Α-amylase Enzyme Research Articles

Assessing the Effect of Temperature on Nutrient Retention in Canistel Fruit (Pouteria campechiana) and Coconut Milk Formulation

Objective: This study aimed to develop innovative fruit-based beverages from underutilized but widely available Canistel fruit around tropical regions and determine its nutrient stability at different temperature treatments. Background: Canistel Fruit (Pouteria campechiana) is an underutilized nutritious tropical fruit containing Vitamin A and complex carbohydrates with high potentiality. Hence, the present study focused on a novel Canistel fruit (Pouteria campechiana)-based beverage. Methods: The higher starchiness of fruit pulp was remedied through α-amylase enzyme treatment. The base formula was prepared with fruit pulp and coconut milk (at ratios of 1:2, 2:3, 1:1), followed by incorporating sugar and stabilizers. The two-way preservation techniques of pasteurization (85oC, 15 min) and sterilizing techniques (121oC, 15 min) were used. Sensory acceptance by a trained panel from each formula of beverages, i.e., fruit pulp: coconut milk at ratios of 2:3 from each technique, was analyzed for physical and nutritional properties, fatty acid composition, and antioxidants. Results: A significant difference (p<0.05) was found among two-way processing techniques for the pH, oBrix, viscosity, and titratable acidity, as well as total sugars, crude protein, and crude fibre. The predominant fatty acid in both beverages was lauric acid. Vitamin A contents (mg/kg) were 0.3±0. and 0.2±0.01, respectively. Conclusion: This study showed Canistel fruit as a viable source for upgrading nutritional status when paired with coconut milk and other ingredients, and both processing techniques retained vitamin A, which fulfilled 8 – 10 % of the daily requirement by 200 ml of beverage.

In Silico Exploration of Isoxazole Derivatives of Usnic Acid: Novel Therapeutic Prospects Against α-Amylase for Diabetes Treatment.

Diabetes mellitus (DM) a metabolic disorder characterized by high blood sugar levels causing damage to various organs over time. Current anti-diabetic drugs have limitations and side effects, prompting a search for new inhibitors targeting the α-amylase enzyme. This study aims to discover such inhibitors from thirty isoxazole derivatives of usnic acid using in silico approaches. The potential inhibitory effects of compounds were investigated using ADMET, molecular docking, molecular dynamic simulation, principal component analysis and density functional theory studies. ADMET analysis exhibited a wide range of physicochemical, pharmacokinetic, and drug-like qualities with no significant side effects which were then investigated using molecular docking experiment to determine the lead compound with the best binding affinity for the α-amylase enzyme. All compounds showed good binding affinity against α-amylase enzyme (-7.9 to -9.2 kcal/mol) where compound-13 showed the best binding affinity of -9.2 kcal/mol forming hydrogen bonds with Leu162, Tyr62, Glu233 and Asp300 amino acids. Furthermore, the binding posture and the stability of the compound-13-α-amylase enzyme complex was confirmed by molecular dynamic simulation experiment. Moreover, compound-13 showed binding energy value of -27.92 ± 5.61 kcal/mol, which indicated it could be an α-amylase inhibitor. Additionally, the reactivity of compound-13 was further confirmed by density functional theory analysis. The above findings suggest compound-13 to be a potential α-amylase inhibitor in DM. And setting the stage for further in vitro and in vivo experimental validation.

Integrative metabolomics and chemometrics depict the metabolic alterations of differently processed red kidney beans (Phaseolus vulgaris L.) and in relation to in-vitro anti-diabetic efficacy

