ACE-inhibitory Activity Research Articles

Identification and Molecular Docking Analysis of Angiotensin-Converting Enzyme Inhibitors from Finger Millet (Eleusine coracana).

Hypertension remains a significant global health concern, contributing significantly to cardiovascular diseases and mortality rates. The inhibition of angiotensin-converting enzyme (ACE) plays a crucial role in alleviating high blood pressure. We investigated the potential of finger millets (Eleusine coracana) as a natural remedy for hypertension by isolating and characterizing its ACE-inhibitory compound. First, we evaluated the ACE-inhibitory activity of the finger millet ethanol extract and subsequently proceeded with solvent fractionation. Among the solvent fractions, the ethyl acetate fraction exhibited the highest ACE inhibitory activity and was further fractionated. Using preparative high-performance liquid chromatography, the ethyl acetate fraction was separated into four subfractions, with fraction 2 (F2) exhibiting the highest ACE inhibitory activity. Subsequent 1H-nuclear magnetic resonance (NMR) and 13C-NMR analyses confirmed that the isolated compound from F2 was catechin. Furthermore, molecular docking studies indicated that catechin has the potential to act as an ACE inhibitor. These findings suggest that finger millets, particularly as a source of catechin, have the potential to be used as a natural antihypertensive.

Two Novel Angiotensin-Converting Enzyme (ACE) Inhibitory and ACE2 Upregulating Peptides from the Hydrolysate of Pumpkin (Cucurbita moschata) Seed Meal.

Pumpkin (Cucurbita moschata) seed meal (PSM), the major byproduct of pumpkin seed oil industry, was used to prepare angiotensin-converting enzyme (ACE) inhibitory and angiotensin-converting enzyme 2 (ACE2) upregulating peptides. These peptides were isolated and purified from the PSM hydrolysate prepared using Neutrase 5.0 BG by ultrafiltration, Sephadex G-15 column chromatography, and reversed-phase high-performance liquid chromatography. Two peptides with significant ACE inhibition activity were identified as SNHANQLDFHP and PVQVLASAYR with IC50 values of 172.07 and 90.69 μM, respectively. The C-terminal tripeptides of the two peptides contained Pro, Phe, and Tyr, respectively, and PVQVLASAYR also had Val in its N-terminal tripeptide, which was a favorable structure for ACE inhibition. Molecular docking results declared that the two peptides could interact with ACE through hydrogen bonds and hydrophobic interactions. Furthermore, the two peptides performed protective function on EA.hy926 cells by decreasing the secretion of endothelin-1, increasing the release of nitric oxide, and regulating the ACE2 activity. In vitro simulated gastrointestinal digestion showed the two peptides exhibited good stability against gastrointestinal enzyme digestion. In conclusion, PSM is a promising material for preparing antihypertensive peptides.

Peptide Inhibitors of Angiotensin-I Converting Enzyme (ACE) Bioavailability in Legumes Subjected to Hydrothermal Treatment

The objective of this study was to evaluate the effect of Angiotensin-I Converting Enzyme (ACE) inhibitory peptides derived from five legumes (Vigna unguiculata, Cicer arietinum, Lens culinaris, Vicia faba, and Phaseolus vulgaris) after undergoing a hydrothermal treatment. The seeds were divided into two groups: one was subjected to drying and grinding, and the other one to cooking for 2 hours (100 °C), followed by drying and grinding. The flours obtained from the different processes were subjected to digestion with pepsin-pancreatin, and the resulting peptides were evaluated for their ACE inhibitory activity. The obtained results were subjected to analysis of variance and Tukey's test. The group consisting of the treatments V. unguiculata (82.63%), V. unguiculata cooked (96.41%), and C. arietinum (80.84%) showed the highest percentages of ACE inhibition, while the group comprising V. faba (6.0%), cooked L. culinaris (3.03%), and P. vulgaris (4.0%) exhibited the lowest inhibition percentages. These results demonstrate that V. unguiculata, V. faba, and C. arietinum can undergo hydrothermal treatment while still retaining their bioactive potential, ensuring a cooked flour, ready for formulating a multifunctional food.

Study on the Digestion-Induced Changes in the Characteristics and Bioactivity of Korean Native and Overseas Cattle-Derived Peptides.

