Investigation on antioxidant, angiotensin converting enzyme and dipeptidyl peptidase IV inhibitory activity of Bambara bean protein hydrolysates

Mune, Martin Alain Mune; Minka, Samuel René; Henle, Thomas

doi:10.1016/j.foodchem.2018.01.001

Cited by 82 publications

(42 citation statements)

References 36 publications

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“…The peptide IPQVS contained Pro as the second N-terminal amino acid residue, indicating greatly probable DPP-IV-inhibitory activity . On the basis of the DPP-IV-inhibitory activity of IPQVS being higher than that of MPGPS (Table ), the first amino acid residue at the N-terminus may also affect the DPP-IV-inhibitory activity of the peptide with the same Pro position . Significant differences ( P < 0.05) were observed for the DPP-IV IC 50 values of the peptides HQEEPL and ELHQEEPL (>200 and 78.46 ± 4.94 μM, respectively).…”

Section: Resultsmentioning

confidence: 97%

Identification and Quantification of DPP-IV-Inhibitory Peptides from Hydrolyzed-Rapeseed-Protein-Derived Napin with Analysis of the Interactions between Key Residues and Protein Domains

Yao

et al. 2019

J. Agric. Food Chem.

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Previously reported peptides derived from napin of rapeseed (Brassica napus) have been shown to inhibit DPP-IV in silico. In the present study, napin extracted from rapeseed was hydrolyzed by commercial enzymes and filtered by an ultrafiltration membrane. The napin hydrolysate was then purified by a Sephadex G-15 gel-filtration column and preparative RP-HPLC. A two-enzyme-combination approach with alcalase and trypsin was the most favorable in terms of the DPP-IVinhibitory activity (IC 50 = 0.68 mg/mL) of the napin hydrolysate. Three peptides and one modified peptide (pyroglutamate mutation at the N-terminus) were identified using HPLC-triple-TOF-MS/MS. DPP-IV-inhibitory activity and the types of enzyme inhibition were also determined. Meanwhile, key residues associated with the interactions between the selected peptides and DPP-IV were investigated by molecular docking. IPQVS has key amino acid residues (Tyr547, Glu205, and Glu206) that are consistent with Diprotin A. ELHQEEPL could form a better covalent bond with Arg358 in the S3 pocket of DPP-IV.

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Section: Resultsmentioning

confidence: 97%

Identification and Quantification of DPP-IV-Inhibitory Peptides from Hydrolyzed-Rapeseed-Protein-Derived Napin with Analysis of the Interactions between Key Residues and Protein Domains

Yao

et al. 2019

J. Agric. Food Chem.

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“…Using the in silico peptide prediction approach, investigators have predicted DPP-IV inhibitory peptides in food protein precursors including silver carp proteins, sodium caseinate hydrolysates, α-lactalbumin, yam dioscorin hydrolysates, β-lactoglobulin hydrolysates, and bambara bean protein hydrolysates [43,64,65,66,67,68].…”

Section: Methods For Discovering Food-derived Dpp-iv Inhibitory Pementioning

confidence: 99%

Discovery of Food-Derived Dipeptidyl Peptidase IV Inhibitory Peptides: A Review

Liu

Cheng

2019

IJMS

119

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Diabetes is a chronic metabolic disorder which leads to high blood sugar levels over a prolonged period. Type 2 diabetes mellitus (T2DM) is the most common form of diabetes and results from the body’s ineffective use of insulin. Over ten dipeptidyl peptidase IV (DPP-IV) inhibitory drugs have been developed and marketed around the world in the past decade. However, owing to the reported adverse effects of the synthetic DPP-IV inhibitors, attempts have been made to find DPP-IV inhibitors from natural sources. Food-derived components, such as protein hydrolysates (peptides), have been suggested as potential DPP-IV inhibitors which can help manage blood glucose levels. This review focuses on the methods of discovery of food-derived DPP-IV inhibitory peptides, including fractionation and purification approaches, in silico analysis methods, in vivo studies, and the bioavailability of these food-derived peptides. Moreover, food-derived DPP-IV inhibitory peptides discovered during this decade are listed and distributed in a 3D scatter plot graph based on their IC50, molecular weight, and grand average of hydropathicity values, which can help us to understand the relationship between the features of the peptides and their activities.

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“…The performance of enzymatic hydrolysis to produce bioactive peptides will be discussed in this section. Generation of DPP-IV inhibitory peptides from food proteins can be achieved using a single protease or multiple enzymes obtained from plants (e.g., papain) [49,79,89,90], animals (e.g., pepsin, trypsin, and Corolase PP) [2,3,35,81], or microorganisms (e.g., alcalase, protamex, and flavourzyme) [9,[91][92][93]. Each protease requires the provision of specific conditions (e.g., pH and temperature, enzyme/substrate ratio, and hydrolysis time) to optimize hydrolysis efficiency or the DPP-IV inhibitory effect of hydrolysate.…”

Section: Enzymatic Hydrolysates Of Food Proteinsmentioning

confidence: 99%

Characteristics of Food Protein-Derived Antidiabetic Bioactive Peptides: A Literature Update

Nong

Hsu

2021

IJMS

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Diabetes, a glucose metabolic disorder, is considered one of the biggest challenges associated with a complex complication of health crises in the modern lifestyle. Inhibition or reduction of the dipeptidyl peptidase IV (DPP-IV), alpha-glucosidase, and protein-tyrosine phosphatase 1B (PTP-1B) enzyme activities or expressions are notably considered as the promising therapeutic strategies for the management of type 2 diabetes (T2D). Various food protein-derived antidiabetic bioactive peptides have been isolated and verified. This review provides an overview of the DPP-IV, PTP-1B, and α-glucosidase inhibitors, and updates on the methods for the discovery of DPP-IV inhibitory peptides released from food-protein hydrolysate. The finding of novel bioactive peptides involves studies about the strategy of separation fractionation, the identification of peptide sequences, and the evaluation of peptide characteristics in vitro, in silico, in situ, and in vivo. The potential of bioactive peptides suggests useful applications in the prevention and management of diabetes. Furthermore, evidence of clinical studies is necessary for the validation of these peptides’ efficiencies before commercial applications.

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Investigation on antioxidant, angiotensin converting enzyme and dipeptidyl peptidase IV inhibitory activity of Bambara bean protein hydrolysates

Cited by 82 publications

References 36 publications

Identification and Quantification of DPP-IV-Inhibitory Peptides from Hydrolyzed-Rapeseed-Protein-Derived Napin with Analysis of the Interactions between Key Residues and Protein Domains

Identification and Quantification of DPP-IV-Inhibitory Peptides from Hydrolyzed-Rapeseed-Protein-Derived Napin with Analysis of the Interactions between Key Residues and Protein Domains

Discovery of Food-Derived Dipeptidyl Peptidase IV Inhibitory Peptides: A Review

Characteristics of Food Protein-Derived Antidiabetic Bioactive Peptides: A Literature Update

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