Red kidney beans (RKB) serve as a powerhouse packed with a plethora of largely unexplored extraordinary chemical entities with potential significance. However, their nutraceutical applications as a functional hypoglycemic food still lag behind and warrant further investigation. With a scope to optimize chemical and biological traits of RKB, green modification approaches (processing methods) seem inevitable. Accordingly, the current study offered the first integrative workflow to scrutinize dynamic changes in chemical profiles of differently processed RKB and their potential entanglements on diabetes mitigation using Ultra Performance Liquid Chromatography-mass spectrometry (UPLC-MS/MS) coupled with chemometrics. Different physical and biological processing treatments namely germination, fermentation, cooking and dehulling were preliminarily implemented on RKB. Complementarily, the concomitant metabolite alterations among differently processed RKB were monitored and interpreted. Next, an in-vitro α-amylase and α-glycosidase inhibitory testing of the differently processed samples was conducted and integrated with orthogonal projection to latent structures (OPLS) analysis to pinpoint the possible efficacy compounds. A total of 72 compounds spanning fatty acids and their glycerides, flavonoids, phenolic acids, amino acids, dipeptides, phytosterols and betaxanthins were profiled. Given this analysis and compared with raw unprocessed samples, it was found that flavonoids experienced notable accumulation during germination while both fermentation and dehulling approaches sharply intensified the content of amino acids and dipeptides. Comparably, Fatty acids, phytosterols and betaxanthins were unevenly distributed among the comparable samples. Admittedly, OPLS-DA revealed an evident discrimination among the processed samples assuring their quite compositional discrepancies. In a more targeted approach, kaempferol-O-sophoroside, quercetin, carlinoside and betavulgarin emerged as focal discriminators of sprouted samples while citrulline, linoleic acid, linolenoyl-glycerol and stigmasterol were the determining metabolites in cooked samples. Our efficacy experimental findings emphasized that the different RKB samples exerted profound inhibitory actions against both α-amylase and α-glycosidase enzymes with the most promising observations in the case of sprouted and cooked samples. Coincidently, OPLS analysis revealed selective enhancement of possible efficacy constituents primarily citrulline, formononetin, gamabufotalin, kaempferol-O-sophoroside, carlinoside, oleic acid and ergosterol in sprouted and cooked samples rationalizing their noteworthy α-amylase and α-glucosidase inhibitory activities. Taken together, this integrated work provides insightful perspectives beyond the positive impact of different processing protocols on bioactives accumulation and pharmacological traits of RKB expanding their utilization as functional hypoglycemic food to rectify diabetes.

Ultrasound-assisted synthesis of 4-thiazolidinone Schiff bases and their antioxidant, α-glucosidase, α-amylase inhibition, mode of inhibition and computational studies

AbstractDiabetes mellitus (DM) has become a growing concern to global public health, being at the forefront of acute disorders and causes of mortality across the globe. Clinically approved drugs that are currently being used are faced with severe side effects, consequently necessitating the development of new drugs with no/fewer side effects and improved pharmacological potency. Herein, we report a rapid and efficient synthesis of thiazolidinone Schiff bases (2a-2t) from benzylidenehydrazines and thioglycolic acid under neat conditions through ultra-sonication. All the synthesized compounds were obtained in exceptional yields (89–95%) and confirmed by 1D and 2D nuclear magnetic resonance (NMR) spectroscopy, as well as High-resolution mass spectrometry (HRMS). The synthesized compounds were then evaluated for their antidiabetic activity through α-glucosidase and α-amylase inhibitory potentials and their antioxidant activity through Nitric Oxide (NO), 2,2′-diphenyl-1-picrylhydrazyl (DPPH), and Ferric reducing antioxidant power (FRAP) assays. Among them, 2q (IC50 = 96.63 μM) and 2h (IC50 = 125.27 μM) emerged as the most potent derivatives against α-amylase relative to reference drug acarbose (IC50 = 131.63 µM), respectively. Antioxidant evaluation further revealed that the synthesized derivatives were excellent NO scavengers disclosing 2n (IC50 = 44.95 µM) as the most potent derivative. Moreover, in silico ADME calculations predicted these compounds to have excellent drug-like properties. Kinetic studies disclosed the mode of α-amylase inhibition as competitive while molecular docking studies of the most active derivatives performed into the binding active site of human pancreatic α-amylase enzyme deciphered their ligand-protein interactions that explicated their observed experimental potencies.

Synthesis of modified Schiff base appended 1,2,4-triazole hybrids scaffolds: elucidating the invitro and in silico α-amylase and α-glucosidase inhibitors potential.

