models. Journal of Medicinal Plants Research, 7 (39): 2898-2905.
3. Balti, R., Nedjar-Arroume, N., Bougatef, A., Guillochon, D. and Nasri, M. (2010). Three novel angiotensin I-converting enzyme (ACE) inhibitory peptides from cuttlefish (Sepia officinalis) using digestive proteases. Food Research International 43:1136–1143.
4. Benjakul, S. and Morrissey, M.T. (1997). Protein hydrolysates from Pacific whiting solid wastes. J Agric Food Chem. 45(9):3423–3430. doi: 10.1021/jf970294g.
5. Ben-Khaled, H., Ghlissi, Z., Chtourou, Y., Hakim, A., Ktari, N., Fatma, M. A., Barkia, A., Sahnoun Z., and Nasri, M. (2012). Effect of protein hydrolysates from sardinelle (Sardinella aurita) on the oxidative status and blood lipid profile of cholesterol-fed rats. Food Research International 45(1): 60-68. doi.org/10.1016/j.foodres.2011.10.003
6. Bernardini, R. D., Harnedy, P., Bolton, D., Kerry, J., O’Neill, E., Mullen, A. M., and Hayes, M. (2011). Antioxidant and antimicrobial peptidic hydrolysates from muscle protein sources and by-products-Review. Food Chemistry 124: 1296-1307
7. Bougatef A., Hajji M., Balti R., Lassoued I., Triki-Ellouz Y. and Nasri M. (2009).Antioxidant and free radical-scavenging activities of smooth hound (Mustelus mustelus) muscle protein hydrolysates obtained by gastrointenstinal proteases. Food Chemistry, 114 (4):1198-1205.
8. Cao W., He X., Zhao Z. and Zhaung C. (2013). Analysis of protein composition and antioxidant activity of hydrolysates from Paphia undulate. Journal of Food and Nutrition Research 1(3): 30-36.
9. Chalamaiah, M., Kumar, B. D., Hemalatha, R., and Jyothirmayi, T. (2012). Fish Protein Hydrolysates: proximate composition, amino acid composition, antioxidant activities and applications: a review. Food Chemistry, 135: 3020-3038.
10. Chonlatid, S., Opeyemi, J. O. and Chitchamai, O. (2018). Evaluation of in-vitro α-amylase and α-glucosidase inhibitory potentials of 14 medicinal plants constituted in Thai folk antidiabetic formularies. Chemistry and Biodiversity 15(4):e1800025. http://doi.org/10.1002/cbdv.201800025
11. Cristina, T. F., Manuel, A. and Vioque, J. (2012). Iron-chelating activity of chickpea protein hydrolysate peptides. Food Chemistry, 134:1585-1588.
12. Daud, N. A., Babji, A. S. and Mohamad Y. S. (2013). “Antioxidant activities of Red Tilapia (Oreochromis niloticus) protein hydrolysates as influenced by thermolysin and alcalase”. In AIP Conference Proceedings 1571: 687-691. https://doi.org/10.1063/1.4858734
13. Elavarasan, K., Shamasundar, B. A., Badii, F. and Howell, N. (2016). Angiotensin I-converting enzyme (ACE) inhibitory activity and structural properties of oven- and freeze-dried protein hydrolysate from fresh water fish (Cirrhinus mrigala). Food Chemistry, 206: 210–216.
14. Erdmann, K., Cheung, B.W.Y. and Schroder, H. (2008). The possible roles of food-derived bioactive peptides in reducing the risk of cardiovascular disease. Journal of Nutritional Biochemistry, 19(10):643-654.
15. Fan, J., He, J., Zhuang, Y., and Sun, L. (2012). Purification and identification of antioxidant peptides from enzymatic hydrolysates of tilapia (Oreochromis niloticus) frame protein. Molecules. 17(11): 12836-12850.
16. Farvin, K.H.S., Andersen, L.L., Nielsen, H.H., Jacobsen, C., Jakobsen, G., Johansson, I., and Jessen. F. (2014) Antioxidant activity of Cod (Gadus morhua) protein hydrolysates: in-vitro assays and evaluation in 5% fish oil- in-water emulsion. Food Chemistry 149: 326-334.
17. Froese I., Rainer K. and Pauly D. (2014). Sarotherodon galillaeus. Fish Base, 23:3-10.
18. Harnedy, P. and FitzGerald, R. J. (2013). Extraction of protein from the macroalga Palmaria palmate. LWT- Food Science and Technology 51(1):375–382DOI: 10.1016/j.lwt.2012.09.023
19. Hoyle, N. T. and Merritt, J. H. (1994). Quality of fish protein hydrolysates from herring (Clupea harengas). Journal of Food Science, 59: 76-79.
20. Huang, F. J. and Wu, T. (2010). Purification and Characterization of a New Peptide (S-8300) from Shark Liver. Journal of Food Biochemistry. 34: 962–970. DOI: 10.1111/j.1745-4514.2010.00336.x.
21. Jan, F., Kumar, S. and Jha, R. (2016). Effect of bPP-IV inhibition on the antidiabetic property of enzyme treated sheep milk casein. Veterinary World 9(10):1152–1156. http://doi.org/10.14202/vetworld.2016.1152-1156
22. Jerome, J. A. and Odekanyin, O. O. (2019). Comparative studies on the antioxidant potential of hydrolysates of Mormyrus rume muscle protein. Ife Journal of Science 21(2): 431-440
23. Jia J., Zhou Y., Lu J., Chen A., Li Y. and Zheng G. (2010). Enzymatic hydrolysis of Alaska pollack (Theragra chalcogramma) skin and antioxidant activity of the resulting hydrolysate. Journal of the Science of Food and Agriculture. 90(4):635-640
24. Kehinde, B. A., and Sharma, P. (2018). Recently isolated antidiabetic hydrolysates and peptides from multiple food sources: a review. Critical Reviews in Food Science and Nutrition, 21:1-19
25. Korczek, K., Tkaczewska J. and Migdal, W. (2018). Antioxidant and Antihypertensive Protein Hydrolysates in Fish Products- a Review. Czech Journal of Food Sciences 36(3): 01-25.
