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KMID : 1161420160190020187
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Journal of Medicinal Food
2016 Volume.19 No. 2 p.187 ~ p.195
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Potential Therapeutic Applications of Mucuna pruriens Peptide Fractions Purified by High-Performance Liquid Chromatography as Angiotensin-Converting Enzyme Inhibitors, Antioxidants, Antithrombotic and Hypocholesterolemic Agents
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Herrera-Chale Francisco
Ruiz-Ruiz Jorge Carlos
Betancur-Ancona David
Segura-Campos Maira Rubi
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Abstract
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A Mucuna pruriens protein concentrate was hydrolyzed with a digestive (pepsin?pancreatin) enzymatic system. The soluble portion of the hydrolysate was fractionated by ultrafiltration and the ultrafiltered peptide fraction (PF) with lower molecular weight was purified by reversed-phase high-performance liquid chromatography. The PF obtained were evaluated by testing the biological activity in vitro. Fractions showed that the ability to inhibit the angiotensin-converting enzyme had IC50 values that ranged from 2.7 to 6.2 μg/mL. Trolox equivalent antioxidant capacity values ranged from 132.20 to 507.43?mM/mg. The inhibition of human platelet aggregation ranged from 1.59% to 11.11%, and the inhibition of cholesterol micellar solubility ranged from 0.24% to 0.47%. Hydrophobicity, size, and amino acid sequence could be factors in determining the biological activity of peptides contained in fractions. This is the first report that M. pruriens peptides act as antihypertensives, antioxidants, and inhibitors for human platelet aggregation and cholesterol micellar solubility in vitro.
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KEYWORD
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biological activity, Mucuna pruriens, peptide fractions, protein hydrolysate, purification
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