The current study involves the synthesis of Schiff bases based on 1,2,4-triazoles skeleton and assessing their α-amylase and α-glucosidase profile. Furthermore, the precise structures of the synthesized derivatives were elucidated using various spectroscopic methods such as 1H-NMR, 13C-NMR and HREI-MS. Using glimepiride as the reference standard, the invitro α-glucosidase and α-amylase inhibitory activities of the synthesized compounds were evaluated in order to determine their potential anti-diabetic properties. All analogues showed varied range of inhibitory activity having IC50 values ranging from 17.09±0.72 to 45.34±0.03 μM (α-amylase) and 16.35±0.42 to 42.31±0.09 μM (α-glucosidase), respectively. Specifically, the compounds 1, 7 and 8 were found to be significantly active with IC50 values of 17.09±0.72, 19.73±0.42, and 23.01±0.04 μM (against α-amylase) and 16.35±0.42, 18.55±0.26, and 20.07±0.02 μM (against α-glucosidase) respectively. The obtained results were compared with the Glimepiride reference drug having IC50values of 13.02±0.11 μM (for α-glucosidase) and 15.04±0.02 μM (for α-amylase), respectively. The structure-activity relationship (SAR) studies were conducted based on differences in substituent patterns at varying position of aryl rings A and B may cause to alter the inhibitory activities of both α-amylase and α-glucosidase enzymes. Additionally, the molecular docking study was carried out to explore the binding interactions possessed by most active analogues with the active sites of targeted α-amylase and α-glucosidase enzymes.

Safety evaluation of an extension of use of the food enzyme α-amylase from the non-genetically modified Bacillus licheniformis strain AE-TA.

The food enzyme α-amylase (4-α-d-glucan glucanohydrolase; EC 3.2.1.1) is produced with the non-genetically modified microorganism Bacillus licheniformis strain AE-TA by Amano Enzyme Inc. A safety evaluation of this food enzyme was made previously, in which EFSA concluded that this food enzyme did not give rise to safety concerns when used in eight food manufacturing processes. Subsequently, the applicant has requested to extend its use to include one additional process and to revise the use levels. In this assessment, EFSA updated the safety evaluation of this food enzyme when used in a total of nine food manufacturing processes. As the food enzyme-total organic solids (TOS) are removed from the final foods in two food manufacturing processes, the dietary exposure to the food enzyme-TOS was estimated only for the remaining seven processes. Dietary exposure was calculated to be up to 0.382 mg TOS/kg body weight per day in European populations. Based on the data provided for the previous evaluation and the revised dietary exposure in the present evaluation, the Panel concluded that this food enzyme does not give rise to safety concerns under the revised intended conditions of use.

Safety evaluation of a second extension of use of the food enzyme α-amylase from the non-genetically modified Cellulosimicrobium funkei strain AE-AMT.

The food enzyme α-amylase (4-α-d-glucan glucanohydrolase i.e. EC 3.2.1.1) is produced with the non-genetically modified Cellulosimicrobium funkei strain AE-AMT by Amano Enzyme Inc. A safety evaluation of this food enzyme was made previously, in which EFSA concluded that the food enzyme did not give rise to safety concerns when used in seven food manufacturing processes. Subsequently, the applicant has requested to extend its use to include three additional processes. In this assessment, EFSA updated the safety evaluation of this food enzyme when used in a total of ten food manufacturing processes. As the food enzyme-total organic solids (TOS) are removed from the final foods in one food manufacturing process, the dietary exposure to the food enzyme-TOS was estimated only for the remaining nine processes. The dietary exposure was calculated to be up to 0.049 mg TOS/kg body weight (bw) per day in European populations. When combined with the no observed adverse effect level previously reported (230 mg TOS/kg bw per day, the highest dose tested), the Panel derived a margin of exposure of at least 4694. Based on the data provided for the previous evaluation and the revised margin of exposure in the present evaluation, the Panel concluded that this food enzyme does not give rise to safety concerns under the intended conditions of use.

