Journal articles: 'Acid α-glucosidase'

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Kato, Naoki, Sachie Suyama, Masao Shirokane, Masashi Kato, Tetsuo Kobayashi, and Norihiro Tsukagoshi. "Novel α-Glucosidase from Aspergillus nidulans with Strong Transglycosylation Activity." Applied and Environmental Microbiology 68, no. 3 (March 2002): 1250–56. http://dx.doi.org/10.1128/aem.68.3.1250-1256.2002.

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ABSTRACT Aspergillus nidulans possessed an α-glucosidase with strong transglycosylation activity. The enzyme, designated α-glucosidase B (AgdB), was purified and characterized. AgdB was a heterodimeric protein comprising 74- and 55-kDa subunits and catalyzed hydrolysis of maltose along with formation of isomaltose and panose. Approximately 50% of maltose was converted to isomaltose, panose, and other minor transglycosylation products by AgdB, even at low maltose concentrations. The agdB gene was cloned and sequenced. The gene comprised 3,055 bp, interrupted by three short introns, and encoded a polypeptide of 955 amino acids. The deduced amino acid sequence contained the chemically determined N-terminal and internal amino acid sequences of the 74- and 55-kDa subunits. This implies that AgdB is synthesized as a single polypeptide precursor. AgdB showed low but overall sequence homology to α-glucosidases of glycosyl hydrolase family 31. However, AgdB was phylogenetically distinct from any other α-glucosidases. We propose here that AgdB is a novel α-glucosidase with unusually strong transglycosylation activity.

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Ponce, Elvira, David P. Witte, Rochelle Hirschhorn, Maryann L. Huie, and Gregory A. Grabowski. "Murine Acid α-Glucosidase." American Journal of Pathology 154, no. 4 (April 1999): 1089–96. http://dx.doi.org/10.1016/s0002-9440(10)65361-8.

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Alqahtani, Ali S., Syed Hidayathulla, Md Tabish Rehman, Ali A. ElGamal, Shaza Al-Massarani, Valentina Razmovski-Naumovski, Mohammed S. Alqahtani, Rabab A. El Dib, and Mohamed F. AlAjmi. "Alpha-Amylase and Alpha-Glucosidase Enzyme Inhibition and Antioxidant Potential of 3-Oxolupenal and Katononic Acid Isolated from Nuxia oppositifolia." Biomolecules 10, no. 1 (December 30, 2019): 61. http://dx.doi.org/10.3390/biom10010061.

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Nuxia oppositifolia is traditionally used in diabetes treatment in many Arabian countries; however, scientific evidence is lacking. Hence, the present study explored the antidiabetic and antioxidant activities of the plant extracts and their purified compounds. The methanolic crude extract of N. oppositifolia was partitioned using a two-solvent system. The n-hexane fraction was purified by silica gel column chromatography to yield several compounds including katononic acid and 3-oxolupenal. Antidiabetic activities were assessed by α-amylase and α-glucosidase enzyme inhibition. Antioxidant capacities were examined by 2,2-diphenyl-1-picrylhydrazyl (DPPH) and 2,2′-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) (ABTS) scavenging assays. Further, the interaction between enzymes (α-amylase and α-glucosidase) and ligands (3-oxolupenal and katononic acid) was followed by fluorescence quenching and molecular docking studies. 3-oxolupenal and katononic acid showed IC50 values of 46.2 μg/mL (101.6 µM) and 52.4 μg/mL (119.3 µM), respectively against the amylase inhibition. 3-oxolupenal (62.3 µg/mL or 141.9 μM) exhibited more potent inhibition against α-glucosidases compared to katononic acid (88.6 µg/mL or 194.8 μM). In terms of antioxidant activity, the relatively polar crude extract and n-butanol fraction showed the greatest DPPH and ABTS scavenging activity. However, the antioxidant activities of the purified compounds were in the low to moderate range. Molecular docking studies confirmed that 3-oxolupenal and katononic acid interacted strongly with the active site residues of both α-amylase and α-glucosidase. Fluorescence quenching results also suggest that 3-oxolupenal and katononic acid have a good affinity towards both α-amylase and α-glucosidase enzymes. This study provides preliminary data for the plant’s use in the treatment of type 2 diabetes mellitus.