This study was conducted to compare and analyze the changes in the biochemical characteristics and biological activity of peptide extracts derived from Chickso, Hanwoo, and Wagyu beef during digestion. The results of the in vitro digestion analysis revealed that the digestion rate, total free amino acid content, and antioxidant and antihypertensive activities of Chickso loin and shank myofibrillar proteins were significantly higher (p<0.05) than those of Hanwoo and Wagyu loin and shank myofibrillar proteins. Particularly, the peptide extracts of Chickso loin and shank had a high angiotensin-converting enzyme inhibitory activity. In mice in vivo digestion experiment, the blood serum of mice fed with Chickso loin peptide extract (<10 kDa) showed the highest antioxidant enzyme activity. Thus, Chickso peptide extracts were deemed to be similar or more bioactive than Hanwoo and Wagyu peptide extracts, and can be used as bioactive materials.

A combined in vitro and in silico study of the inhibitory mechanism of angiotensin-converting enzyme with peanut peptides

Food-derived peptides with low molecular weight, high bioavailability, and good absorptivity have been exploited as angiotensin-converting enzyme (ACE) inhibitors. In the present study, in-vitro inhibition kinetics of peanut peptides, in silico screening, validation of ACE inhibitory activity, molecular dynamics (MD) simulations, and HUVEC cells were performed to systematically identify the inhibitory mechanism of ACE interacting with peanut peptides. The results indicate that FPHPP, FPHY, and FPHFD peptides have good thermal, pH, and digestive stability. MD trajectories elucidate the dynamic correlation between peptides and ACE and verify the specific binding interaction. Noteworthily, FPHPP is the best inhibitor with a strongest binding affinity and significantly increases NO, SOD production, and AT2R expression, and decreases ROS, MDA, ET-1 levels, ACE, and AT1R accumulation in Ang II-injury HUVEC cells.

Novel Blood Pressure-Lowering Effect of Spathulenol in Rats

In recent years, natural compounds from plant sources are sought after as alternative anti-hypertensive treatments. Spathulenol (Spa), a terpenoid plant metabolite obtained mainly from the Origanum species has shown anecdotal evidence of blood pressure (BP)-lowering properties probably through the effects on vasoreactivity. This study aimed to investigate the BP-lowering activities of Spa in vivo as well as to ascertain the mechanisms of action in vitro. Male Sprague-Dawley (SD) rats (n=16) and spontaneously hypertensive rats (SHR) (n=16) with their normotensive Wistar-Kyoto (WKY) rats (n=16) as controls were subjected to anaesthesia and administered intravenous boluses of Spa at 0.0, 0.045, 0.90, 0.18, 0.36, and 0.7 mg/kg or positive control losartan at 0.0, 0.6, 1.2, 1.8, 2.4 and 3.0 mg/kg. The BP and heart rate (HR) of the rats were recorded by a computerised physiographical system (Power Lab) through carotid arterial cannulation that was connected to a pressure transducer. The data were analysed by using the Lab Chart 6 software. Spathulenol was also tested for angiotensin-converting enzyme (ACE) inhibitory activity by using the ACE1 inhibitor screening kit (PromoKine). Spathulenol was able to decrease the BP of rats in a dose-dependent manner with the BP-lowering effect being significantly (p &lt; 0.05) higher in the SHRs than in the WKY controls. Furthermore, Spa was able to inhibit the ACE activity suggesting the possibility that this could be one of the mechanisms underlying the observed BP-lowering effect.

Peptidomics-based identification of antihypertensive and antidiabetic peptides from sheep milk fermented using Limosilactobacillus fermentum KGL4 MTCC 25515 with anti-inflammatory activity: in silico, in vitro, and molecular docking studies.