Design, Synthesis, Biological Evaluation and Docking, ADME Studies of Novel Phenylsulfonyl Piperazine Analogues as α-Amylase Inhibitors

Diabetes mellitus (DM) stands as one of the most widespread diseases encountered today. It is primarily characterized by diminished insulin levels and heightened blood glucose concentrations. Inhibition of the α-amylase enzyme plays a pivotal role in the management of diabetes mellitus. Piperazine and sulfonamide groups are recognized for their extensive range of biological effects. The current study involved synthesizing five phenylsulfonyl piperazine derivatives. An evaluation of their α-amylase inhibitory capacities was conducted. Phenylsulfonyl piperazine derivatives (compounds 1-5) exhibited notable α-amylase enzymatic inhibition, with compound 4 showing the most substantial potential for inhibition. The inhibitory percentage of compound 4 (80.61±0.62) surpassed that of the standard drug acarbose (78.81±0.02). The molecular docking studies identified compound 4 as possessing the most substantial inhibitory effect on the α-amylase enzyme, with notable binding energy -8.2 kcal/mol. This compound exhibited specific interactions, including π-π stacking and π-anion interactions with key enzyme residues, solidifying its role as a potent inhibitor

Synthesis and In Silico Analysis of New Polyheterocyclic Molecules Derived from [1,4]-Benzoxazin-3-one and Their Inhibitory Effect against Pancreatic α-Amylase and Intestinal α-Glucosidase.

This study focuses on synthesizing a new series of isoxazolinyl-1,2,3-triazolyl-[1,4]-benzoxazin-3-one derivatives 5a-5o. The synthesis method involves a double 1,3-dipolar cycloaddition reaction following a "click chemistry" approach, starting from the respective [1,4]-benzoxazin-3-ones. Additionally, the study aims to evaluate the antidiabetic potential of these newly synthesized compounds through in silico methods. This synthesis approach allows for the combination of three heterocyclic components: [1,4]-benzoxazin-3-one, 1,2,3-triazole, and isoxazoline, known for their diverse biological activities. The synthesis procedure involved a two-step process. Firstly, a 1,3-dipolar cycloaddition reaction was performed involving the propargylic moiety linked to the [1,4]-benzoxazin-3-one and the allylic azide. Secondly, a second cycloaddition reaction was conducted using the product from the first step, containing the allylic part and an oxime. The synthesized compounds were thoroughly characterized using spectroscopic methods, including 1H NMR, 13C NMR, DEPT-135, and IR. This molecular docking method revealed a promising antidiabetic potential of the synthesized compounds, particularly against two key diabetes-related enzymes: pancreatic α-amylase, with the two synthetic molecules 5a and 5o showing the highest affinity values of 9.2 and 9.1 kcal/mol, respectively, and intestinal α-glucosidase, with the two synthetic molecules 5n and 5e showing the highest affinity values of -9.9 and -9.6 kcal/mol, respectively. Indeed, the synthesized compounds have shown significant potential as antidiabetic agents, as indicated by molecular docking studies against the enzymes α-amylase and α-glucosidase. Additionally, ADME analyses have revealed that all the synthetic compounds examined in our study demonstrate high intestinal absorption, meet Lipinski's criteria, and fall within the required range for oral bioavailability, indicating their potential suitability for oral drug development.

Substrate Influence on Enzymatic Activity in Cordyceps militaris for Health Applications

