Converting Enzyme Inhibitory Activity Research Articles

Changes in functional activities and volatile flavor compounds of fermented mung beans, cowpeas, and quinoa started with Bacillus amyloliquefaciens SY07.

In this work, the functional activities including α-glucosidase, α-amylase, angiotensin converting enzyme (ACE) inhibitory activity, and antioxidant activity of mixed grains (mung beans, cowpeas, and quinoa) fermented with Bacillus amyloliquefaciens SY07 were investigated. The volatile flavor of the mixed grains collected every 12h during 72h-fermentation were further detected as well. The inhibition on α-glucosidase and α-amylase reached up to 89.34% and 50.03% with the sample concentration of 5.17 and 9.38mg/mL, respectively. Moreover, the ACE inhibitory activity reached to 93.66% with the sample concentration of 0.59mg/mL. The antioxidant capacity of the mixed grains, evaluated by ABTS and DPPH radical scavenging capacities and ferric ion reducing power, was also significantly improved (p<0.05) during fermentation. The maximum of ABTS and DPPH radical scavenging capacities increased to 8.64 and 3.21mg TE/g DW, respectively, and the maximum ferric ion reducing power reached to 5.73mg TE/g DW. Twenty-one volatile flavor compounds with odor activity values (OAVs)≥1 were detected, and six key volatile flavor substances were identified by OPLS-DA analysis, namely, isovaleric acid, acetoin, phenylacetic acid, (Z)-2-nonenol, 1-hexanol, and 1-octen-3-ol, with overall strong creamy, sweet, baked-potato, and cocoa flavors upon fermentation. These findings revealed a favorable pathway for B. amyloliquefaciens SY07 to be used to improve the functional and flavor properties of fermented grains, which would also be of great value for further elucidating the mechanism of the formation of the volatile flavor differences and developing novel quality cereal-based products.

Identification of barley-derived peptides with angiotensin converting enzyme inhibitory activity

Identification of barley-derived peptides with angiotensin converting enzyme inhibitory activity

Comprehensive chemical profile, angiotensin-I converting enzyme inhibitory and calcium chelation activity of rice wine lees and rice vinegar residues: A novel development strategy

Comprehensive chemical profile, angiotensin-I converting enzyme inhibitory and calcium chelation activity of rice wine lees and rice vinegar residues: A novel development strategy

Identification of the Heptapeptide PR7 and Octapeptide SF8 With Potent Antioxidative and Angiotensin Converting Enzyme Inhibitory Activity From the Fermented Dairy By‐Product “Buttermilk”

Identification of the Heptapeptide PR7 and Octapeptide SF8 With Potent Antioxidative and Angiotensin Converting Enzyme Inhibitory Activity From the Fermented Dairy By‐Product “Buttermilk”

Anti-hypertensive, anti-inflammatory, glycemic and satiety impact of cocoa flavoured soy-based powder drink mix enriched with bioactive hydrolysates from nests of Aerodramus fuciphagus

Abstract Objectives The edible bird’s nest hydrolysates (EBNH) are renowned for their health benefits. The study aimed to determine their contributory functional effect as an ingredient in the cocoa-flavoured soy-based powder drink mix (PDM). The product’s glycemic and satiety impact were also studied. Materials and Methods The product was enriched with a reasonably low amount of spray-dried EBNH. The product’s functional effect with respect to in vitro angiotensin converting enzyme (ACE) inhibitory activity and human red blood cells membrane stabilization (RBCMS) activity were evaluated, using its water extract (90 - 95 oC). The glycemic and satiety impact were evaluated using 12 and 30 subjects, respectively, who consumed 250 mL of the product, containing 25 g of available carbohydrates. Results The enriched PDM’s ACE inhibitory activity and RBCMS activity were significantly higher (p&amp;lt;0.05) than those that were devoid of EBNH. A 240 mL (12.5% w/v) of PDM (containing by weight 3.0% EBNH, 75.44% soybean powder, 20% cocoa powder, 0.5% xanthan gum, 1.0% silicon dioxide and 0.06% sucralose) provides about 3.7 kcal/g energy. Its 250 mL meal (consistency index of 14.17 Pa.sn) is high in protein and dietary fiber. The product’s glycemic index (GI) and glycemic load (GL) are low, 24 and 6.0, respectively, raising a normal level of 2 hours postprandial blood glucose (&amp;lt;6 mmol/L) and satisfies hunger for about 2.5 hours. Conclusion The EBNH, as an ingredient, enhances the PDM’s anti-hypertensive and anti-inflammatory properties. The overall findings suggest that the formulated PDM is a wellness food product capable of promoting good human health, including for dieters and individuals with diabetes.

