Global Advanced Research Journal of Medicine and Medical Sciences (GARJMMS) ISSN: 2315-5159
November 2018, Vol. 7(9), pp. 190-201
Copyright © 2018 Global Advanced Research Journals
Full Length Research Article
Moringa oleifera Seed Protein Hydrolysates: Kinetics of α-amylase Inhibition and Antioxidant Potentials
Olusola A. O.*, Ekun O. E., David T. I., Olorunfemi O. E. and Oyewale M. B.
Department of Biochemistry, Faculty of Science, Adekunle Ajasin University, Akungba-Akoko, Nigeria.
Accepted 25 November, 2018
Proteins from n-hexane - treated Moringa oleifera seed flour were isolated using alkaline solubilization followed by acid-induced precipitation. Two proteolytic enzymes, pepsin and trypsin were used to hydrolyze the protein isolates. The resulting hydrolysates were then evaluated for α-amylase inhibitory properties and kinetics as well as antioxidant activities against superoxide radicals and ferric ions. With the use of starch as substrate, the hydrolysates demonstrated a concentration-dependent inhibition of α-amylase with peptic hydrolysates exhibiting 77.591±0.173% and tryptic hydrolysates demonstrating 84.183±1.670% inhibition (IC50 = 0.547 mg/ml to 0.591 mg/ml). Kinetic data showed an uncompetitive subtype of mixed inhibition for peptic hydrolysates and an uncompetitive mode for tryptic hydrolysates, with ki, of 0.166 mg/ml and 0.179mg/ml for peptic and tryptic hydrolysates respectively. Antioxidant assays using superoxide radicals and ferric ions indicated that tryptic hydrolysates had higher scavenging activitiy while peptic hydrolysates possessed higher ferric reducing power. These results suggest that Moringa oleifera seed proteins may contain biologically active peptide sequences which could be harnessed for the formulation of new additives to food and for development of novel anti-diabetic agents.
Keywords: Moringa oleifera, hydrolysates, pepsin, trypsin, α-amylase inhibition, antioxidant potentials.
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