Cordyceps militaris, well known for its therapeutic potential in managing type-2 diabetes through the inhibition of α-amylase and α-glucosidase enzymes, was the central focus of this research, which investigated the influence of various cultivation substrates on its enzymatic inhibitory properties and bioactive compound content. Previous studies have primarily focused on the general pharmacological benefits of C. militaris but have not thoroughly explored how different substrates affect its bioactive profile and enzyme inhibitory activities. This study aimed to evaluate the impact of substrate selection on the enzyme inhibition activities and the levels of bioactive compounds such as cordycepin and adenosine in C. militaris, demonstrating that substrate selection markedly affects both these enzymes’ inhibition activities and bioactive compound levels. Particularly, C. militaris fruiting bodies grown on Brihaspa atrostigmella showed the highest concentrations of cordycepin (2.932 mg/g) and adenosine (1.062 mg/g). This substrate also exhibited the most potent α-glucosidase inhibition with an IC50 value of 336.4 ± 16.0 µg/mL and the most effective α-amylase inhibition with an IC50 value of 504.6 ± 4.2 µg/mL. Conversely, C. militaris cultivated on the solid residues of Gryllus bimaculatus displayed the strongest xanthine oxidase (XOD) inhibition, with the lowest IC50 value of 415.7 ± 11.2 µg/mL. These findings highlight the critical role of substrate choice in enhancing the medicinal properties of C. militaris, suggesting that optimized cultivation can enhance the bioactive properties for more effective natural therapies for diabetes and other metabolic disorders. This study not only extends the understanding of C. militaris’ pharmacological potential but also illustrates its applicability in developing customized treatment options.

In vitro and in silico assessment of antidiabetic and antioxidant potencies of secondary metabolites from Gymnema sylvestre

This study investigated the chemical constituents, antioxidant potential, and in vitro and in silico antidiabetic activity of Gymnema sylvestre. Column chromatography and spectroscopic techniques identified twelve compounds from the methanol extract, including 4 sterols (1–4), 5 triterpenoids (5–9), and 3 flavonoids (10–12). The chemophenetic significance of all compounds was also investigated. The antioxidant capacity of the extract and compounds (1–4) was evaluated using FRAP and DPPH assays. The extract exhibited strong free radical scavenging activity (IC50 = 48.34 µg/mL), while compounds (1–4) displayed varying degrees of efficacy (IC50 = 98.30–286.13 µg/mL). The FRAP assay indicated significant reducing power for both extract and compounds (58.54, 47.61, 56.61, and 49.11 mg Eq.VitC/g for extract and compounds 1 &2, 3, and 4, respectively). The antidiabetic potential was assessed through α-amylase and α-glucosidase enzyme inhibition assays. The crude extract demonstrated the most potent inhibition (IC50 = 218.46 and 57.42 µg/mL for α-glucosidase and α-amylase respectively) suggesting its potential for managing postprandial hyperglycaemia. In silico studies employed molecular docking and dynamics simulations to elucidate the interactions between identified compounds and α-amylase/α-glucosidase enzymes. The results revealed promising binding affinities between the compounds and target enzymes, with compound 6 demonstrating the highest predicted inhibitory activity with −10 kcal/mol and −9.1 kcal/mol for α-amylase and α-glucosidase, respectively. This study highlights the presence of diverse bioactive compounds in Gymnema sylvestre. The extract exhibits antioxidant properties and inhibits carbohydrate-digesting enzymes, suggesting its potential as a complementary therapeutic approach for managing hyperglycaemia associated with type 2 diabetes.

Extraction of Bioactive Compound-Rich Essential Oil from Cistus ladanifer L. by Microwave-Assisted Hydrodistillation: GC-MS Characterization, In Vitro Pharmacological Activities, and Molecular Docking

Cistus ladanifer L. is an aromatic and resinous perennial shrub commonly used in Moroccan folk medicine against a range of illnesses including skin problems, diabetes, diarrhea, and inflammation. The current investigation aims to determine the bioactive compounds of C. ladanifer essential oil (CL-Eo) extracted by microwave-assisted hydrodistillation and their biological properties using in vitro and molecular docking approaches. The GC-MS analysis identified linderol (17.76%), gamma-terpinene (17.55%), and borneol (13.78%) as main bioactive compounds. CL-Eo significantly inhibited α-amylase (IC50 = 0.41 ± 0.009 mg/mL), α-glucosidase (IC50 = 0.49 ± 0.002 mg/mL) and lipase (IC50 = 0.45 ± 0.004 mg/mL) enzymes. Moreover, CL-Eo showed significant hemoglobin glycation as well as antioxidant capacity as indicated by DPPH, ABTS, Frap and beta-carotene tests. The antimicrobial evaluation used disc-diffusion and microdilution tests in vitro. The results showed that CL-Eo had significant antibacterial activity, particularly against P. mirabilis (17.16 ± 1.04 mm), and moderate effects against L. innocua (13.48 ± 1.65 mm) and E. coli (12.47 ± 0.61 mm). In addition, it demonstrated potent antifungal activity against C. albicans (18.01 ± 0.91 mm) and C. tropicalis (16.45 ± 0.32 mm). The MIC and MBC tests provided confirmation that CL-Eo exhibited potent growth inhibition. The MIC ranged from 0.25 to 8.0% v/v and the MBC or MFC ranged from 0.25 to 16.0% v/v Eo. The tolerance level ratio showed bactericidal and fungicidal effects against tested microbial strains in varying degrees. According to these data, CL-Eo might be suggested as a promising candidate for drug development, specifically for combating candidiasis and diabetes.