This study investigated the synthesis of bioactive peptides from sheep milk through fermentation with Limosilactobacillus fermentum KGL4 MTCC 25515 strain and assessed lipase inhibition, ACE inhibition, α-glucosidase inhibition, and α-amylase inhibition activities during the fermentation process. The study observed the highest activities, reaching 74.82%, 70.02%, 72.19%, and 67.08% (lipase inhibition, ACE inhibition, α-glucosidase inhibition, and α-amylase inhibition) after 48h at 37°C, respectively. Growth optimization experiments revealed that a 2.5% inoculation rate after 48h of fermentation time resulted in the highest proteolytic activity at 9.88mg/mL. Additionally, fractions with less than 3kDa of molecular weight exhibited superior ACE-inhibition and anti-diabetic activities compared to other fractions. Fermentation of sheep milk with KGL4 led to a significant reduction in the excessive production of NO, TNF-α, IL-6, and IL-1β produced in RAW 267.4 cells upon treatment with LPS. Peptides were purified utilizing SDS-PAGE and electrophoresis on 2D gels, identifying a maximum number of proteins bands ranging 10-70kDa. Peptide sequences were cross-referenced with AHTPDB and BIOPEP databases, confirming potential antihypertensive and antidiabetic properties. Notably, the peptide (GPFPILV) exhibited the highest HPEPDOCK score against both α-amylase and ACE.

STUDY OF ANGIOTENSIN-I CONVERTING ENZYME INHIBITORY PEPTIDES DERIVED FROM Ficus pumila var. awkeotsang SEEDS HYDROLYSATE

Hypertension also known as high blood pressure that has associated with multi-metabolic pathways such as the renin-angiotensin-aldosterone system (RAAS). There have been several synthetic ACE inhibitory drugs used clinically as therapeutics for hypertension. However, synthetic drugs showed side effects on human health after long-term use. Therefore, alternative natural ACE inhibitors from food-derived are necessary to develop. The study aimed to examine the activity of angiotensin-I converting enzyme inhibitory peptides derived from Ficus pumila var. awkeotsang seeds hydrolysate and to study the efficiency of enzymatic digestion. This study used four enzymes (trypsin, pepsin, thermolysin, and chymotrypsin) to release bioactive peptides from Ficus pumila var. awkeotsang seeds that could exhibit an antihypertensive effect. The results showed that Ficus pumila var. awkeotsang trypsin hydrolysate has the highest ACEI activity, 90.37%, and the IC50 reached 169±3.5 µg/mL. Then, the hydrolysate produced by trypsin has the highest degree of hydrolysis, 4%, after 8 hours of incubation. Hence, Ficus pumila var. awkeotsang seeds hydrolysate could develop as an alternative natural product that is responsible for ACE-inhibitory activity.

Protein identification and potential bioactive peptides from pumpkin (Cucurbita maxima) seeds

AbstractPumpkin is an economically important crop all over the world. Approximately, 18%–21% of pumpkins, consisting of peels and seeds by‐products, are wasted during processing. In addition, the seeds are rich in protein and have the potency of bioactive peptide production. This study aims to recognize the proteins and investigate the potential bioactive peptides from pumpkin (Cucurbita maxima) seeds. Pumpkin seeds were subjected to hot air drying (HAD) at 55°C for 12 h and freeze‐drying (FD) at −80°C for 54 h before they were powdered, analyzed, and precipitated by isoelectric point to obtain pumpkin seed protein isolates (PSPI). PSPI comprised 11S globulin subunit beta, 2S seed storage albumin, and chaperonin CPN60‐1. To generate hydrolysate peptides, PSPI was hydrolyzed using papain, pepsin, and bromelain. FD group pepsin hydrolysates had the highest peptide content of 420.83 mg/g. ACE inhibition and DPP‐IV inhibition activity were analyzed for each enzymatic hydrolysate. The pepsin hydrolyzed sample exhibited the highest ACE inhibition of 70.26%, and the papain hydrolyzed sample exhibited the highest DPP‐IV inhibition of 30.51%. The simulated gastrointestinal digestion (SGID) conducted by pepsin and pancreatin increased ACE inhibitory activity from 76.93% to 78.34%, and DPP‐IV inhibited activity increased from 58.62% to 77.13%. Pepsin and papain hydrolysates were fractionated using ultrafiltration to measure ACE and DPP‐IV inhibition activity. The highest free radical scavenging abilities were exhibited by the &lt;1 kDa hydrolysate fractions with 78.34% ACE inhibitory activities and 79.55% DPP‐IV inhibitory activities. This research revealed that pumpkin seeds had the potency to produce bioactive peptides.