26. Lowry O.H., Rosebrough N.J., Farr A.L. and Randall R.J. (1951). Protein measurement with the folin phenol reagent. Journal of Biological Chemistry. 193: 265-275.
27. Morais, H. A., Silvestre, M. P. C., Silva, V. D. M., Silva, M. R., Cristina, A., Silva, S. E. and Silveira, J. N. (2013). Correlation between the degree of hydrolysis and the peptide profile of whey protein concentrate hydrolysates: Effect of the enzyme type and reaction time. American Journal of Food Technology, 8(1): 1-16.
28. Nasri, M. (2017). Protein hydrolysates and biopeptides: Production, biological activities and applications in foods and health benefits. A review. Advances in Food and Nutrition Research, 81: 109-159.
29. Nasri, R., Ben Khaled H., Nedjar-Arroume N., Chaâbouni M. K., Dhulster P. and Nasri M. (2012). Antioxidant and Free Radical-Scavenging Activities of Goby (Zosterisessor ophiocephalus) Muscle Protein Hydrolysates Obtained by Enzymatic Treatment. Journal of Food Biotechnology 26(3): 266-279.
30. Nasri, R., O. Abdelhedi, I. Jemil, I. Daoued, K. Hamden, C. Kallel, A.Elfeki, M. Lamri-Senhadji, A. Boualga, M. Nasri, and M. Karra-Chaabouni. (2015). Ameliorating effects of goby fish protein hydrolysates on high-fat-high-fructose diet-induced hyperglycemia; oxidative stress and deterioration of kidney function in rats. Chemico-Biological Interactions 242:71–280. https://doi.org/10.1016/j.cbi.2015.08.003
31. Ngo, D.H., Vo, T.S., Ngo, D.N. and Kim, S.K. (2012).Biological activities and potential health benefits of bioactive peptides derived from marine organisms. International Journal of Biological Macromolecules. 51(4):378-383.
32. Persson, T., Popescu, B. O. and Cedazo-Minguez, A. (2014).Oxidative Stress in Alzheimer’s Disease: Why Did Antioxidant Therapy Fail?. Oxidative Medicine and Cellular Longevity, vol. 2014, Article ID 427318. https://doi.org/10.1155/2014/427318.
33. Picot, L., Bordenave, S., Didelot, S., Fruitierarnaudin, I., Sannier, F., Thorkelsson, G., Berge, J., Guerard, F., Chabeaud, A. and Picot, J. (2006). Antiproliferative activity of fish protein hydrolysates on human breast cancer cell lines. Process Biochem. 41:1217–1222.
34. Rahimi, R., Nikfar, S., Larijani, B., and Abdollahi, M. (2005). A review on the role of antioxidants in the management of diabetes and its complications. Biomed Pharmacother. 59:365–373.
35. Ramadhan, H. A, Nawas, T. Zhang, X., Pembe, W. M., Xia W. andXu, Y. (2017). Purification and identification of a novel antidiabetic peptide from Chinese giant salamander (Andrias davidianus) protein hydrolysate against α-amylase and α-glucosidase. International Journal of Food Properties, 20: S3360-S3372. DOI: 10.1080/10942912.2017.1354885
36. Saiga, A.; Tanabe, S.; Nishimura, T. Antioxidant activity of peptides obtained from porcine myofibrillar proteins by protease treatment. J. Agric. Food Chem. 2003, 51, 3661–3667.
37. Sun L., Zhaung Y., He J. and Fan J. (2012). Purification and identification of antioxidant peptides from enzymatic hydrolysis of tilapia (Oreochromis niloticus) frame protein.Molecules.17:12836-12850.
38. Toniato, J., Penman, D. J. and Martins, C. (2010). Discrimination of tilapia species of the genera Oreochromis, Tilapia and Sarotherodon by PCR-RFLP of 5S rDNA. Aquaculture Research 41(6): 934–938DOI: 10.1111/j.1365-2109.2009.02366.x
39. Wang, J., K. Du, L. Fang, C. Liu, W. Min, and J. Liu. (2018). Evaluation of the antidiabetic activity of hydrolyzed peptides derived from Juglans mandshurica maxim. fruits in insulin-resistant HepG2 cells and type 2 diabetic mice. Journal of Food Biochemistry 42(3):e12518. http://doi.org/10.1111/jfbc.12518
40. Xia, E. Q., Zhu, S. S., He, M. J., Luo, F., Fu, C. Z. and Zou, T. B. (2017). Marine peptides as potential agents for the management of Type-2 Diabetes Mellitus-A Prospect. Marine Drugs 15(4): 88-104.
41. Zambrowicz, A., Eckert, E., Pokora, M., Bobak, Ł., Da˛browska, A., Szołtysik, M., Trziszka, T. and Chrzanowska, J. (2015). Antioxidant and antidiabetic activities of peptides isolated from a hydrolysate of an egg-yolk protein by-product prepared with a proteinase from Asian pumpkin (Cucurbita ficifolia). RSC Advances 5(14):10460–10467. http:// doi.org/10.1039/C4RA12943A.
42. Zhuang, Y. L., Sun, L. P., Zhao, X., Hou, H., Li, B. F. (2010) Investigation of Gelatin polypeptides of Jellyfish (Rhopilema esculentum) for their antioxidant activity in vitro. Food Technol. Biotechnol. 48(2): 222-228.