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Saleh, Mohammed S. M., Mohammad Jamshed Siddiqui, Nabil Ali Al-Mekhlafi, Hussah Abdullah Alshwyeh, Ahmed Mediani, Nor Hadiani Ismail, and Yusof Kamisah. "Gas Chromatography-Mass Spectrometry Coupled with Multivariate Statistical Analysis to Identify the Alpha Glucosidase Inhibitors from Flesh of Salacca zalacca Fruits and Their Molecular Docking Studies." Evidence-Based Complementary and Alternative Medicine 2021 (January 25, 2021): 1–10. http://dx.doi.org/10.1155/2021/8867773.

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Fruit of salak (Salaaca zalacca) is traditionally used and commercialized as an antidiabetic agent. However, scientific evidence to prove this folk claim is quite lacking. Therefore, this research was aimed to evaluate the α-glucosidase inhibition activity of S. zalacca fruit and identify the bioactive compounds. The fruits were extracted by different ratios of ethanol and water (0, 20, 40, 60, 80, 100%, v/v) to get E0 (100% water), E20 (20% ethanol), E40 (40% ethanol), E60 (60% ethanol), E80 (80% ethanol), and E100 (100% ethanol) extracts. The extracts obtained were subjected to the α-glucosidase inhibitory assay. Gas chromatography-mass spectrometry- (GC-MS-) based metabolomics approach was used in profiling the bioactive metabolites present in the extracts. Orthogonal partial least square (OPLS) was used to correlate GC-MS data and α-glucosidase assay results to identify the possible chemical markers. All active compounds identified were subjected to molecular docking. The extracts from the S. zalacca fruit showed potent inhibition activity against α-glucosidase. The IC50 values from the α-glucosidase inhibitory assay ranged between 16 and 275 µg/ml. Overall, E60 displayed significantly higher α-glucosidase inhibition activity, while E0 showed the lowest α-glucosidase inhibition activity. Major compounds detected in S. zalacca fruits were sugars, fatty acids, and sterols, including myo-inositol, palmitic acid, stearic acid, and β-sitosterol. Moreover, the results obtained from molecular docking indicated that palmitic acid and β-sitosterol were close to the active side of the enzyme. Some of the residues that interacted include HID295, ASN259, LEU313, LYS125, PHE159, VAL216, PHE178, TYR72, TYR158, HIE315, ARG315, and PHE303. The bioassay result strongly suggests that E60 extract from S. zalacca fruits has potential α-glucosidase inhibitory activity. The hydrophobic compounds, including palmitic acid and β-sitosterol, were found to induce the α-glucosidase inhibition activity.

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Ernawati, Teni, Maksum Radji, Muhammad Hanafi, Abdul Mun’im, and Arry Yanuar. "Cinnamic Acid Derivatives as α-Glucosidase Inhibitor Agents." Indonesian Journal of Chemistry 17, no. 1 (April 1, 2017): 151. http://dx.doi.org/10.22146/ijc.23572.

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This paper reviews biological activity of some cinnamic acid derivative compounds which are isolated from natural materials and synthesized from the chemical compounds as an agent of α-glucosidase inhibitors for the antidiabetic drug. Aegeline, anhydroaegeline and aeglinoside B are natural products isolated compounds that have potential as an α-glucosidase inhibitor. Meanwhile, α-glucosidase inhibitor class of derivatives of cinnamic acid synthesized compounds are p-methoxy cinnamic acid and p-methoxyethyl cinnamate. Chemically, cinnamic acid has three main functional groups: first is the substitution of the phenyl group, second is the additive reaction into the α-β unsaturated, and third is the chemical reaction with carboxylic acid functional groups. The synthesis and modification of the structure of cinnamic acid are very influential in inhibitory activity against α-glucosidase.

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Kato, Atsushi, Izumi Nakagome, Mizuki Hata, Robert J. Nash, George W. J. Fleet, Yoshihiro Natori, Yuichi Yoshimura, Isao Adachi, and Shuichi Hirono. "Strategy for Designing Selective Lysosomal Acid α-Glucosidase Inhibitors: Binding Orientation and Influence on Selectivity." Molecules 25, no. 12 (June 19, 2020): 2843. http://dx.doi.org/10.3390/molecules25122843.