Biological properties of LMW-peptide fractions from apricot kernel protein: Nutritional, antibacterial and ACE-inhibitory activities

In this study, angiotensin-converting enzyme (ACE) inhibitory, antioxidant and antibacterial activities, and nutritional quality of low molecular weights (LMWs) peptide fractions (PFs) from apricot-kernel (Prunus armeniaca cv. Tabarzeh) with PFs <3, 3–10, 10–30 and 30–100 kDa were investigated. The ratio of essential to total (E/T) amino acids (∼34.5 %) and PER value (1.8–1.9) indicated the high nutritional and digestibility of peptide fractions. Antioxidant indices were affected by enzymatic hydrolysis, molecular weight (Mw) and concentration of peptides. In general, the highest inhibition of DPPH− (89.2 %), ABTS+ (93.1 %), TEAC (2.52 mM), OH• (78.1 %), NO• (70.4 %), total antioxidant activity (2.01), reducing power (1.27), ACE inhibitory (75.1 %), chelation of Fe2+ (90.2 %) and Cu2+ (40.2 %) metal-ions were related to low Mw fractions (PF-3 and PF-10). The hydrolysates and primary protein showed enhanced antibacterial effects against Escherichia coli and Bacillus cereus with diameter of inhibition zones of 17 and 14 mm, respectively. Overall, apricot-kernel peptides can be considered as a nutrient source, natural antioxidant and preservative with ACE-inhibitory effect in dietary supplements and food formulations.

Two novel angiotensin-converting enzyme (ACE) and dipeptidyl peptidase IV (DPP-IV) inhibiting peptides from tilapia (Oreochromis mossambicus) skin and their molecular docking mechanism.

In the study, papain was used to hydrolyze tilapia (Oreochromis mossambicus) skin to obtain a tilapia skin hydrolysate (TSH) with dual angiotensin-converting enzyme (ACE) and dipeptidyl peptidase IV (DPP-IV) inhibitory activities. The resulting TSH was sequentially fractionated by ultrafiltration, size exclusion separation chromatography, and reverse-phase high-performance liquid chromatography. Its inhibitory effects on ACE and DPP-IV were determined by commercial reagent kits. Two peptides purified from TSH were identified as Gly-Pro-Leu-Gly-Ala-Leu (GPLGAL) and Lys-Pro-Ala-Gly-Asn (KPAGN) by the ultra-performance liquid chromatography-tandem mass spectrometry (UPLC-MS/MS). Inhibitory concentration (IC50) of GPLGAL on ACE and DPP-IV were 117.20±1.69 and 187.10±2.75µM, respectively. IC50 of KPAGN on ACE and DPP-IV were 137.40±2.33 and 259.20±2.85µM, respectively. The molecular simulation demonstrated that the binding affinities of GPLGAL to ACE and DPP-IV proteins were -8.5 and -7.4kcal/mol, respectively, whereas those of KPAGN to ACE and DPP-IV proteins were -7.9 and -6.7kcal/mol, respectively. GPLGAL interacted with 21 amino acid residues of the ACE active site, whereas KPAGN engaged with 19 amino acid residues. Additionally, GPLGAL interacted with 10 amino acid residues of the DPP-IV active site, whereas KPAGN engaged with 13 amino acid residues. The two peptides predominantly occupied the active sites of ACE (His513, Tyr523, and Ala354) and DPP-IV (Tyr662 and Arg125) through hydrogen bonding. This leads to the deactivation of ACE and DPP-IV. PRACTICAL APPLICATION: Accelerate tilapia skin development and high-value utilization; provide foundation for preparing the peptides with dual ACE and DPP-IV inhibiting activity.

Genotypic Profiling, Functional Analysis, Cholesterol-Lowering Ability, and Angiotensin I-Converting Enzyme (ACE) Inhibitory Activity of Probiotic Lactiplantibacillus plantarum K25 via Different Approaches.

