Greek oregano (Origanum vulgare), marjoram (Origanum majorana), rosemary (Rosmarinus officinalis), and Mexican oregano (Lippia graveolens) are concentrated sources of bioactive compounds. The aims were to characterize and examine extracts from greenhouse-grown or commercially purchased herbs for their ability to inhibit dipeptidyl peptidase IV (DPP-IV) and protein tyrosine phosphatase 1B (PTP1B), enzymes that play a role in insulin secretion and insulin signaling, respectively. Greenhouse herbs contained more polyphenols (302.7-430.1 μg of gallic acid equivalents/mg of dry weight of extract (DWE)) and flavonoids (370.1-661.4 μg of rutin equivalents/mg of DWE) compared to the equivalent commercial herbs. Greenhouse rosemary, Mexican oregano, and marjoram extracts were the best inhibitors of DPP-IV (IC₅₀=16, 29, and 59 μM, respectively). Commercial rosemary, Mexican oregano, and marjoram were the best inhibitors of PTP1B (32.4-40.9% at 500 μM). The phytochemicals eriodictyol, naringenin, hispidulin, cirsimaritin, and carnosol were identified by LC-ESI-MS as being present in greenhouse-grown Mexican oregano and rosemary. Computational modeling indicated that hispidulin, carnosol, and eriodictyol would have the best binding affinities for DPP-IV. Biochemically, the best inhibitors of DPP-IV were cirsimaritin (IC₅₀=0.43±0.07 μM), hispidulin (IC₅₀=0.49±0.06 μM), and naringenin (IC₅₀=2.5±0.29 μM). Overall, herbs contain several flavonoids that inhibit DPP-IV and should be investigated further regarding their potential in diabetes management.
The aim of this study was to evaluate the effect of germination and alcalase hydrolysis of common bean proteins on the generation of bioactive peptides with potential to reduce parameters related to the risk of developing type-2 diabetes (T2D) in vitro. Germination (25°C up to 72 h) and alcalase hydrolysis (up to 4 h) produced peptides with high antioxidant capacity (1085 μmol TE/g soluble protein, SP). After 24 h of germination, there was an increase of 44% in α-amylase inhibitory capacity of the peptides relative to acarbose (1 mM). Simulated gastrointestinal digestion of the non-germinated and non-hydrolyzed sample (G0-0h) produced bioactive peptides that inhibited dipeptidyl peptidase-IV (DPP-IV) (IC 50 = 1.2 mg SP/mL); however, the IC 50 was not improved by either germination or alcalase hydrolysis. Insulin secretion by glucose stimulated (20 mM) INS-1E pancreatic β-cells, increased 45% from the basal state with 2 mg SP/mL of G0-0h. Germination did not improve the stimulation of insulin. Computational modeling showed that the peptide RGPLVNPDPKPFL obtained after 48 h germination and 1 h alcalasehydrolysis was able to inhibit DPP-IV by interacting with its S1, S2, and S3 pockets of the active site. Germination and alcalase hydrolysis can be applied to improve some markers related to the management of T2D. Furthermore, simulated gastrointestinal digestion of common bean proteins without any treatment produced bioactive peptides with the ability to inhibit DPP-IV, resulting in increased insulin released from pancreatic cells in vitro.
Chickpeas are inexpensive, protein rich (approximately 20% dry mass) pulses available worldwide whose consumption has been correlated with positive health outcomes. Dietary peptides are important molecules derived from dietary proteins, but a comprehensive analysis of the peptides that can be produced from chickpea proteins is missing in the literature. This review provides information from the past 20 years on the enzymatic production of peptides from chickpea proteins, the reported bioactivities of chickpea protein hydrolysates and peptides, and the potential bitterness of chickpea peptides in food products. Chickpea peptides have been enzymatically produced with pepsin, trypsin, chymotrypsin, alcalase, flavorzyme, and papain either alone or in combination, but the sequences of many of the peptides in chickpea protein hydrolysates remain unknown. In addition, a theoretical hydrolysis of chickpea legumin by stem bromelain and ficin was performed by the authors to highlight the potential use of these enzymes to produce bioactive chickpea peptides. Antioxidant activity, hypocholesterolemic, and angiotensin 1‐converting enzyme inhibition are the most studied bioactivities of chickpea protein hydrolysates and peptides, but anticarcinogenic, antimicrobial, and anti‐inflammatory effects have also been reported for chickpea protein hydrolysates and peptides. Chickpea bioactive peptides are not currently commercialized, but their bitterness could be a major impediment to their incorporation in food products. Use of flavorzyme in the production of chickpea protein hydrolysates has been proposed to decrease their bitterness. Future research should focus on the optimization of chickpea bioactive peptide enzymatic production, studying the bioactivity of chickpea peptides in humans, and systematically analyzing chickpea peptide bitterness.
The objective of this study was to investigate the biochemical antioxidant potential of peptides derived from enzymatically hydrolyzed mung bean (Vigna radiata) albumins using an 2,2′-Azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) (ABTS) radical scavenging assay, a ferrous ion chelating assay and an oxygen radical absorbance capacity (ORAC) assay. Peeled raw mung bean was ground into flour and mixed with buffer (pH 8.3, 1:20 w/v ratio) before being stirred, then filtered using 3 kDa and 30 kDa molecular weight cut-off (MWCO) centrifugal filters to obtain albumin fraction. The albumin fraction then underwent enzymatic hydrolysis using either gastrointestinal enzymes (pepsin and pancreatin) or thermolysin. Peptides in the hydrolysates were sequenced. The peptides showed low ABTS radical-scavenging activity (90–100 μg ascorbic acid equivalent/mL) but high ferrous ion chelating activity (1400–1500 μg EDTA equivalent/mL) and ORAC values (>120 μM Trolox equivalent). The ferrous ion chelating activity was enzyme- and hydrolysis time-dependent. For thermolysin hydrolysis, there was a drastic increase in ferrous ion chelating activity from t = 0 (886.9 μg EDTA equivalent/mL) to t = 5 min (1559.1 μg EDTA equivalent/mL) before plateauing. For pepsin–pancreatin hydrolysis, there was a drastic decrease from t = 0 (878.3 μg EDTA equivalent/mL) to t = 15 (138.0 μg EDTA equivalent/mL) after pepsin was added, but this increased from t = 0 (131.1 μg EDTA equivalent/mL) to t = 15 (1439.2 μg EDTA equivalent/mL) after pancreatin was added. There was no significant change in ABTS radical scavenging activity or ORAC values throughout different hydrolysis times for either the thermolysin or pepsin–pancreatin hydrolysis. Overall, mung bean hydrolysates produced peptides with high potential antioxidant capacity, being particularly effective ferrous ion chelators. Other antioxidant assays that use cellular lines should be performed to measure antioxidant capacity before animal and human studies.
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