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Deoxynojirimycin (DNJ) is the archetypal iminosugar, in which the configuration of the hydroxyl groups in the piperidine ring truly mimic those of d-glucopyranose; DNJ and derivatives have beneficial effects as therapeutic agents, such as anti-diabetic and antiviral agents, and pharmacological chaperones for genetic disorders, because they have been shown to inhibit α-glucosidases from various sources. However, attempts to design a better molecule based solely on structural similarity cannot produce selectivity between α-glucosidases that are localized in multiple organs and tissues, because the differences of each sugar-recognition site are very subtle. In this study, we provide the first example of a design strategy for selective lysosomal acid α-glucosidase (GAA) inhibitors focusing on the alkyl chain storage site. Our design of α-1-C-heptyl-1,4-dideoxy-1,4-imino-l-arabinitol (LAB) produced a potent inhibitor of the GAA, with an IC50 value of 0.44 µM. It displayed a remarkable selectivity toward GAA (selectivity index value of 168.2). A molecular dynamic simulation study revealed that the ligand-binding conformation stability gradually improved with increasing length of the α-1-C-alkyl chain. It is noteworthy that α-1-C-heptyl-LAB formed clearly different interactions from DNJ and had favored hydrophobic interactions with Trp481, Phe525, and Met519 at the alkyl chain storage pocket of GAA. Moreover, a molecular docking study revealed that endoplasmic reticulum (ER) α-glucosidase II does not have enough space to accommodate these alkyl chains. Therefore, the design strategy focusing on the shape and acceptability of long alkyl chain at each α-glucosidase may lead to the creation of more selective and practically useful inhibitors.

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Salehi, Albert, Bo-Guang Fan, Mats Ekelund, Gunnar Nordin, and Ingmar Lundquist. "TPN-evoked dysfunction of islet lysosomal activity mediates impairment of glucose-stimulated insulin release." American Journal of Physiology-Endocrinology and Metabolism 281, no. 1 (July 1, 2001): E171—E179. http://dx.doi.org/10.1152/ajpendo.2001.281.1.e171.

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We examined the relation between nutrient-stimulated insulin secretion and the islet lysosome acid glucan-1,4-α-glucosidase system in rats undergoing total parenteral nutrition (TPN). During TPN treatment, serum glucose was normal, but free fatty acids, triglycerides, and cholesterol were elevated. Islets from TPN-infused rats showed increased basal insulin release, a normal insulin response to cholinergic stimulation but a greatly impaired response when stimulated by glucose or α-ketoisocaproic acid. This impairment of glucose-stimulated insulin release was only slightly ameliorated by the carnitine palmitoyltransferase 1 inhibitor etomoxir. However, in parallel with the impaired insulin response to glucose, islets from TPN-infused animals displayed reduced activities of islet lysosomal enzymes including the acid glucan-1,4-α-glucosidase, a putative key enzyme in nutrient-stimulated insulin release. By comparison, the same lysosomal enzymes were increased in liver tissue. Furthermore, in intact control islets, the pseudotetrasaccharide acarbose, a selective inhibitor of acid α-glucosidehydrolases, dose dependently suppressed islet acid glucan-1,4-α-glucosidase and acid α-glucosidase activities in parallel with an inhibitory action on glucose-stimulated insulin secretion. By contrast, when incubated with intact TPN islets, acarbose had no effect on either enzyme activity or glucose-induced insulin release. Moreover, when acarbose was added directly to TPN islet homogenates, the dose-response effect on the catalytic activity of the acid α-glucosidehydrolases was shifted to the right compared with control homogenates. We suggest that a general dysfunction of the islet lysosomal/vacuolar system and reduced catalytic activities of acid glucan-1,4-α-glucosidase and acid α-glucosidase may be important defects behind the impairment of the transduction mechanisms for nutrient-stimulated insulin release in islets from TPN-infused rats.

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Chen, Shaodan, Bing Lin, Jiangyong Gu, Tianqiao Yong, Xiong Gao, Yizhen Xie, Chun Xiao, Janis Yaxian Zhan, and Qingping Wu. "Binding Interaction of Betulinic Acid to α-Glucosidase and Its Alleviation on Postprandial Hyperglycemia." Molecules 27, no. 8 (April 13, 2022): 2517. http://dx.doi.org/10.3390/molecules27082517.