Synthesis and characterization of newly phthalocyanine molecules: Their enzyme inhibition and antioxidant properties, in silico and in vitro

Pcs exhibiting maximum absorption in the phototherapeutic window continue to shine as a beacon of hope in the treatment of cancer. In particular, they maintain skin sensitivity after treatment and can treat deep-seated tumors by stimulating them with broad-spectrum radiation. This makes them advantageous compared to their counterparts. In this study, Novel 1,2,3-triazole schiff base (5a), its methoxy homolog (5b), and their silicon complexes (SiPc-6a and SiPc-6b) were synthesized. Their proposed structures were confirmed by FT-IR, NMR, UV–vis and MS instrumental techniques. Compound (6b) showed inhibitory activity on amylase and glucosidase enzymes. Moreover, considering the glucosidase activity, compound (6b) (IC50, 22.4 ± 1.0 µM) was observed to be more effective than the standard compound (IC50, 186.1 ± 5.8 µM). Molecular docking studies showed that the synthesized compounds bind to the same enzymes with high affinity. The binding energy of SiPc-6a compound with α-amylase, α-glucosidase and tyrosinase enzymes are -10.28, -11.31 and -11.9 kcal/mol, respectively. And another compound, SiPc-6b, has a binding energy of -11.46, -10.11 and -10.27 kcal/mol with a-amylase, a-glucosidase and tyrosinase enzymes, respectively. Based on experimental results that support each other with binding energy values in quality and quantity indicating efficient binding, it is concluded that these compounds can be used in candidate drug discovery. Beside these, as a result of the studies, it was understood that all molecules have antioxidant activity. Additionally, molecular electrostatic potentials, frontier orbital analysis, natural bond orbital (NBO) properties of compounds calculated with DFT and TD-DFT methods and these properties associated with structural properties.

Evaluation of the Inhibitory Effect on α-glucosidase and α-amylase Enzymes of Triterpenes Isolated from Commelina diffusa Burm.f.

Evaluation of the Inhibitory Effect on α-glucosidase and α-amylase Enzymes of Triterpenes Isolated from Commelina diffusa Burm.f.

Novel benzene sulfonamide-piperazine hybrid compounds: design, synthesis, antioxidant, enzyme inhibition activities and docking, ADME profiling studies.

Benzene sulfonamides are an important biological substituent for several activities. In this study, hybridization of benzene sulfonamide with piperazine derivatives were investigated for their antioxidant capacity and enzyme inhibitory potencies. Six molecules were synthesized and characterized. DPPH, ABTS, FRAP, CUPRAC, chelating and phosphomolybdemum assays were applied to evaluate antioxidant capacities. Results show that compounds have high antioxidant capacity and compound 4 has the best antioxidant activity among them. Compound 4 has higher antioxidant activity than references for FRAP (IC50: 0.08 mM), CUPRAC (IC50: 0.21 mM) and phosphomolybdenum (IC50: 0.22 mM) assays. Besides this, compound 4 has moderate DPPH and ABTS antioxidant capacity. Furthermore, enzyme inhibition activities of these molecules were investigated against AChE, BChE, tyrosinase, α-amylase and α-glucosidase enzymes. It was revealed that all compounds have good enzyme inhibitory potential except for α-amylase enzyme. The best inhibitory activities were observed for AChE with compound 5 the same value (IC50: 1.003 mM), for BChE with compounds 2 and 5 the same value (IC50: 1.008 mM), for tyrosinase compound 4 (IC50: 1.19 mM), and for α-glucosidase with compound 3 (IC50: 1.000 mM). Docking studies have been conducted with these molecules, and the results correlate well with the inhibitory assays.

