Polysaccharides (AOPs) were extracted from Alpiniae oxyphyllae fructus using three distinct methods: hot water (AOP-HW), hydrochloric acid (AOP-AC), and NaOH/NaBH4 (AOP-AL). This study systematically investigated and compared the physicochemical properties, structural characteristics, antioxidant activities, and α-amylase inhibitory activities of the extracted polysaccharides. Among the three AOPs, AOP-AC exhibited the highest yield (13.76%) and neutral sugar content (80.57%), but had the lowest molecular weight (121.28 kDa). Conversely, AOP-HW had the lowest yield (4.54%) but the highest molecular weight (385.42 kDa). AOP-AL was predominantly composed of arabinose (28.42 mol%), galacturonic acid (17.61 mol%), and galactose (17.09 mol%), while glucose was the major sugar in both AOP-HW (52.31 mol%) and AOP-AC (94.77 mol%). Functionally, AOP-AL demonstrated superior scavenging activities against DPPH, hydroxyl, and ABTS radicals, whereas AOP-AC exhibited the strongest inhibitory effect on α-amylase. These findings indicate that the extraction solvent significantly influences the physicochemical and biological properties of AOPs, thus guiding the selection of appropriate extraction methods for specific applications. The results of this study have broad implications for industries seeking natural polysaccharides with antioxidant and enzymatic inhibitory properties.

The Food and Agricultural Organization estimates a 17% loss in the food production chain, making it imperative to adopt scientific and technological approaches to address this issue for sustainability. Industrial food production waste and its value-added applications, particularly in relation to a wide variety of pathogenic microorganisms and the health-related effects have not been thoroughly investigated. This study explores the potential of food production waste extracts-lemon peel (LP), hot trub (HT), and coffee silverskin (CSS) as sources of bioactive compounds. Extraction was conducted using hydro-methanolic extraction with yields in LP (482 mg/1 g) > HT (332 mg/1 g) > CSS (20 mg/1 g). The agar diffusion assay revealed the substantial antibacterial activity of all three extracts against Erwinia Amylovora, Escherichia coli, Bacillus subtilis, and Bacillus aquimaris. All extracts demonstrated activity against Gram-positive and Gram-negative bacteria, displaying minimum inhibitory concentrations effective against pathogenic bacteria like Listeria monocytogenes, Staphylococcus aureus, Vibrio parahaemolyticus, and Salmonella enterica. Total phenolic content (TPC in mg GAE/1g) was 100, 20, and 100 for CSS, HT, and LP, respectively. Antioxidant activity by ABTS indicated IC50 of 3.09, 13.09, and 2.61 for LP, HT, and CSS, respectively. Also, the antioxidant activity of the extracts was further confirmed by DPPH assay with the best activity in CSS (9.84 GAEg-1) and LP (9.77 mg of GAEg-1) rather than in HT (1.45 GAEg-1). No adverse cytotoxic effects on HaCaT cells were observed. Pancreatic amylase inhibition demonstrated antidiabetic potential, with LP showing the highest levels (92%). LC-MS characterization identified polyphenols as the main compounds in CSS, prenylated compounds in HT, and flavanols in LP. The findings imply the potential sustainable use of food production waste in industry.