The profile of plant bioactive compounds in Xinjiang, China unifloral safflower honey and their inhibitory on ACE, and determination of the mechanism of inhibition

Investigating the plant bioactive compounds in unifloral safflower honey from Xinjiang, China, is helpful for verifying its botanical origin and evaluating its functional properties. Therefore, this study quantifying hydroxysafflor yellow A (HSYA), anhydroxysafflor yellow B (ASYB), quercetin, kaempferol, rutin, myricetin, hyperoside, gallic acid, quinic acid, and ferulic acid in safflower honey by high-performance liquid chromatography; HSYA and ASYB accounted for 16.12–28.83% and 13.63–33.09%, respectively, of the quantified plant bioactive compounds and were considered characteristic markers for authentication. These compounds also exhibit angiotensin converting enzyme (ACE) inhibitory activity; the IC50 ranges from 13.33 to 132.45 μmol L−1, and the inhibition constant (Ki) is between 17.13 and 121.34 μmol L−1. HSYA (IC50 = 20.24 μmol L−1, Ki = 19.63 μmol L−1) and ASYB (IC50 = 19.33 μmol L−1, Ki = 17.13 μmol L−1) exhibited the strongest inhibitory effects. Molecular simulation studies have shown that these bioactive compounds bind key residues in the active pocket of ACE through hydrogen bonding and hydrophobic interactions, leading to ACE inhibition. Overall, HSYA and ASYB could be considered bioactive chemical markers for verifying the botanical origin of Xinjiang, China, unifloral safflower honey, and safflower honey may be a potential functional food by inhibiting ACE.

ESSENTIAL OIL CONTENTS AND BIOLOGICAL ACTIVITIES OF THYMUS CANOVIRIDIS JALAS AND THYMUS SIPYLEUS BOISS.

Objective: Members of the Lamiaceae family are considered to be major sources of bioactive therapeutic agents. Many of them are important medicinal and aromatic plants used in traditional and modern medicine and in the food, cosmetic and pharmaceutical industries. The aim of this study was to investigate in detail the biological activities and chemical composition of the essential oils of Thymus canoviridis Jalas and Thymus sipyleus Boiss. species belonging to the genus Thymus, one of the most important genera of the Lamiaceae family. Material and Method: The essential oil content of the species was determined by GC-MS. Antioxidant activities of the essential oils were determined using lipid peroxidation, DPPH free radical, ABTS cation radical and CUPRAC methods. In addition, cytotoxic activities against breast cancer (MCF-7) and colon cancer (HT-29) cell lines and anticholinesterase (against AChE and BChE enzymes), urease, tyrosinase, elastase, collagenase and angiotensin converting enzyme inhibition activities were determined. Result and Discussion: When the essential oil composition of T. sipyleus was analyzed, the major compounds were 1,8-cineole (eucalyptol) (18.16%), camphor (15.08%) and endo-borneol (11.63%), while T. canoviridis was found to be rich in carvacrol (72.88%). T. canoviridis showed high antioxidant activity in lipid peroxidation (IC50: 45.72±0.12 μg/ml), ABTS (IC50: 6.12±0.03 μg/ml) and CUPRAC (IC50: 5.31±0.01 μg/ml) methods. The selectivities of T. canoviridis and T. sipyleus species against MCF-7 cell line were 4.39 and 6.81, respectively. In the enzyme inhibition studies, both Thymus species showed moderate inhibition activity against BChE enzyme (Inhibition%: 57.88±1.14, 39.21±0.89, respectively). In addition, T. sipyleus showed moderate inhibition of elastase enzyme (Inhibition%: 25.33±0.79). When the results are evaluated in general, it can be said that T. canoviridis essential oil with its rich carvacrol content and high cytotoxic and antioxidant activity can be preferred as a safer and natural option instead of synthetic preservatives in food, pharmaceutical and cosmetic industries to extend shelf life and ensure food safety.