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Inhibiting the intestinal α-glucosidase can effectively control postprandial hyperglycemia for type 2 diabetes mellitus (T2DM) treatment. In the present study, we reported the binding interaction of betulinic acid (BA), a pentacyclic triterpene widely distributed in nature, on α-glucosidase and its alleviation on postprandial hyperglycemia. BA was verified to exhibit a strong inhibitory effect against α-glucosidase with an IC50 value of 16.83 ± 1.16 μM. More importantly, it showed a synergistically inhibitory effect with acarbose. The underlying inhibitory mechanism was investigated by kinetics analysis, surface plasmon resonance (SPR) detection, molecular docking, molecular dynamics (MD) simulation and binding free energy calculation. BA showed a non-competitive inhibition on α-glucosidase. SPR revealed that it had a strong and fast affinity to α-glucosidase with an equilibrium dissociation constant (KD) value of 5.529 × 10−5 M and a slow dissociation. Molecular docking and MD simulation revealed that BA bound to the active site of α-glucosidase mainly due to the van der Waals force and hydrogen bond, and then changed the micro-environment and secondary structure of α-glucosidase. Free energy decomposition indicated amino acid residues such as PHE155, PHE175, HIE277, PHE298, GLU302, TRY311 and ASP347 of α-glucosidase at the binding pocket had strong interactions with BA, while LYS153, ARG210, ARG310, ARG354 and ARG437 showed a negative contribution to binding affinity between BA and α-glucosidase. Significantly, oral administration of BA alleviated the postprandial blood glucose fluctuations in mice. This work may provide new insights into the utilization of BA as a functional food and natural medicine for the control of postprandial hyperglycemia.

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Salehi, Albert, Henrik Mosén, and Ingmar Lundquist. "Insulin release transduction mechanism through acid glucan 1,4-α-glucosidase activation is Ca2+ regulated." American Journal of Physiology-Endocrinology and Metabolism 274, no. 3 (March 1, 1998): E459—E468. http://dx.doi.org/10.1152/ajpendo.1998.274.3.e459.

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An important signal involved in glucose-stimulated insulin secretion is transduced through the action of a lysosomal acid, glucan 1,4-α-glucosidase. We investigated the Ca2+ dependency of this enzyme activity in relation to insulin release. In isolated islets, increased levels of extracellular Ca2+induced a large increase in acid glucan 1,4-α-glucosidase activity accompanied by a similar increase in insulin release at both substimulatory and stimulatory concentrations of glucose. At low glucose the Ca2+ “inflow” blocker nifedipine unexpectedly stimulated enzyme activity without affecting insulin release. However, nifedipine suppressed45Ca2+outflow from perifused islets at low glucose and at Ca2+ deficiency when intracellular Ca2+ was mobilized by carbachol. This nifedepine-induced retention of Ca2+ was reflected in increased acid glucan 1,4-α-glucosidase activity. Adding different physiological Ca2+ concentrations or nifedipine to islet homogenates did not increase enzyme activity. Neither selective glucan 1,4-α-glucosidase inhibition nor the ensuing suppression of glucose-induced insulin release was overcome by a maximal Ca2+ concentration. Hence, Ca2+-induced changes in acid glucan 1,4-α-glucosidase activity were intimately coupled to similar changes in Ca2+-glucose-induced insulin release. Ca2+ did not affect the enzyme itself but presumably activated either glucan 1,4-α-glucosidase-containing organelles or closely interconnected messengers.

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Dong, Qi, Na Hu, Huilan Yue, and Honglun Wang. "Inhibitory Activity and Mechanism Investigation of Hypericin as a Novel α-Glucosidase Inhibitor." Molecules 26, no. 15 (July 28, 2021): 4566. http://dx.doi.org/10.3390/molecules26154566.

