Antioxidant and Biochemical Properties of Protein Hydrolysates Prepared from Sacha Inchi Meal
Keywords:
sacha inchi meals, protein hydrolysate, antioxidant properties, bioactive peptideAbstract
The oil from sacha inchi is one type of oil which is very popular, especially among health-conscious people. However, after the oil extraction process, 50% of meal (residue) from the initial material remained, which is high in protein. This seems suitable to produce protein hydrolysate and peptide which is beneficial in bioactivity. This research aimed to produce the protein hydrolysate and peptide, which are good sources of antioxidants and have a biochemical effect to restrain the enzyme causing chronic diseases while also adding the value to the sacha inchi meal. Enzymatic hydrolysate was extracted from sacha inchi meal protein isolate by using flavourzyme. The sacha inchi protein hydrolysate (SPH) was further fractionated into peptide sizes of 1, 3, 5 and 10 kDa using membrane ultrafiltration. The <1 kDa peptides exhibited significantly better (p<0.05) diphenyl-1-picryhydradzyl (DPPH) and hydroxyl radical scavenging activities when compared to peptide fractions of higher molecular weights. The high activity of <1 kDa peptides in these antioxidant assay systems may be related to the high levels of total hydrophobic and aromatic amino acids. In comparison to glutathione, the SPH and its membrane fractions had higher ability to chelate metal ions. In addition, the <1 kDa peptides had the greatest ACE-inhibition (Hypertension), DPP-IV inhibition (Type 2 Diabetes), α-amylase
inhibition and α-glucosidase inhibition (Obesity) an IC50 value of 1.56, 2.31, 3.77 and 1.84 mg/ml, respectively. Antioxidant activities and enzyme inhibition were determined by the molecular weight and amino acid from peptide fractions.
References
Adebiyi, A.P. and R.E. Aluko. 2011. Functional properties of protein fractions obtained from commercial yellow field pea (Pisum sativum L.) seed protein isolate. Food Chem. 128(4): 902-908.
Aluko, R.E. 2019. Food protein-derived renin-inhibitory peptides: in vitro and in vivo properties. J. Food Biochem. 43: e12648.
Awosika, T.O. and R.E. Aluko. 2019. Inhibition of the in vitro activities of α-amylase, α-glucosidase and pancreatic lipase by yellow field pea (Pisum sativum L.) protein hydrolysates. Int. J. Food Sci. Technol. 54(6): 2021-2034.
Barbana, C. and J.I. Boye. 2010. Angiotensin I-converting enzyme inhibitory activity of chickpea and pea protein hydrolysates. Food Res. Int. 43(6): 1642-1649.
Chirinos, R., R. Pedreschi and D. Campos. 2020. Enzyme-assisted hydrolysates from sacha inchi (Plukenetia volubilis) protein with in vitro antioxidant and antihypertensive properties. J. Food Process. Preserv. 44(12): e14969.
Connolly, A., M.B. O’Keeffe, C.O. Piggott, A.B. Nongonierma and R.J. FitzGerald. 2015. Generation and identification of angiotensin converting enzyme (ACE) inhibitory peptides from a brewers’ spent grain protein isolate. Food Chem. 176: 64-71.
Fasuan, T.O., S.O. Gbadamosi and T.O. Omobuwajo. 2018. Characterization of protein isolate from Sesamum indicum seed: In vitro protein digestibility, amino acid profile, and some functional properties. Food Sci. Nutr. 6(6): 1715-1723.
Foh, M.B.K., I. Amadou, B.M. Foh, M.T. Kamara and W. Xia. 2010. Functionality and antioxidant properties of tilapia (Oreochromis niloticus) as influenced by the degree of hydrolysis. Int. J. Mol. Sci. 11(4): 1851-1869.
Girgih, A.T., C.C. Udenigwe and R.E. Aluko. 2011. In vitro antioxidant properties of hemp seed (Cannabis sativa L.) protein hydrolysate fractions. J. Am. Oil Chem. Soc. 88(3): 381-389.
Han, R., J. Maycock, B.S. Murray and C. Boesch. 2019. Identification of angiotensin converting enzyme and dipeptidyl peptidase-IV inhibitory peptides derived from oilseed proteins using two integrated bioinformatic approaches. Food Res Int. 115: 283-291.