Bioactive, Pro-Apoptotic-Angiotensin Converting Enzyme Inhibitor Effects and Properties of Ultrasound-Treated Traditional Poppy Vinegar Using the Response Surface Methodology Model.

Poppy vinegar with functional properties is a fermented product. This study evaluated traditionally produced poppy vinegar. The study was conducted on poppy vinegar to determine the maximum increase in angiotensin converting enzyme (ACE) inhibitory activity %, total phenolic content (TPC), and radical scavenging activity (DPPH) of the vinegar at different combinations of ultrasound treatment duration (2-14 min) and amplitude (40-100%). The optimal parameters obtained using the response surface methodologies (RSM) were the duration of the ultrasound of 5.5 min and the amplitude of the ultrasound at 57%. When the DPPH values, ACE inhibition %, and TPC and DPPH values obtained with the RSM model were compared with the experimental values, the difference was 9.80, 3.0, and 4.6%, respectively, showing good agreement between actual and predicted values. The higher ultrasound intensities and longer treatment times had a significant effect on antioxidant activity. Poppy vinegar samples significantly induced the apoptosis of lung cancer cells, particularly those stored for 6 and 12 months. The amounts of protocatechuic acid, gallic acid, neohesperidin, hydroxybenzoic acid, resveratrol, rutin, trans-cinnamic acid, quercetin, and flavon in poppy vinegar were determined, which decreased significantly as storage time increased. TPC and TFC were determined to be 90.39 mg of GAE/100 mL and 29.86 mg of TEAC/mL, respectively, and there was no significant change in these bioactive compounds after 6 months of storage. The highest value of ACE inhibitory activity was found at the beginning of the storage period. The present study was the first study to examine the bioactive components, ACE inhibition activity, pro-apoptotic activities, and phenolic composition of traditionally produced ultrasound-treated poppy vinegar during storage. The control of production parameters and the design of ideal poppy vinegar fermentation processes could benefit from this research.

Chemical characterization and angiotensin-I converting enzyme inhibitory activity of Indonesian stinky beans

The chemical composition of four Indonesian stinky beans has been explored. Those bean are Petai (Parkia speciosa), Lamtoro Gung (Leucaena leucochepala ssp. Glabrata (Rose) S. Zarate), Jengkol (Pithecellobium jiringa) and Kabau (Archidendron bubalinum). This exploration belongs to the local food utilization research theme of functional food sources. Those beans have a unique flavour and usually lead to foul stools, sweat, urine or mouth odour. Their intense flavour may be due to the content of amino acids. High hydrophobic and negative charge hydrophilic amino acids are crucial in preventing hypertension through inhibition of angiotensin I-converting enzyme (ACE) activity. This study evaluated the chemical properties of beans and its angiotensin I-converting enzyme inhibitory (ACE-I) peptides. The amino acid profile was determined as preliminary data to ensure the content of hydrophobic and negative charge hydrophilic amino acids. Their ability to inhibit ACE was studied to represent an antihypertensive effect. In vitro gastrointestinal digestion was applied to obtain more small molecular peptides and evaluate their ACE-I activity after digestion. Petai has the highest glutamic acid (20.90 g/100 g protein d.b.), lysine (13.31 g/100 g protein d.b.), arginine (11.76 g/100 g protein d.b.), leucine (10.98 g/100 g protein d.b.), and aspartic acid (10.72 g/100 g protein d.b.). Fresh Jengkol has the highest ACE-I activity (67.59%). Subsequential digestion by pepsin and pancreatin improves the ACE-I activity, and Kabau had the highest (79.87%). Based on the results, Indonesian stinky beans can prevent hypertension by inhibiting ACE activity and being used as a protein source alternative

Antioxidant capacity and peptidomic analysis of in vitro digested Camelina sativa L. Crantz and Cynara cardunculus co-products

