Identification of Bioactive Peptides with α-Amylase Inhibitory Potential from Enzymatic Protein Hydrolysates of Red Seaweed (Porphyra spp)

Abstract

Inhibition of α-amylase enzyme is one therapeutic approach in lowering glucose level in the blood to manage diabetes mellitus. In this study α-amylase inhibitory peptides were identified from proteolytic enzymes hydrolysates of red seaweed laver ( Porphyra species) using consecutive chromatographic techniques. In the resultant fractions from RP-HPLC (D-), D inhibited α-amylase activity (88.67 ± 1.05%) significantly ( p ≤ 0.5) at 1 mg/mL protein concentration. A mass spectrometry (ESI-Q-TOF- MS) analysis was used to identify peptides from this fraction. Two novel peptides were identified as Gly-Gly-Ser-Lys and Glu-Leu-Ser. To validate their α-amylase inhibitory activity, these peptides were synthesized chemically. The peptides were demonstrated inhibitory activity at IC value: 2.58 ± 0.08 mM (Gly-Gly-Ser-Lys) and 2.62 ± 0.05 mM (Glu-Leu-Ser). The inhibitory kinetics revealed that these peptides exhibited noncompetitive binding mode. Thus, laver can be a potential source of novel ingredients in food and pharmaceuticals in diabetes mellitus management.

Fractionation of hydrolysate from corn germ protein by ultrafiltration: In vitro antidiabetic and antioxidant activity

“…Another proposed inhibitory mechanism of biopeptides is the binding of peptides to the allosteric site of the enzyme in the enzyme structure (like calcium and chloride ion site) and create an unstable conformation. This conformation change can restrict the displacement of the enzyme on substrate (Admassu, Gasmalla, Yang, & Zhao, 2018; Siow & Gan, 2016). Calcium ions often have crucial roles in structure, function, and stability of α‐amylases, and the removal of calcium ions from some α‐amylase can inactivate the enzyme (Liao et al, 2019).…”

Health Functionality and Quality Control of Laver (Porphyra, Pyropia): Current Issues and Future Perspectives as an Edible Seaweed

“…Anti-cancer polysaccharides (dietary fiber, porphyran), phospholipids, sterol, peptide [17,[46][47][48][49][50][51][52][53][54] Prevention of cardiovascular disease (e.g., hypertension, atherosclerosis, ischemia) betaine, dietary fiber, taurine, porphyran [17,[55][56][57][58][59][60][61] Antioxidant effect (e.g., Anti-ageing) porphyran, glycoprotein, polyphenols, tocopherols, peptide [62][63][64][65][66][67] Anti-inflammatory effect and immunomodulation glycoprotein, porphyran [64,[68][69][70][71][72][73] Alcohol metabolism glycoprotein [74,75] Prevention of nervous diseases (e.g., Alzheimer's diseases, methylmalonic acidemias) taurine, porphyran [38,76,77] Prevention of bone disease (e.g., osteoporosis, rheumatoid arthritis) porphyran, glycoprotein [64,78] Anti-diabetes mellitus phenolic compounds (carotenoids, anthocyanins), polysaccharides (porphyran), peptide [79][80][81][82] Porphyran is the distinctive dietary fiber found in laver, and its health effects were intensively studied to determine the nutritional/functional quality of ...…”

Bioactive peptides with antidiabetic properties: a review

“…Admassu et al . () identified two α‐amylase inhibitory peptides, GGSK and ELS, from proteolytic enzymes hydrolysates of red seaweed laver ( Porphyra species). After chemical synthesis, the two peptides still exhibited inhibitory activity, with IC 50 values of 2.58 ± 0.08 m m for GGSK and 2.62 ± 0.05 m m for ELS.…”

“…A combined bioinformatics approach using Peptide Ranker and Pepsite2 software was employed by Evaristus et al (2018) to effectively identify a-amylase inhibitory peptides, with twenty from Nephelium mutabile seed proteins. Admassu et al (2018) identified two a-amylase inhibitory peptides, GGSK and ELS, from proteolytic enzymes hydrolysates of red seaweed laver (Porphyra species). After chemical synthesis, the two peptides still exhibited inhibitory activity, with IC 50 values of 2.58 AE 0.08 mM for GGSK and 2.62 AE 0.05 mM for ELS.…”

“…Trp58, Trp59, Tyr62, Asp96, Arg195, Asp197, Glu233, His299, Asp300 and His305) and forming a sliding barrier that prevents the formation of an enzyme/substrate intermediate (Evaristus et al, 2018). Likely owing to differences in structural properties, including amino acid composition, hydrophobicity and position at the N-and C-terminal regions, the peptide GGSK demonstrates mixed inhibition, whereas the other peptide (ELS) exhibits non-competitive inhibition (Admassu et al, 2018). Using a similar mechanism, the bioactive peptides extracted from pinto beans interact or bind to the active domain, ultimately restricting protein conformation and affecting the degree of enclosure of the substrate by the enzyme (Ngoh et al, 2017).…”