Jack, F.K. and I. Mona. 1966. The kinetics of the papain-catalyzed hydrolysis of esters of carbobenzoxyglycine evidence for an acyl-enzyme Intermediate. J. Biochem. 5(2): 783-791.
Jagersberger, J. 2013. Development of Novel Products on Basis of Sacha Inchi-Use of Press Cakes and Hulls. Austria: University of Vienna. 125 p.
Lan, V.T., K. Ito, M. Ohno, T. Motoyama, S. Ito and Y. Kawarasaki. 2015. Analyzing a dipeptide library to identify human dipeptidyl peptidase IV inhibitor. Food Chem. 175: 66-73.
Landry, J. and S. Delhaye. 1992. Simplified procedure for the determination of tryptophan of foods and feedstuffs from barytic hydrolysis. J. Agric. Food Chem. 40(5): 776-779.
Lepping, P., J. Delieu, R. Mellor, J.H.H. Williams, P.R. Hudson and C. Hunter-Lavin. 2011. Antipsychotic medication and oxidative cell stress: A systematic review. J. Clin. Psychiatry. 72(3): 273-285.
Malomo, S.A., J.O. John, A.T. Girgih and R.E. Aluko. 2015. Structural and antihypertensive properties of enzymatic hemp seed protein hydrolysates. Nutrients 7(9): 7616-7632.
Markwell, M.A.K., S.M. Haas, L.L. Bieber and N.E. Tolbert. 1978. A modification of the Lowry procedure to simplify protein determination in membrane and lipoprotein samples. Anal. Biochem. 87(1): 206-210.
Maurer, N.E., B. Hatta-Sakoda, G. Pascual-Chagman and L.E. Rodriguez-Saona. 2012. Characterization and authentication of a novel vegetable source of omega-3 fatty acids, sacha inchi (Plukenetia volubilis L.) oil. Food Chem. 134(2): 1173-1180.
Parrado, J., F. Millan, I. Hernandez-Pinzon, J. Bautista and A. Machado. 1993. Characterization of enzymatic sunflower protein hydrolyzates. J. Agric. Food Chem. 41(11): 1821-1825.
Saiga, A., S. Tanabe and T. Nishimura. 2003. Antioxidant activity of peptides obtained from porcine myofibrillar proteins by protease treatment. J. Agric. Food Chem. 51(12): 3661-3667.
Santos, P.M., D.L.J. Batista, L.A.F. Ribeiro, E.F. Boffo, M.D. Cerqueira, D. Martins, R.D. Castro, L.C. Souza-Neta, E. Pinto, L. Zambotti-Villelae, P. Colepicoloe, L.G. Fernandez, G.A.B. Canuto and P.R. Ribeiro. 2018. Identification of antioxidant and antimicrobial compounds from the oilseed crop Ricinus communis using a multiplatform metabolite profiling approach. Ind. Crops Prod. 124(15): 834-844.
Sathe, S.K., H.H. Kshirsagar and G.M. Sharma. 2012. Solubilization, fractionation, and electrophoretic characterization of Inca peanut (Plukenetia volubilis L.) proteins. Plant Foods Hum. Nutr. 67(3): 247-255.
Theerakarunwong, P., P. Sanporkha, C. Hattakosol and N. Laohakulchit. 2021. Effect of flavozyme concentration and degradation time on chemical properties-physics of protein hydrolyzate from sacha inchi meal. Prawarun Agr. J. 18(2): 69-79. [in Thai]
Udenigwe, C.C. and R.E. Aluko. 2011. Chemometric analysis of the amino acid requirements of antioxidant food protein hydrolysates. Int. J. Mol. Sci. 12(5): 3148-3161.
Wang, S., F. Zhu and Y. Kakuda. 2018. Sacha inchi (Plukenetia volubilis L.): Nutritional composition, biological activity, and uses. Food Chem. 265: 316-328.
Zheng, L., Y. Zhao, C. Xiao, D. Sun-Waterhouse, M. Zhao and G. Su. 2015. Mechanism of the discrepancy in the enzymatic hydrolysis efficiency between defatted peanut flour and peanut protein isolate by flavorzyme. Food Chem. 168: 100-106.
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