In recent decades, the food system has been faced with the significant problem of increasing food waste. Therefore, the feed industry, supported by scientific research, is attempting to valorise the use of discarded biomass as co-products for the livestock sector, in line with EU objectives. In parallel, the search for functional products that can ensure animal health and performances is a common fundamental goal for both animal husbandry and feeding. In this context, camelina cake (CAMC), cardoon cake (CC) and cardoon meal (CM), due valuable nutritional profile, represent prospective alternatives. Therefore, the aim of this work was to investigate the antioxidant activity of CAMC, CC and CM following in vitro digestion using 2,2′-azinobis-(3-ethylbenzothiazoline-6-sulphonic acid) (ABTS), Ferric reducing antioxidant power (FRAP) and oxygen radical absorbance capacity (ORAC) assays. Total phenolic content (TPC) and angiotensin converting enzyme (ACE) inhibitory activity, actively involved in modulating antioxidant properties, were also studied. Further, a peptidomic analysis was adopted to substantiate the presence of bioactive peptides after in vitro digestion. The results obtained confirmed an interesting nutritional profile of CAMC, CC and CM and relevant antioxidant and ACE inhibitory activities. In particular, considering antioxidant profile, CM and CC revealed a significantly higher (10969.80 ± 18.93 mg TE/100 g and 10451.40 ± 149.17 mg TE/100 g, respectively; p < 0.05) ABTS value than CAMC (9511.18 ± 315.29 mg TE/100 g); a trend also confirmed with the FRAP assay (306.74 ± 5.68 mg FeSO4/100 g; 272.84 ± 11.02 mg FeSO4/100 g; 103.84 ± 3.27 mg FeSO4/100 g, for CC, CM and CAMC, respectively). Similar results were obtained for TPC, demonstrating the involvement of phenols in modulating antioxidant activity. Finally, CAMC was found to have a higher ACE inhibitory activity (40.34 ± 10.11%) than the other matrices. Furthermore, potentially bioactive peptides associated with ACE inhibitory, anti-hypertensive, anti-cancer, antimicrobial, antiviral, antithrombotic, DPP-IV inhibitory and PEP-inhibitory activities were identified in CAMC. This profile was broader than that of CC and CM. The presence of such peptides corroborates the antioxidant and ACE profile of the sample. Although the data obtained report the important antioxidant profile of CAMC, CC, and CM and support their possible use, future investigations, particularly in vivo trials will be critical to evaluate and further investigate their effects on the health and performance of farm animals.

In vitro digestibility and angiotensin converting enzyme (ACE) inhibitory activity of solid-state fermented fava beans (Vicia faba L.)

Reducing the content of quickly absorbed carbohydrates and saturated fats in snack formulations while increasing the consumption of high-quality proteins are effective strategies to prevent obesity in childhood. Thus, the nutritional value, digestibility, and functionality of fava beans (Vicia faba L.) fermented with Pleurotus ostreatus were examined as potential ingredients for food design. Solid-state fermentation enhanced the protein content by 16% with a rise in essential (25%) and non-essential (15%) amino acids while decreasing total carbohydrate content and tannin levels. Moreover, fermentation modified the amino acid profile released during digestion, increasing amino acids such as valine, isoleucine, and threonine, which are vital for health and development in childhood. Furthermore, the bioaccessible fraction of the fermented bean showed a 60% of ACE inhibition and improved magnesium bioaccessibility. Consequently, fava beans fermented with Pleurotus ostreatus emerged as a new ingredient in the development of new protein-rich snacks tailored for children and adolescents.

Modification of Bioactive Properties in Food Protein Hydrolysates by Alcalase and Trypsin

Abstract Background Protein hydrolysates are the fragments of proteins that form during the hydrolysis with promised bioactive properties. Enzymatic hydrolysis produces bioactive peptides with specific amino acid profile. Among all the properties, angiotensin-I converting enzyme (ACE-I) inhibitory activity of the protein hydrolysates attained maximum attention to combat life-threatening disease like hypertension. Methodology In the present study 10 protein-rich food sources (&gt; 20% protein content on dry basis) were used to prepare protein hydrolysates using alcalase and trypsin to investigate the effect of enzymes on ACE-I inhibitory and antioxidant activity. Results Among all the sources, the highest degree of hydrolysis was observed in sardine (62.89%) followed by soybean (61.24%) when hydrolyzed by alcalase. Kidney pea exhibited highest ACE-I inhibitory activity with IC50 value of 0.517 and 0.521 when hydrolyzed using both trypsin and alcalase, respectively. All the sources selected showed nonsignificant changes in ACE-I inhibitory activity between alcalase and trypsin (p &lt; 0.05) except Bengal gram and chicken. Antioxidant activity was higher in alcalase hydrolyzed egg yolk (43.08%). Conclusion Among the sources, all animal proteins hydrolyzed using alcalase exhibited significantly higher (p &lt; 0.05) antioxidant activity than trypsin. However, protein hydrolysates prepared from sardine using alcalase would yield bioactive peptides with higher ACE-I inhibitory and antioxidant activity. Therefore, use of alcalase as a substitution for trypsin would be economical for large-scale production. Henceforth, food protein hydrolyzed by alcalase can be used as a functional ingredient for the development of functional or nutraceutical foods to combat lifestyle diseases.