Due to its alleged health advantages, several uses in biotechnology and food safety, the well-known probiotic strain Lactiplantibacillus plantarum K25 has drawn interest. This in-depth investigation explores the genetic diversity, makeup, and security characteristics of the microbial genome of L. plantarum K25, providing insightful knowledge about its genotypic profile and functional characteristics. Utilizing cutting-edge bioinformatics techniques like comparative genomics, pan-genomics, and genotypic profiling was carried out to reveal the strain's multidimensional potential in various fields. The results not only add to our understanding of the genetic makeup of L. plantarum K25 but also show off its acceptability in various fields, notably in biotechnology and food safety. The explanation of evolutionary links, which highlights L. plantarum K25's aptitude as a probiotic, is one notable finding from this research. Its safety profile, which is emphasized by the absence of genes linked to antibiotic resistance, is crucial and supports its status as a promising probiotic option.

Olive Pomace Extract Contains Low Molecular Weight Peptides and Possesses ACE Inhibitory Activity.

The aim of the present study was to determine the ACE inhibitory activity of aqueous extracts of olive pomace and to understand whether they represent a good source of bioactive LMW peptides for nutritional and pharmacological applications. We produced a water extract from olive pomace (var. Picual) and obtained its low molecular weight (LMW) fraction (<3 kDa). The calculated yield of extraction was 100.2 ± 7.9 mg of LMW peptides per 100 g of olive pomace. The olive pomace LMW fraction possessed strong ACE inhibitory activity (IC50 = 3.57 ± 0.22 µg prot/mL). The LMW fraction (<3 kDa) was analysed by nanoscale liquid chromatography-Orbitrap coupled with tandem mass spectrometry and de novo sequencing. Thirty new peptides, containing between 7-17 amino acids and molecular masses ranging 778-1354 Da, were identified by the Peaks database algorithm using the available Olea europaea (cv. Farga) genome database. Ten new peptides were also identified by Peaks de novo sequencing. The protein sources of twelve peptides detected in the database by Peaks DB were identified by BLAST search. The ACE inhibitory activity of the identified peptides was predicted by BIOPEP software. We conclude that olive pomace possesses ACE inhibitory activity and contains low molecular weight peptides with (predicted) biological activity. Olive pomace may represent a good source of peptides for nutritional and pharmaceutical applications. In our study, it has been shown that olive pomace possesses ACE inhibitory activity and contains low molecular weight peptides with (predicted) biological activity. Olive pomace may represent a good source of peptides for nutritional and pharmaceutical applications. More research is needed in order to identify the in vivo effects of olive pomace bioactive peptides.

Production of Antioxidant, Angiotensin-Converting Enzyme Inhibitory and Osteogenic Gelatin Hydrolysate from Labeo rohita Swim Bladder.

Optimization of antioxidants and angiotensin-converting enzyme (ACE) inhibitory potential gelatin hydrolysate production from Labeo rohita (rohu) swim bladder (SBGH) by alcalase using central composite design (CCD) of response surface methodology (RSM) was investigated. The maximum degree of hydrolysis (DH), 2,2-diphenyl-1-picrylhydrazyl (DPPH), 2,2'-azino-bis-3-ethylbenzthiazoline-6-sulphonic acid (ABTS), total antioxidants (TAO), and ACE inhibitory activity were achieved at 0.1:1.0 (w/w) enzyme to substrate ratio, 61°C hydrolysis temperature, and 94-min hydrolysis time. The resulting SBGH obtained at 19.92% DH exhibited the DPPH (24.28µM TE/mg protein), ABTS (34.47µM TE/mg protein), TAO (12.01µg AAE/mg protein), and ACE inhibitory (4.91µg/mg protein) activity. Furthermore, SBGH at 100µg/ml displayed osteogenic property without any toxic effects on MC3T3-E1 cells. Besides, the protein content of rohu swim bladder gelatin (SBG) and SBGH was 93.68% and 94.98%, respectively. Both SBG and SBGH were rich in glycine, proline, glutamic acid, alanine, arginine, and hydroxyproline amino acids. Therefore, SBGH could be an effective nutraceutical in functional food development.

Optimization of Extraction Process and Activity of Angiotensin-Converting Enzyme (ACE) Inhibitory Peptide from Walnut Meal.