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α-glucosidase is a major enzyme that is involved in starch digestion and type 2 diabetes mellitus. In this study, the inhibition of hypericin by α-glucosidase and its mechanism were firstly investigated using enzyme kinetics analysis, real-time interaction analysis between hypericin and α-glucosidase by surface plasmon resonance (SPR), and molecular docking simulation. The results showed that hypericin was a high potential reversible and competitive α-glucosidase inhibitor, with a maximum half inhibitory concentration (IC50) of 4.66 ± 0.27 mg/L. The binding affinities of hypericin with α-glucosidase were assessed using an SPR detection system, which indicated that these were strong and fast, with balances dissociation constant (KD) values of 6.56 × 10−5 M and exhibited a slow dissociation reaction. Analysis by molecular docking further revealed that hydrophobic forces are generated by interactions between hypericin and amino acid residues Arg-315 and Tyr-316. In addition, hydrogen bonding occurred between hypericin and α-glucosidase amino acid residues Lys-156, Ser-157, Gly-160, Ser-240, His-280, Asp-242, and Asp-307. The structure and micro-environment of α-glucosidase enzymes were altered, which led to a decrease in α-glucosidase activity. This research identified that hypericin, an anthracene ketone compound, could be a novel α-glucosidase inhibitor and further applied to the development of potential anti-diabetic drugs.

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Xue, Na, Yutao Jia, Congwei Li, Binnan He, Caiqin Yang, and Jing Wang. "Characterizations and Assays of α-Glucosidase Inhibition Activity on Gallic Acid Cocrystals: Can the Cocrystals be Defined as a New Chemical Entity During Binding with the α-Glucosidase?" Molecules 25, no. 5 (March 5, 2020): 1163. http://dx.doi.org/10.3390/molecules25051163.

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Cocrystallization with co-former (CCF) has proved to be a powerful approach to improve the solubility and even bioavailability of poorly water-soluble active pharmaceutical ingredients (APIs). However, it is still uncertain whether a cocrystal would exert the pharmacological activity in the form of a new chemical entity, an API-CCF supramolecule. In the present study, gallic acid (GA)-glutaric acid and GA-succinimide cocrystals were screened. The solubility, dissolution rate and oral bioavailability of the two cocrystals were evaluated. As expected, AUCs of GA-glutaric acid and GA-succinimide cocrystals were 1.86-fold and 2.60-fold higher than that of single GA, respectively. Moreover, experimental evaluations on α-glucosidase inhibition activity in vitro and theoretical simulations were used to detect whether the two cocrystals would be recognized as a new chemical entity during binding with α-glucosidase, a target protein in hypoglycemic mechanisms. The enzyme activity evaluation results showed that both GA and glutaric acid displayed α-glucosidase inhibition activity, and GA-glutaric acid cocrystals showed strengthened α-glucosidase inhibition activity at a moderate concentration, which is attributed to synergism of the two components. Molecular docking displayed that the GA-glutaric acid complex deeply entered the active cavity of the α-glucosidase in the form of a supramolecule, which made the guest-enzyme binding configuration more stable. For the GA and succinimide system, succinimide showed no enzyme inhibition activity, however, the GA-succinimide complex presented slightly higher α-glucosidase inhibition activity than that of GA. Molecular docking simulation indicated that the guest molecules entering the active cavity of the α-glucosidase were free GA and succinimide, not the GA-succinimide supramolecule.

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Pérez-Nájera, Viridiana Candelaria, Janet Alejandra Gutiérrez-Uribe, Marilena Antunes-Ricardo, Sergio Hidalgo-Figueroa, Carmen Lizette Del-Toro-Sánchez, Luis A. Salazar-Olivo, and Eugenia Lugo-Cervantes. "Smilax aristolochiifolia Root Extract and Its Compounds Chlorogenic Acid and Astilbin Inhibit the Activity of α-Amylase and α-Glucosidase Enzymes." Evidence-Based Complementary and Alternative Medicine 2018 (June 25, 2018): 1–12. http://dx.doi.org/10.1155/2018/6247306.