Antioxidant and angiotensin converting enzyme inhibitory activities of red lionfish (Pterois volitans L.) muscle protein hydrolysates obtained using pepsin-pancreatin system

Despite being an invasive species and representing a threat in the area, red lionfish (Pterois volitans L.) meat is valued for its pleasant taste and high protein content. The objective of the present work was to evaluate the angiotensin converting enzyme inhibition (ACE-I) and the antioxidant activities of red lionfish muscle protein hydrolysates in vitro. Hydrolysates were obtained using the pepsin-pancreatin system, and their degree of hydrolysis (DH), electrophoretic, and amino acid profile were determined. Subsequently, their ACE-I and ABTS+ radical scavenging activity were evaluated, selecting those with the highest response. The highest DH (66.1%) was found in the hydrolysate obtained at 120 min of reaction time (H120); electrophoresis revealed the action of the enzymes on the muscle proteins. The highest bioactivities occurred during hydrolysis with pepsin for 60 min (H60), obtaining the highest ACE-I of 68.8% (evaluated with 500 µg protein) with a DH of 16.8%, ACE-I related amino acid content of 33.6%, and hydrophobic amino acid content of 42.9%. With the 30 min hydrolysates (H30), the highest Trolox equivalent antioxidant capacity of 60.3 mM/mg protein was obtained with 18.4% DH and 22.1% radical scavenger amino acids; its comparison with H120 proved that higher DH did not produce a greater response in ABTS+ radical scavenging activity, DPPH, reducing power, and copper chelation assays; with β-carotene bleaching being the exception. Therefore, it can be concluded that red lionfish muscle hydrolysates could be a promising source of peptides with antihypertensive and antioxidant properties, and can be suitable as functional ingredients.

A strategy to boost xanthine oxidase and angiotensin converting enzyme inhibitory activities of peptides via molecular docking and module substitution

Molecular docking and activity evaluation screened the dipeptide module GP with low xanthine oxidase (XOD) inhibitory activity and modules KE and KN with high activity, and identified them as low- and high-contribution modules, respectively. We hypothesized the substitution of low-contribution modules in peptides with high contributions would boost their XOD inhibitory activity. In the XOD inhibitory peptide GPAGPR, substitution of GP with both KE and KN led to enhanced affinity between the peptides and XOD. They also increased XOD inhibitory activity (26.4% and 10.3%) and decreased cellular uric acid concentrations (28.0% and 10.4%). RNA sequencing indicated that these improvements were attributable to the inhibition of uric acid biosynthesis. In addition, module substitution increased the angiotensin-converting enzyme inhibitory activity of GILRP and GAAGGAF by 84.8% and 76.5%. This study revealed that module substitution is a feasible strategy to boost peptide activity, and provided information for the optimization of hydrolysate preparation conditions.

Impact of Lactiplantibacillus plantarum and casein fortification on angiotensin converting enzyme inhibitory peptides in yogurt: identification and in silico analysis.