Fluorinated indeno-quinoxaline bearing thiazole moieties as hypoglycaemic agents targeting α-amylase, and α-glucosidase: synthesis, molecular docking, and ADMET studies

Inhibition of α-glucosidase and α-amylase are key tactics for managing blood glucose levels. Currently, stronger, and more accessible inhibitors are needed to treat diabetes. Indeno[1,2-b] quinoxalines-carrying thiazole hybrids 1–17 were created and described using NMR. All analogues were tested for hypoglycaemic effect against STZ-induced diabetes in mice. Compounds 4, 6, 8, and 16 were the most potent among the synthesised analogues. These hybrids were examined for their effects on plasma insulin, urea, creatinine, GSH, MDA, ALT, AST, and total cholesterol. Moreover, these compounds were tested against α-glucosidase and α-amylase enzymes in vitro. The four hybrids 4, 6, 8, and 16 represented moderate to potent activity with IC50 values 0.982 ± 0.04, to 10.19 ± 0.21 for α-glucosidase inhibition and 17.58 ± 0.74 to 121.6 ± 5.14 μM for α-amylase inhibition when compared to the standard medication acarbose with IC50=0.316 ± 0.02 μM for α-glucosidase inhibition and 31.56 ± 1.33 μM for α-amylase inhibition. Docking studies as well as in silico ADMT were done.

Chemical Composition of Extracts and Fractions from Miconia Ibaguensis (Melastomataceae) Leaves and Evaluation of Biological Activities.

The study aimed to assess the chemical composition of Miconia ibaguensis leaves extracts and fractions obtained from the ethanolic extract (EE), along with evaluating their antifungal, antibacterial, antidiabetic, and antioxidant activities. The ethyl acetate fraction (EAF) exhibited potent antifungal activity against Candida spp (1.95-3.90 μg mL-1) and potent antioxidant activity in the DPPH (1.74±0.07 μg mL-1), FRAP (654.01±42.09 μmol ETrolox/gsample), and ORAC (3698.88±37.28 μmol ETrolox/gsample) methods. The EE displayed inhibition against the α-amylase enzyme (8.42±0.05 μg mL-1). Flavonoids, hydrolysable tannins, triterpenoids, and phenolic acids, identified in the EE and fractions via (-)-HPLC-ESI-MS/MS analysis, were found to contribute to the species' biological activity potentially. These findings suggest promising avenues for further research and potential applications in pharmacology and natural products, offering new possibilities in the fight against global health issues.

The Effectiveness of the Α-Amylase Enzyme Inhibition by Several Traditional Medicinal Ingredients Black Turmeric, Aromatic Ginger, Black Cumin, Forest Bee Honey and Sweet Leaves in Ready to Drink Formulation

The inhibition of α-amylase enzymes can delay the remaining carbohydrates in the small intestine and reduce the travel of postprandial blood glucose, therefore the content of compounds in the form of tannins, flavonoids, saponins and terpen is believed to be able inhibit the α-amylase enzymes. Knowing the effectiveness of α-amylase enzyme inhibition by some traditional medicine ingredients (Curcuma caesia, Kaempferia galanga, Nigella sativa, Apis dorsata, and Stevia rebaudiana) and organoleptic properties of the ready to drink formulation. This study is an experimental study using the design "Pretest-Posttest with control Groug" on the sample in the form of liquid extracts. Plant liquid extract is tested for its inhibition of α-amylase and used as a formulation of herbal drink ready to drink. The result IC50 values of black turmeric extract (6.46 mg/ml), aromatic ginger (6.10 mg/ml), black cumin (7.36 mg/ml), forest bee honey (2.59 mg//ml) and sweet leaves (4,85 mg/ml). The results of IC50 formulations 1 (8.03 mg/ml) and 2 (14.18 mg/ml) and glibenclamide values are (2.53 mg/ml). Conclusion the effectiveness of α-amylase inhibition of sweet leaf extract is better than other extracts and formulation 1 is better than formulation 2.

