Antioxidant and enzyme inhibitory properties of sacha inchi ( Plukenetia volubilis ) protein hydrolysate and its peptide fractions

Abstract

The objective of this study was to determine the in vitro activities such as antioxidant and inhibitions of angiotensin converting enzyme, dipeptidyl peptidase‐IV, prolyl oligopeptidase, and 3‐hydroxy‐3‐methyl‐glutaryl‐coenzyme A reductase of sacha inchi protein hydrolysate (SPH) and its membrane ultrafiltration peptide fractions. SPH was prepared after hydrolysis of sacha inchi protein using papain followed by separation into peptide fractions (F1: <1 kDa, F2: 1–3 kDa, F3: 3–5 kDa, and F4: 5–10 kDa) via ultrafiltration membranes. SPH and the peptide fractions were tested for multifunctional properties, specifically functional ability as antioxidants and enzyme inhibitors. Surface hydrophobicity was an important contributing factor to the activity of antioxidative peptides. The DPPH inhibitory activity of F4 was significantly higher (p < .05) than activities of the SPH and other fractions. The smaller peptides with <1 kDa size (F1) showed the most potent (p < .05) antioxidant properties based on the stronger scavenging of ABTS, DPPH, and superoxide radicals in addition to better attenuation of linoleic acid peroxidation. Moreover, the F1 was also the strongest inhibitor of angiotensin converting enzyme, dipeptidyl peptidase‐IV, prolyl oligopeptidase inhibition, and 3‐hydroxy‐3‐methyl‐glutaryl‐coenzyme A reductase based on the lower IC50 values. It was concluded that the smaller size of the F1 peptides was the main determinant of its strong antioxidant and enzyme inhibition potency, which could be taken as an advantage to formulate functional foods and nutraceuticals with potential activities in ameliorating some of the chronic human diseases. Practical applications The results of present study indicate that SPH and its ultrafiltration fractions are potential sources of antihypertensive, antidiabetic, inhibition of POP, reduced cholesterol, and strong antioxidant peptides. The strong angiotensin converting enzyme, dipeptidyl peptidase‐IV, prolyl oligopeptidase inhibition, and 3‐hydroxy‐3‐methyl‐glutaryl‐coenzyme inhibitory efficiency of the F1 peptides (MW < 1 kDa) suggest potential utility as an antihypertensive, antidiabetic agent, reduce cholesterol and brain plasticity and memory formation because the small peptide size could enhance absorption from the gastrointestinal tract. Overall, results from this study indicate that SPH, especially the F1 peptides may have applications as ingredients for the formulation of functional foods and nutraceuticals.

Protective effect of antioxidant peptides from bass (Lateolabrax japonicus) on oxidative stress injury in Caco‐2 cells

“…At the same time, it was also a component amino acid of the endogenous antioxidant GSH, which played an important role in the antioxidant system of the body. In addition, the classification of amino acids showed that LPH contained a significant number of hydrophobic amino acids (HAAs), which accounted for 27.2% of the total It is reported that peptides’ solubility in lipids may be increased by the presence of HAAs, which could facilitate their entry into target organs and thus increase the antioxidant activity in vitro (Suwanangul et al., 2022). In addition, acidic amino acids and basic amino acids with high content in LPH could play an antioxidant role by chelating metal ions and scavenging free radicals, respectively (Phongthai & Rawdkuen, 2020).…”

Isolation and identification of dipeptidyl peptidase‐IV inhibitory peptides from Sacha inchi meal

“…Protein hydrolysates are defined as a complex mixture of peptides and free amino acids produced by enzymatic hydrolysis, which increases the bioavailability of proteins and reduces the immunoreactivity of native proteins 8 . Studies reported that enzymatically hydrolyzed Sacha inchi protein has antioxidant, antihypertensive, enzyme inhibition (α‐amylase, α‐glucosidase and pancreatic lipase) activities 9,10 . Inspired by diabetes‐related enzyme (α‐amylase and α‐glucosidase) inhibitory activities, it is speculated that SIM hydrolysate may also have inhibitory activity on DPP‐IV, which is also an important enzyme related to diabetes.…”

“…8 Studies reported that enzymatically hydrolyzed Sacha inchi protein has antioxidant, antihypertensive, enzyme inhibition (⊍-amylase, ⊍-glucosidase and pancreatic lipase) activities. 9,10 Inspired by diabetes-related enzyme (⊍-amylase and ⊍-glucosidase) inhibitory activities, it is speculated that SIM hydrolysate may also have inhibitory activity on DPP-IV, which is also an important enzyme related to diabetes. As expected, in previous studies, 11 we employed proteases to hydrolyze SIM protein, and found that the hydrolysates exhibited DPP-IV inhibition activity.…”

Purification and Identification of Novel Antioxidant Peptides from Hydrolysates of Peanuts (Arachis hypogaea) and Their Neuroprotective Activities

“…Studies have explored the antioxidant properties of protein hydrolysates or bioactive peptides from plant sources . Enzymes, such as pepsin, papain, and flavorzyme, were used to produce sacha inchi (Plukenetia volubilis L.) protein hydrolysates, of which the pepsin hydrolysate showed the highest hydrolysis degree and antioxidant activity . The alkaline protein hydrolysate of golden melon (Cucurbita pepo L. var.…”