In order to further realize the resource reuse of walnut meal after oil extraction, walnut meal was used as raw material to prepare polypeptide, and its angiotensin-converting enzyme (ACE) inhibitory activity was investigated. The ACE inhibitory peptides were prepared from walnut meal protein by alkaline solution and acid precipitation. The hydrolysis degree and ACE inhibition rate were used as indexes to optimize the preparation process by single-factor experiment and response surface method. The components with the highest ACE activity were screened by ultrafiltration, and their antioxidant activities were evaluated in vitro. The effect of gastrointestinal digestion on the stability of walnut peptide was analyzed by measuring molecular weight and ACE inhibition rate. The results showed that the optimal extraction conditions were pH 9.10, hydrolysis temperature 54.50 °C, and hydrolysis time 136 min. The ACE inhibition rate of walnut meal hydrolysate (WMH) prepared under these conditions was 63.93% ± 0.43%. Under the above conditions, the fraction less than 3 kDa showed the highest ACE inhibitory activity among the ACE inhibitory peptides separated by ultrafiltration. The IC50 value of scavenging ·OH free radical was 1.156 mg/mL, the IC50 value of scavenging DPPH free radical was 0.25 mg/mL, and the IC50 value of scavenging O2- was 3.026 mg/mL, showing a strong total reducing ability. After simulated gastrointestinal digestion in vitro, the ACE inhibitory rate of walnut peptide decreased significantly, but it still maintained over 90% ACE inhibitory activity. This study provides a reference for the application of low-molecular-weight walnut peptide as a potential antioxidant and ACE inhibitor.

Preparation, identification, and molecular docking of novel angiotensin-converting enzyme inhibitory peptides derived from rice-based distillers' spent cakes.

Rice-based distillers' spent cake (RDSC), a by-product of the Chinese liquor (Baijiu) industry, is a potential source of angiotensin-converting enzyme (ACE) inhibitory peptide. Since ACE plays a crucial role in controlling hypertension, inhibition of ACE has been widely emphasized. The ACE inhibitory active peptide derived from by-products of food has been recognized as a safer and cheaper inhibitor. Aimed to discover ACE-inhibiting active peptides in RDSC. Hydrolysis of RDSC by alcalase for 4 h followed by ultrafiltration yielded low-molecular-weight (< 3 kDa) fractions. Subsequently, a comprehensive method using a combination of liquid chromatography quadrupole time-of-flight mass spectrometry (LC-Q-TOF-MS) and LC-Q-Exactive-MS to identify the novel short peptides (3-5 amino acids residues; n = 7) and medium-sized peptides (more than 6 amino acids residues; n = 6). In vitro activity assay showed that the peptides KPFFPGL, GFPRPLL, GPPGVF, and VGK exhibited the highest activity with inhibitory concentration of 50% (IC50) of 11.63, 12.34, 19.55, and 33.54 μmol L-1. Molecular docking reveal that the active and inactive sites (Glu123, Asp121, Arg522, and Lys118) play important roles in enhancing the ACE inhibitory activity of peptides. Here we report a comprehensive method that effectively extracted and identified the bioactive peptides from RDSC. Four highly active novel peptides may be the most promising candidates for functional foods against hypertension, provide significant information for enhancing value of rice-based distilled by-products. © 2024 Society of Chemical Industry.

A novel angiotensin I-converting enzyme inhibitory peptide from walnut (Juglans sigillata) protein hydrolysates and its evaluation in Ang II-induced HUVECs and hypertensive rats

This study aims to seek angiotensin-I-converting enzyme inhibitory (ACEi) peptides from walnut using different enzymatic hydrolysis, and further to validate the potent ACEi peptides identified and screened via peptidomics and in silico analysis against hypertension in spontaneously hypertensive rats (SHRs). Results showed that walnut protein hydrolysate (WPH) prepared by combination of alcalase and simulated gastrointestinal digestion exhibited high ACEi activity. WPH was separated via Sephadex-G25, and four peptides were identified, screened and verified based on their PeptideRanker score, structural characteristic and ACE inhibition. Interestingly, FDWLR showed the highest ACEi activity with IC50 value of 8.02 μg/mL, which might be related to its close affinity with ACE observed in molecular docking. Subsequently, high absorption and non-toxicity of FDWLR was predicted via in silico absorption, distribution, metabolism, excretion and toxicity. Furthermore, FDWLR exhibited positively vasoregulation in Ang II-induced human umbilical vein endothelial cells, and great blood pressure lowering effect in SHRs.