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Regulating activities of α-amylase and α-glucosidase through the use of specific inhibitors is a main strategy for controlling type 2 diabetes. Smilax aristolochiifolia root decoctions are traditionally used in Mexico as hypoglycemic and for weight loss, but the active principles and mechanisms underlying such putative metabolic effects are yet unknown. Here, we isolated the major bioactive compounds from a hydroethanolic extract of S. aristolochiifolia root by fast centrifugal partition chromatography and evaluated their effects against pancreatic α-amylase and yeast α-glucosidase. A chlorogenic acid-rich fraction (CAF) inhibited α-amylase activity with an IC50 value of 59.28 μg/mL in an uncompetitive manner and α-glucosidase activity with an IC50 value of 9.27 μg/mL in a noncompetitive mode. Also, an astilbin-rich fraction (ABF) inhibited α-glucosidase activity with an IC50 value of 12.30 μg/mL, in a noncompetitive manner. CAF inhibition α-amylase was as active as acarbose while both CAF and ABF were 50-fold more potent inhibitors of α-glucosidase than acarbose. The molecular docking results of chlorogenic acid and astilbin with α-amylase and α-glucosidase enzymes correlated with the inhibition mechanisms suggested by enzymatic assays. Our results prove that S. aristolochiifolia roots contain chlorogenic acid and astilbin, which inhibit carbohydrates-hydrolyzing enzymes, suggesting a new mechanism for the hypoglycemic effect reported for this plant.

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Li, Yunbo, Xiaoling Liu, Haoyu Zhou, Bo Li, and Igor Kostiantinovich Mazurenko. "Inhibitory Mechanism of Engeletin Against α-Glucosidase." Natural Product Communications 16, no. 1 (January 2021): 1934578X2098672. http://dx.doi.org/10.1177/1934578x20986723.

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The inhibitory mechanism of engeletin against α-glucosidase was investigated for the first time by fluorescence spectroscopy and molecular docking. The results showed that engeletin could inhibit α-glucosidase in a noncompetitive inhibition mode with a half-maximal inhibitory concentration value of 48.5 ± 6.0 µg/mL (0.11 ± 0.014 mmol/L). It was found that engeletin could cause static fluorescence quenching of α-glucosidase by forming a complex with α-glucosidase. The thermodynamic parameters indicated that the combination of engeletin and α-glucosidase was driven by hydrophobic force. The molecular docking results confirmed that some amino acid residues of α-glucosidase (Trp391, Arg428, Glu429, Gly566, Trp710, Glu771) could interact with engeletin by hydrogen bonding.

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Nemzer, Boris, Diganta Kalita, and Nebiyu Abshiru. "Quantification of Major Bioactive Constituents, Antioxidant Activity, and Enzyme Inhibitory Effects of Whole Coffee Cherries (Coffea arabica) and Their Extracts." Molecules 26, no. 14 (July 16, 2021): 4306. http://dx.doi.org/10.3390/molecules26144306.

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Coffee cherry is a rich source of chlorogenic acids (CGAs) and caffeine. In this study we examined the potential antioxidant activity and enzyme inhibitory effects of whole coffee cherries (WCC) and their two extracts on α-amylase, α-glucosidase and acetylcholinesterase (AChE) activities, which are targets for the control of diabetes and Alzheimer’s diseases. Whole coffee cherry extract 40% (WCCE1) is rich in chlorogenic acid compounds, consisting of a minimum of 40% major isomers, namely 3-caffeoylquinic acids, 4-caffeoylquinic acids, 5-caffeoylquinic acids, 3,4-dicaffeoylquinic acid, 3,5-dicaffeoylquinic acid, 4,5-dicaffeoylquinic acid, 4-feruloylquinc acid, and 5-feruloylquinc acid. Whole coffee cherry extract 70% (WCCE2) is rich in caffeine, with a minimum of 70%. WCCE1 inhibited the activities of digestive enzymes α-amylase and α-glucosidase, and WCCE2 inhibited acetylcholinesterase activities with their IC50 values of 1.74, 2.42, and 0.09 mg/mL, respectively. Multiple antioxidant assays—including DPPH, ABTS, FRAP, ORAC, HORAC, NORAC, and SORAC—demonstrated that WCCE1 has strong antioxidant activity.

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Ramadhan, Rico, and Preecha Phuwapraisirisan. "Arylalkanones from Horsfieldia macrobotrys are Effective Antidiabetic Agents Achieved by α-Glucosidase Inhibition and Radical Scavenging." Natural Product Communications 10, no. 2 (February 2015): 1934578X1501000. http://dx.doi.org/10.1177/1934578x1501000230.