Alzheimer\'s disease (AD) and diabetes are non-communicable diseases with global impacts. Inhibitors of acetylcholinesterase (AChE) and butyrylcholinesterase (BChE) are suitable therapies for AD, while α-amylase and α-glucosidase inhibitors are employed as antidiabetic agents. Compounds were isolated from the medicinal plant Terminalia macroptera and evaluated for their AChE, BChE, α-amylase, and α-glucosidase inhibitions. From 1H and 13C NMR data, the compounds were identified as 3,3\'-di-O-methyl ellagic acid (1), 3,3\',4\'-tri-O-methyl ellagic acid-4-O-β-D-xylopyranoside (2), 3,3\',4\'-tri-O-methyl ellagic acid-4-O-β-D-glucopyranoside (3), 3,3\'-di-O-methyl ellagic acid-4-O-β-D-glucopyranoside (4), myricetin-3-O-rhamnoside (5), shikimic acid (6), arjungenin (7), terminolic acid (8), 24-deoxysericoside (9), arjunglucoside I (10), and chebuloside II (11). The derivatives of ellagic acid (1-4) showed moderate to good inhibition of cholinesterases, with the most potent being 3,3\'-di-O-methyl ellagic acid, with IC50 values of 46.77 ± 0.90 µg/mL and 50.48 ± 1.10 µg/mL against AChE and BChE, respectively. The compounds exhibited potential inhibition of α-amylase and α-glucosidase, especially the phenolic compounds (1-5). Myricetin-3-O-rhamnoside had the highest α-amylase inhibition with an IC50 value of 65.17 ± 0.43 µg/mL compared to acarbose with an IC50 value of 32.25 ± 0.36 µg/mL. Two compounds, 3,3\'-di-O-methyl ellagic acid (IC50 = 74.18 ± 0.29 µg/mL) and myricetin-3-O-rhamnoside (IC50 = 69.02 ± 0.65 µg/mL), were more active than the standard acarbose (IC50 = 87.70 ± 0.68 µg/mL) in the α-glucosidase assay. For α-glucosidase and α-amylase, the molecular docking results for 1-11 reveal that these compounds may fit well into the binding sites of the target enzymes, establishing stable complexes with negative binding energies in the range of -4.03 to -10.20 kcalmol-1. Though not all the compounds showed binding affinities with cholinesterases, some had negative binding energies, indicating that the inhibition was thermodynamically favorable.

In this study, the α-glucosidase (maltase-glucoamylase: MGAM) and α-amylase inhibitory properties elicited by xylooligosaccharides (XOSs) prepared from dulse xylan were analysed as a potential mechanism to control postprandial hyperglycaemia for type-2 diabetes prevention and treatment. Xylan was purified from red alga dulse powder and used for enzymatic hydrolysis using Sucrase X to produce XOSs. Fractionation of XOSs produced xylobiose (X2), β-(1→3)-xylosyl xylobiose (DX3), xylotriose (X3), β-(1→3)-xylosyl-xylotriose (DX4), and a dulse XOS mixture with n ≥ 4 xylose units (DXM). The different fractions exhibited moderate MGAM (IC50 = 11.41-23.44 mg/mL) and α-amylase (IC50 = 18.07-53.04 mg/mL) inhibitory activity, which was lower than that of acarbose. Kinetics studies revealed that XOSs bound to the active site of carbohydrate digestive enzymes, limiting access to the substrate by competitive inhibition. A molecular docking analysis of XOSs with MGAM and α-amylase clearly showed moderate strength of interactions, both hydrogen bonds and non-bonded contacts, at the active site of the enzymes. Overall, XOSs from dulse could prevent postprandial hyperglycaemia as functional food by a usual and continuous consumption.

UNASSIGNED: This work presents proteins, amino acids profiles and antioxidant and properties of camel and cow milk fractions produced using an integrated coagulation-centrifugation process.
UNASSIGNED: Antioxidant activity using DPPH radical scavenging assay; and antidiabetic activity antidiabetic activity using in vitro α-amylase inhibitory activity were assessed on defatted milk fractions and their extracts using water/ethanol or HCl/ethanol solvents. Protein profiles and amino acids composition were analyzed by high-performance liquid chromatography.
UNASSIGNED: The predominant protein found in cow and camel milk was β-casein in sodium caseinate, β-lactoglobulin was found in the whey of cow milk, whereas α-lactalbumin was detected in the whey fractions of camel. The primary amino acids (comprising 1% to 5.2%) in skim milk and sweet whey milk were leucine, proline, and lysine. However, acid whey, casein fractions (sodium caseinate, and β-casein) from both camel and cow milk exhibited elevated concentrations of histidine, leucine, lysine and proline (1.12 - 6.62%). Camel milk and its different protein fractions showed an interesting in vitro α-amylase inhibitory activity varying, according to different milk fractions and extraction methods, from 19.10 ± 1.40 to 97.40 ± 1.50%. Whatever the used method, the whey fractions from camel milk, both acid and sweet, displayed ed the highest antioxidant activity. Principal components analysis showed a positive correlation between the total phenols content, antioxidant (DPPH assay) and antidiabetic (α amylase inhibition test) activities within the milk fractions. Sweet and acid cow milk fractions seem to be the most promising for deeper exploration of in vivo biological activities and are promising milk derivatives for specific nutritional diet and/or functional food formulation.