In this study, the effects of Lactiplantibacillus plantarum M11 (Lb. plantarum M11) in conjunction with sodium caseinate on the characteristics and angiotensin converting enzyme (ACE) inhibitory activity of yogurt were investigated. ACE inhibitory peptides (ACEIPs) in yogurt were identified by nano-LC-MS/MS and potential ACEIPs were predicted by in silico and molecular docking methods. The results showed that the ACE-inhibitory activity of yogurt was significantly enhanced (p < 0.05), while maintaining the quality characteristics of the yogurt. Thirteen ACEIPs in the improved yogurt (883 + M11-CS group) were identified, which were more abundant than the other yogurt groups (control 883 group, 883 + M11 group and 883-CS group). Two novel peptides with potential ACE inhibitory activity, YPFPGPIH and NILRFF, were screened. The two peptides showed PeptideRanker scores above 0.8, small molecular weight and strong hydrophobicity, and were non-toxic after prediction. Molecular docking results showed that binding energies with ACE were -9.4 kcal mol-1 and -10.7 kcal mol-1, respectively, and could bind to the active site of ACE. These results indicated that yogurt with Lb. plantarum M11 and sodium caseinate has the potential to be utilized as a functional food with antihypertensive properties. The combination of ACEIP-producing strains and casein fortification could be an effective method to promote the release of ACEIPs from yogurt.

A new benzophenanthridine alkaloid from stem bark of Zanthoxylum rhetsa and its biological activities

A new benzophenanthridine alkaloid 6-butanoyldihydrochelerythrine (1) and five known alkaloids 6-acetonyldihydronitidine (2), 6-acetonyldihydrochelerythrine (3), isocorydine (4), (O)-methyltembamide (5), N-(4-methoxyphenethyl)benzamide (6) were isolated from the stem barks of Zanthoxylum rhetsa. These structures were elucidated by 1D, 2D NMR spectroscopy and by mass spectrometry. This is the first time that compounds 2–6 were identified from Zanthoxylum rhetsa and the first time that compounds 4 and 6 were identified from the genus Zanthoxylum. Bioactivity results of isolated compounds showed that 1, 2, 5 and 6 exhibited inhibitory activity against MCF7 and A549 cell lines, while 3 showed the inhibitory activity against A549 cell line; all isolated compounds 1–6 inhibited at least two strain microorganisms; compound 4 showed angiotensin II converting enzyme inhibitory activity in vitro with IC50 value of 65.58 µM and in silico with a docking score of −11.52 kcal/mol.

Characterization of Proteins Extracted from Ulva sp., Padina sp., and Laurencia sp. Macroalgae Using Green Technology: Effect of In Vitro Digestion on Antioxidant and ACE-I Inhibitory Activity.

Macroalgal proteins were extracted from Ulva rigida (URPE) (green), Padina pavonica (PPPE) (brown), and Laurencia obtusa (LOPE) (red) using ultrasound-assisted enzymatic extraction, which is one of the green extraction technologies. Techno-functional, characteristic, and digestibility properties, and biological activities including antioxidant (AOA) and angiotensin-I converting enzyme (ACE-I) inhibitory activities were also investigated. According to the results, the extraction yield (EY) (94.74%) was detected in the extraction of L. obtusa, followed by U. rigida and P. pavonica. PPPE showed the highest ACE-I inhibitory activity before in vitro digestion. In contrast to PPPE, LOPE (20.90 ± 0.00%) and URPE (20.20 ± 0.00%) showed higher ACE-I inhibitory activity after in vitro digestion. The highest total phenolic content (TPC) (77.86 ± 1.00 mg GAE/g) was determined in LOPE. On the other hand, the highest AOACUPRAC (74.69 ± 1.78 mg TE/g) and AOAABTS (251.29 ± 5.0 mg TE/g) were detected in PPPE. After in vitro digestion, LOPE had the highest TPC (22.11 ± 2.18 mg GAE/g), AOACUPRAC (8.41 ± 0.06 mg TE/g), and AOAABTS (88.32 ± 0.65 mg TE/g) (p < 0.05). In vitro protein digestibility of three macroalgal protein extracts ranged from 84.35 ± 2.01% to 94.09 ± 0.00% (p < 0.05). Three macroalgae showed high oil holding capacity (OHC), especially PPPE (410.13 ± 16.37%) (p < 0.05), but they showed minimum foaming and emulsifying properties. The quality of the extracted macroalgal proteins was assessed using FTIR, SDS-PAGE, and DSC analyses. According to our findings, the method applied for macroalgal protein extraction could have a potential the promise of ultrasonication application as an environmentally friendly technology for food industry. Moreover, URPE, PPPE, and LOPE from sustainable sources may be attractive in terms of nourishment for people because of their digestibility, antioxidant properties, and ACE-I inhibitory activities.