Biological Activity Evaluation of Olive, Grape, and Fig at Various Mixing Ratios

Purpose: This study aimed to evaluate the antioxidation and enzymatic activity-related qualities of four mixtures prepared with different mixing ratios of olives (O), grapes (V), and figs (F), which are representative ingredients of the Mediterranean diet. Methods: Following mixtures were prepared: olives–figs (OF), grapes–figs (VF), and olives–grapes–figs (OVF). For mixture preparation, the ingredients were mixed in following ratios: olives-to-grapes, olives-to-figs, and grapes-to-figs at ratios of 1:1 (30 g of each) as well as olives-to-grapes-to-figs at a ratio of 1:1:1 (20 g of each). The antioxidant (total polyphenol and flavonoid contents along with 2,2-diphenyl-1-picrylhydrazyl [DPPH] and 2,2′-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) [ABTS] radical scavenging) and enzymatic (α-glucosidase inhibitory and angiotensin-converting enzyme [ACE] inhibitory) activities of the four aforementioned mixtures were measured. Results: OV and OVF mixtures showed the highest total polyphenol (27.25±0.22 mg TAE/g) and flavonoid contents (27.9 ± 2.14 mg QE/g), respectively. DPPH radical scavenging ability was highest in OV (92.86 ± 0.17%). The highest ABTS radical scavenging activity was registered in the OVF mixture (42.88±1.19%). α-glucosidase and ACE inhibitory activity measurements were highest in the OVF mixture (79.75±0.15% and 88.61±0.08%, respectively). Conclusion: Highest physiological activity levels (i.e., anti-oxidation and enzymatic activity) were observed in the olive, grape, and fig (1:1:1) mixture, hence, its regular consumption could improve metabolic syndrome.

Changes in potato peptide bioactivity after gastrointestinal digestion. An in silico and in vitro study of different patatin-rich potato protein isolate matrices

Potato protein has gained attention as a promising protein source, because of its amino acid profile and technological functionality; however, little is reported about its nutritional properties as a function of processing history. In this work, the digesta of the four potato protein matrices (suspension, foam, gel, and heated foam) were analyzed by LC-MS/MS and their bioactivity evaluated in vitro and in silico.Different treatments significantly influenced digestion efficiency and peptide distribution. Heat treatment enhanced the hydrolysis, which led to distinct peptide patterns and distributions compared to unheated proteins. Heated foams showed smallest concentration of residual protein in the intestinal stage, and the highest resistance to digestion. Peptides obtained after digestion exhibited a range of potential health benefits in silico, namely, antimicrobial, antihypertensive, and antioxidant activities. All intestinal digesta showed in vitro DPPH radical scavenging and ACE-inhibitory activity.

Rice dreg protein as a high‐quality plant‐based protein resource: Characterization of structural, functional, and in vitro digestive properties

AbstractBackground and ObjectivesRice dregs, a by‐product of the process of making sugar from broken rice, have a protein content of up to 70%. However, rice dreg protein (RDP) has not yet been fully utilized due to its high‐temperature liquefaction denaturation during sugar production. In this study, the structural, functional, and in vitro digestive properties of rice protein (RP) extracted from broken rice and RDP derived from rice dregs were compared, with a view to providing a basis for further utilization of RDP.FindingsAlthough RDP was a heat‐denatured protein, it was found to have relatively better functional properties and a well‐balanced amino acid composition. Structural analysis results revealed that RDP showed a looser and disordered structure. However, SDS‐PAGE results showed that the subunit composition of the two proteins was similar. The in vitro simulated digestion results showed that the digests of RDP had higher antioxidant and ACE inhibitory activity, but RDP showed significantly lower digestibility than RP.ConclusionsThrough relevant modifications of RDP, RDP has the potential to be a good source of high‐quality protein in the human diet as the demand for plant‐based protein increases.Significance and NoveltyThis study can provide a basic theoretical basis for further development and utilization of RDP, which is also of great practical significance for seeking new plant protein resources and increasing the added value of broken rice.