Ligustrum vulgare (LV), widely cultivated in Europe and often used in hedges, has been historically recognized in folk medicine for its potential health benefits. This study focused on exploring the untargeted identification of secondary metabolites in ethanol extracts (70% v/v) from different morphological parts (young shoots, leaves, flowers and fruits) of LV at various stages of plant development, using ultra-high-performance liquid chromatography with high-resolution mass spectrometry (UHPLC-HRMS). Additionally, the selected biological activities (antioxidant activity, cyclooxygenase-2 inhibition (COX-2), α-amylase inhibition and cytotoxicity) of the tested extracts were determined. Untargeted metabolomics showed that LV extracts were a rich source of phenylethanoid compounds, flavonoids, iridoids and their derivatives. The flowers of LV had the highest content of oleuropein (33.43 ± 2.48 mg/g d.w.). The lowest antioxidant activity was obtained for ripe and post-seasonal fruits, while in the case of other samples, the activity was at a similar level. All tested extracts showed α-amylase and COX-2 inhibitory activity. In addition, LV extracts showed strong antiproliferative properties in colorectal (HT29) and liver (HepG2) cancer cell lines. The obtained results show the difference in the content of bioactive compounds in various morphological parts of Ligustrum vulgare. These differences may influence the multifaceted medicinal potential of this plant.

UNASSIGNED: Novel α-amylase inhibitors play a crucial role in managing diabetes and obesity, contributing to improved public health by addressing these challenging and prevalent conditions. Moreover, the synthesis of anti-oxidant agents is essential due to their potential in combating oxidative stress-related diseases and promoting overall health.
UNASSIGNED: Synthesis of thoisemicarbazone derivatives of 2,4-dichlorophenyl acetic acid and to screened them for their biological activities.
UNASSIGNED: Thiosemicarbazone derivatives (4-13) were synthesized by refluxing 2,4-dichlorophenyl acetic acid with sulfuric acid in ethanol to get the ester (2), which was further refluxed with thiosemicarbazide to get compound (3). Finally, different aromatic aldehydes were refluxed with compound (3) in ethanol in catalytic amount of acetic acid to obtained the final products (4-13). Using modern spectroscopic techniques including HR-ESI-MS, 13C-, and 1H NMR, the structures of the created derivatives were confirmed.
UNASSIGNED: The synthesized derivatives showed excellent to good inhibitory activity in the range of IC50 values of 4.95 ± 0.44 to 69.71 ± 0.05 µM against α-amylase enzyme when compared to standard drug acarbose (IC50 = 21.55 ± 1.31 µM). In case of iron chelating activity, these products showed potent activity better than standard EDTA (IC50 = 66.43 ± 1.07 µM) in the range of IC50 values of 22.43 ± 2.09 to 61.21 ± 2.83 µM. However, the obtained products also show excellent to good activity in the range of IC50 values of 28.30 ± 1.17 to 64.66 ± 2.43 µM against hydroxyl radical scavenging activity when compared with standard vitamin C (IC50 = 60.51 ± 1.02 µM). DFT used to calculate different reactivity factors including ionization potential, electronegativity, electron affinity, chemical softness, and chemical hardness were calculated using frontier molecular orbital (FMO) computations. The molecular docking studies for the synthesized derivatives with α-amylase were carried out using the AutoDock Vina to understand the binding affinities with active sites of the protein.

