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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

Journal of Medicinal Food 2016년 19권 2호 p.187 ~ 195
Herrera-Chale Francisco, Ruiz-Ruiz Jorge Carlos, Betancur-Ancona David, Segura-Campos Maira Rubi,
소속 상세정보
 ( Herrera-Chale Francisco ) - Autonomous University of Yucatan Faculty of Chemical Engineering
 ( Ruiz-Ruiz Jorge Carlos ) - Institute of Technology of Merida Department of Chemical-Biochemical Engineering
 ( Betancur-Ancona David ) - Autonomous University of Yucatan Faculty of Chemical Engineering
 ( Segura-Campos Maira Rubi ) - Autonomous University of Yucatan Faculty of Chemical Engineering

Abstract


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.

키워드

biological activity; Mucuna pruriens; peptide fractions; protein hydrolysate; purification

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