Comparative account of phytochemicals, their bioactivities, triterpenoid saponins, and stigmasterol content from two memory-boosting herbs [Bacopa monnieri (L.) Wettst. and Bacopa floribunda (R.Br.) Wettst.]

Bacopa monnieri and Bacopa floribunda are extensively utilized in various Ayurvedic remedies because of their cognitive-enhancing properties. Phytochemicals, antioxidants, anti-diabetic, anti-acetylcholine esterase activities, and the detection of bioactive substances (triterpenoid saponins and stigmasterol) were examined using HPLC and HR-LC-MS. The results showed that the aqueous extract of B. floribunda had the highest TPC (60.44 ± 5.24 mg TAE/g extract), while the acetonitrile extract had the lowest content (9.35 ± 0.64 mg TAE/g extract). The highest TFC was found in the acetone extracts of B. monnieri and B. floribunda (63.69 ± 13.48 and 61.44 ± 2.94 mg CE/g extract, respectively). Additionally, the acetone extracts of B. floribunda and B. monnieri revealed the greatest TTC (256.8 ± 7.73 mg CE/g extract) and TSC (363.5 ± 10.6 mg DE/g extract), respectively. In antioxidant studies, the acetone and methanol extracts of B. monnieri showed the highest DPPH radical scavenging, FRAP, and MC activities (68.24 ± 1.31 mg AAE/g extract, 160.43 ± 4.34 mg Fe(II)/g extract, and 283.13 ± 1.46 mg EDTA/g extract, respectively). The acetone extract of B. floribunda had better ABTS radical scavenging and PMA (13.29 ± 0.53 mg TE/g extract and 127.7 ± 0.51 mg AAE/g extract, respectively). The acetonitrile extract of B. floribunda showed considerable inhibitory effects against α-amylase (71.89 ± 10.1%), α-glucosidase (93.89 ± 0.19%), and acetylcholine esterase (80.92 ± 0.6%) enzymes. The presence of stigmasterol and four triterpenoid saponins were also confirmed by HPLC. The total amount of triterpenoid saponins was found higher in B. floribunda (4.97 ± 0.012 mg/g DW) than B. monnieri (3.96 ± 0.012 mg/g DW). In contrast, B. monnieri (5.13 ± 0.12 mg/g DW) exhibited the highest stigmasterol content as compared to B. floribunda (3.97 ± 0.35 mg/g DW). For the first time, we report B. floribunda as a potent source of triterpenoid saponins and could be a substitute for B. monnieri.

Antiglycating Effects of Spirulina platensis Aqueous Extract on Glucose-Induced Glycation of Bovine Serum Albumin.

Glucose, the predominant carbohydrate in the human body, initiates nonenzymatic reactions in hyperglycemia, potentially leading to adverse biochemical interactions. This study investigates the interaction between glucose and Bovine Serum Albumin (BSA), along with the protective effects of Spirulina platensis PCC 7345 aqueous extract. Phycobiliproteins (phycocyanin, phycoerythrin, and allophycocyanin) in the extract were quantified using spectrophotometry. The extract's anti-glycation potential was assessed by analyzing its effects on albumin glycation, fluorescent advanced glycation end products (AGEs), thiol group oxidation, and β-amyloid structure generation. Additionally, its antidiabetic potential was evaluated by measuring α-amylase and α-glucosidase enzyme inhibition. Results indicate that the Spirulina extract significantly mitigated ketoamine levels, fluorescence, and protein-carbonyl production induced by glucose, demonstrating a 67.81 % suppression of AGE formation after 28 days. Moreover, it effectively inhibited amyloid formation in BSA cross-linkages. These findings suggest the potential of S. platensis as an anti-glycation and antidiabetic agent, supporting its consideration for dietary inclusion to manage diabetes and associated complications.