Copper(II) complexes with a general formula [Cu2(3,4-F2C6H3CH2COO)4(L)2], where L = 2-methylpyridine (1) and 3-methylpyridine (2), are reported here. The FTIR spectra of the complexes confirmed the bridging bidentate coordination mode of the carboxylate ligand. The low (475 and 449 cm-1) and strong (727 & 725 cm-1) intensity bands in the FTIR spectra, due to Cu-N stretches and pyridyl ring vibrations, confirmed coordination of the 2-/3-methyl pyridine co-ligands in complexes 1 and 2, respectively. A binuclear paddlewheel structural arrangement with a square pyramidal geometry was confirmed for copper atoms in the complexes via single-crystal X-ray analysis. The DPPH, •OH radical, and α-amylase enzyme inhibition assays showed higher activities for the complexes than for the free ligand acid. The binding constant (Kb = 1.32 × 105 for 1 and 5.33 × 105 for 2) calculated via UV-VIS absorption measurements and docking scores (-6.59 for 1 and -7.43 for 2) calculated via molecular docking showed higher SS-DNA binding potential for 2 compared to 1. Viscosity measurement also reflected higher DNA binding ability for 2 than 1. Both complexes 1 and 2 (docking scores of -7.43 and -6.95, respectively) were found to be more active inhibitors than the free ligand acid (docking score of -5.5159) against the target α-amylase protein. This in silico study has shown that the herein reported compounds follow the rules of drug-likeness and exhibit good potential for bioavailability.

This research aimed to determine the biofunctional properties of wheat flour (WF) protein fractions and modifications to the antioxidant, anti-α-amylase and anti-angiotensin-I converting enzyme (ACE) activities induced by the action of digestive endopeptidases in vitro. A molecular characterization of the most abundant protein fractions, i.e., albumins, glutelins-1, glutelins-2 and prolamins, showed that low- and high-MW polypeptides rich in cysteine, glutamic acid and leucine were present in albumins and glutelins, whereas low-MW subunits with a high proportion of polar amino acids prevailed in prolamins. Prolamins exhibited the second-highest water holding capacity (54%) after WF (84%), while albumins provided superior foam stability (76%). Prolamins, glutenins-1 and globulins demonstrated the highest antioxidant activity (up to 95%, 68% and 59%, respectively) both before and after hydrolysis with pepsin (P-H) or trypsin-chymotrypsin (TC-H). Prolamins, globulins and WF strongly inhibited α-amylase (>90%) before and after TC-H, and before P-H (55-71%). Moreover, P-H significantly increased α-amylase inhibition by albumins from 53 to 74%. The fractions with strong ACE inhibitory activity (70-89%) included prolamins and globulins after TC-H or P-H, as well as globulins before TC-H and WF before P-H. This novel evidence indicates that WF protein fractions and their peptide-enriched P and TC hydrolysates are excellent sources of multifunctional bioactives with antioxidant, antihyperglycemic and antihypertensive potential.

Recently, consumer preferences for bilberries have increased markedly. This fact is probably related to their natural constituents, such as phenolic compounds including anthocyanins and tannins, as well as the vitamins and minerals they contain. Phenolic compounds are known for their numerous beneficial effects on human health. Moreover, bilberry fruits have been shown to inhibit the activity of carbohydrate hydrolyzing enzymes, which can significantly decrease the postprandial increase in blood glucose levels. Thus, the aim of the present study is to investigate the inhibitory effect of Vaccinium myrtillus L. extracts on key enzyme α-amylase, linked to type 2 diabetes. No data have been published on the inhibitory properties of Vaccinium myrtillus L. fruits growing wild in Bulgaria against carbohydrate enzymes. Bilberry extracts were analyzed for total polyphenols, total anthocyanin content, antioxidant activity and their inhibitory properties against α-amylase. The contents of flavonols, anthocyanins and stilbenes were determined by HPLC analysis. The identified flavonols in the analyzed bilberry extracts were mainly represented by quercetin derivatives as rutinoside. The predominant anthocyanins for both aqueous and organic solvents were delphinidin-3-galactoside and malvidin-3-glucoside. The results revealed that bilberry extracts are effective inhibitors of α-amylase, with IC50 values from 20.8 to 194.8 μg GAE/mL. All the samples proved to have antioxidant activity measured by three different in vitro assays (FRAP, CUPRAC and DPPH). The inhibitory properties of V. myrtillus L. extracts may provide a new direction in the development and research of new pharmaceuticals for the suppression of postprandial hyperglycemia in diabetic patients.