Ultrafiltration fractionation of rice protein hydrolysates: Physicochemical properties and potential biological activities of different rice protein hydrolysate fractions

In this study, rice protein hydrolysate (RPH) was separated by membrane ultrafiltration, and three ultrafiltration fractions (UFs) with distinct molecular weights (RPP-1, RPP-2 and RPP-3) were yielded. The physicochemical properties and in vitro bioactivities of these fractions were characterized. Among RPH and its UFs, RPP-1 exhibited highest DPPH radical scavenging activity (IC50 = 4.42 ± 0.08 mg/mL) and ferric reducing antioxidant power (84.21 mg GSH/g). RPP-3 exhibited the highest ABTS radical scavenging activity (IC50 = 0.97 ± 0.01 mg/mL). All the samples exhibited angiotensin converting enzyme inhibitory activity (5.38% ± 0.76%–54.14% ± 3.04%) and α-glucosidase inhibitory activity (−38.90% ± 3.20%–99.99% ± 0.01%). In addition, the activation of alcohol dehydrogenase by RPH and its UFs was observed in this study, with an activation percentage of 46.20% ± 4.96%–199.77% ± 7.71%. However, no inhibitory activity towards acetylcholinesterase was detected. In present study, the potential antialcohol and hepatoprotective activity of RPH was observed. Overall, this study would provide a new idea for the high-value utilization of RPH and a theoretical foundation for the development of bioactivity peptides derived from rice protein.

Amino acid composition and angiotensin-i converting enzyme inhibitory activity of Cowpea (&lt;i&gt;Vigna unguiculata&lt;/i&gt;) pepsin-pancreatin protein hydrolysate fractions

Legumes are high in protein and have been linked to the management and prevention of chronic diseases due to their bioactive components. This study investigated the amino acid composition of cowpea protein hydrolysate and its inhibitory impact on angiotensin-I converting enzyme (ACE-I). Cowpea (Vigna unguiculata) protein hydrolysate (CPH) was produced through sequential digestion with pepsin and pancreatin. CPH was then separated using G-50 gel filtration chromatography and reverse phase high performance liquid chromatography (RP-HPLC). The fractions' ACE-I inhibitory activity was then assessed. The IC50 value for the RP-HPLC fraction with the highest ACE-I inhibitory activity (P&lt;0.05) was 6.23 μg/mL. The amino acid profile revealed that a large proportion of hydrophobic amino acids were present in the RP-HPLC fraction containing the peptide with the highest ACE-I inhibitory activity. These findings suggest that CPH has the potential to be employed in the development of functional foods that can aid in the prevention and treatment of hypertension.

Antioxidant, angiotensin converting enzyme inhibitory and anthelmintic activities of bark essential oil of Cinnamomum bejolghota (Buch.-Ham.) Sweet from North East India

Cinnamomum bejolghota (Buch.-Ham.) Sweetisa traditional anthelmintic and cardiotonic medicinal plant. The essential oil extracted from the bark of C. bejolghota was characterized by gas chromatography-mass spectrometry and 28 constituents were identified. Monoterpenoids were found to be dominating chemical constituents with α-terpineol (18.57 %) as the major component of the essential oil. The antioxidant activity of the essential oil was evaluated by DPPH radical, β-carotene bleaching and reducing power assay methods. The essential oil showed in-vitro dose-response hindering activity against angiotensin-converting enzyme with an IC50 value of 33.43 ± 0.46 µg/mL.The essential oil also exhibited potent anthelmintic property in-vitro against Caenorhabditis elegans with an ED50value of 80.53 ± 3.57 µg/mLin adult mortality assay. The inhibitory activity of essential oil against larval development assay showed an ED50value of 72.40 ± 2.68 µg/mL against C. elegans larva. Further, the egg hatching assay using C. eleganseggs demonstrated an ED50 value of 68.27 ± 3.51 µg/mL with this essential oil. Thus, the ethnomedicinal claim has been validated for the bark essential oil, which provides an excellent scope for the development of the C. bejolghota bark essential oil as novel herbal antihypertensive and anthelmintic agents.