Potential Therapeutic Applications ofMucuna pruriensPeptide Fractions Purified by High-Performance Liquid Chromatography as Angiotensin-Converting Enzyme Inhibitors, Antioxidants, Antithrombotic and Hypocholesterolemic Agents

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.

Peptides from Mucuna pruriens L., with protection and antioxidant in vitro effect on HeLa cell line

“…These results are similar to those of Gallegos et al ., who affirmed that antioxidant activity is higher in the lower size fractions, compared with the higher size, and is attributed to the presence of aromatic amino acids, as also indicated by Herrera‐Chalé et al . Likewise, the ultrafiltered fractions with the lowest protein content presented the highest antioxidant response and with statistically significant differences relative to the other compounds.…”

“…These results are similar to those of Gallegos et al, 31 who affirmed that antioxidant activity is higher in the lower size fractions, compared with the higher size, and is attributed to the presence of aromatic amino acids, as also indicated by Herrera-Chalé et al 32 Likewise, the ultrafiltered fractions with the lowest protein content presented the highest antioxidant response and with statistically significant differences relative to the other compounds. Herrera Chalé et al 8 evaluated the antioxidant activity of the protein derivatives from M. pruriens L. and found that F<1 kDa and F1-3 kDa had a higher activity (709 mmol L −1 mg −1 and 537 mmol L −1 mg −1 respectively) than the total hydrolysate and the larger fractions F5-10 kDa and F-10 kDa (102 mmol L −1 mg −1 , 222 mmol L −1 mg −1 , and 10.12 mmol L −1 mg −1 respectively).…”

“…The aromatic amino acid composition is known to be related to these biological activities . It is assumed that because pepsin and pancreatin are proteolytic enzymes that act on aromatic amino acid residues, the lower molecular weight fractions contain a representative number of these amino acids …”

“…36 It is assumed that because pepsin and pancreatin are proteolytic enzymes that act on aromatic amino acid residues, the lower molecular weight fractions contain a representative number of these amino acids. 32 Udenigwe and Aluko 36 mentioned that protein hydrolysates have an important role in the modulation of the nuclear factor kappa B signaling pathways, apoptotic signals, and Bcl2 (important regulator of programmed cell death pathways) and protein phosphorylation. Chakrabarti et al 37 stated that a rice hydrolysate demonstrated a direct action on the reduction of ROS in hemp seed and cereal flour, and a protective effect on cell death.…”

Immunosuppressive effects of protein derivatives from Mucuna pruriens on a streptozotocin‐induced type 1 diabetes murine model

“…Of the wide range of legumes belonging to the family Febaceae, Mucuna pruriens , known as velvet bean, stands out for its high protein content (20%–35%) in its seeds (Brunner, Beaver, & Flores, ). Previous research studies done in protein hydrolysates and peptide fractions of M. pruriens showed effects on inhibition of angiotensin‐converting enzyme, hypotensive, and antioxidant activities (Herrera‐Chalé, Ruiz‐Ruiz, Betancur‐Ancona, & Segura‐Campos, ); moreover, small‐sized peptide fractions such as 3–5 and 1–3 kDa have shown anti‐inflammatory activity decreasing the production of proinflammatory cytokines such as TNF‐α and IL‐6 on peritoneal murine macrophages. These results suggest protein hydrolysates and peptide fractions as possible nutraceuticals or alternative treatment for chronic non‐communicable disease such as TD1 (Martínez‐Leo, Arana‐Argáez, Acevedo‐Fernández, Moo‐Puc, & Segura‐Campos, ).…”