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Horsfielda macrobotrys Merr has long been used by Dayak people in East Kalimantan of Indonesia, for diabetes therapy. Inspired by ethnopharmacological use and promising α-glucosidase and radical scavenging activities, an attempt to identify the active components was carried out. Bioassay-guided isolation yielded two related arylalkanones named 1-(2,4,6-trihydroxyphenyl)-9-phenylnonan-1-one (1) and malabaricone A (2). Arylalkanone 1 showed potent radical scavenging comparable with that of the standard antioxidant, ascorbic acid, and promising inhibition against α-glucosidases. Noticeably, arylalkanone 1 was 3-30 times more potent than malabaricone A (2) in all bioassays examined, thus suggesting the critical role in exerting bioactivities of the hydroxy group on the aryl moiety. This hypothesis was also supported by reduction in inhibitory effects of the methyl ether analogues 1a and 2a. Arylalkanone 1 inhibited yeast α-glucosidase in a mixed-type manner in which the noncompetitive pathway was dominant over competitive inhibition. This study is the first report of α-glucosidase inhibition of arylalkenone-type compounds and the first phytochemicals from H. macrobotrys.

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Coma, P., L. Gomez-Chacon, B. Garcia-Serrano, E. Fernandez, and M. A. Ortiz-Apodaca. "α-Glucosidase and Ν-Acetyl-α-D-glucosaminidase Isoenzymes in Serum." Clinical Chemistry 38, no. 2 (February 1, 1992): 223–26. http://dx.doi.org/10.1093/clinchem/38.2.223.

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Abstract Using different conditions for incubation and fluorometry with 4-methylumbelliferylglycosides as substrates, we demonstrated the presence of acid alpha-glucosidase, "renal" alpha-glucosidase, N-acetyl-beta-D-glucosaminidase A, and N-acetyl-beta-D-glucosaminidase B in freshly drawn normal human serum. The acid alpha-glucosidase enzymatic activity was determined at pH 4.0 in 0.1 mol/L Tris reagent, whereas the renal isoenzyme activity was determined at pH 5.6 in presence of 0.05 mol/L turanose reagent. N-Acetyl-beta-D-glucosaminidases A and B were determined by their different behaviors on heating. The corresponding reference intervals for each enzyme were calculated from results for 40 controls: acid alpha-glucosidase (0.024 +/- 0.010 U/L), renal alpha-glucosidase (0.035 +/- 0.012 U/L), N-acetyl-beta-D-glucosaminidase A (10.2 +/- 2.9 U/L), and N-acetyl-beta-D-glucosaminidase B (4.4 +/- 2.1 U/L).

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Pujirahayu, Niken, Debu Kumar Bhattacharjya, Toshisada Suzuki, and Takeshi Katayama. "α-Glucosidase Inhibitory Activity of Cycloartane-Type Triterpenes Isolated from Indonesian Stingless Bee Propolis and Their Structure–Activity Relationship." Pharmaceuticals 12, no. 3 (July 1, 2019): 102. http://dx.doi.org/10.3390/ph12030102.

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This study reports on the antioxidant activity and α-glucosidase inhibitory activity of five cycloartane-type triterpenes isolated from Indonesian stingless bee (Tetragonula sapiens Cockerell) propolis and their structure–activity relationships. The structure of the triterpenes was determined to include mangiferolic acid (1), Cycloartenol (2), ambonic acid (3), mangiferonic acid (4), and ambolic acid (5). The inhibitory test results of all isolated triterpenes against α-glucosidase showed a high potential for inhibitory activity with an IC50 range between 2.46 and 10.72 µM. Among the compounds tested, mangiferonic acid (4) was the strongest α-glucosidase inhibitor with IC50 2.46 µM compared to the standard (–)-epicatechin (1991.1 µM), and also had antioxidant activities with IC50 values of 37.74 ± 6.55 µM. The study on the structure–activity relationships among the compounds showed that the ketone group at C-3 and the double bonds at C-24 and C-25 are needed to increase the α-glucosidase inhibitory activity. The carboxylic group at C-26 is also more important for increasing the inhibitory activity compared with the methyl group. This study provides an approach to help consider the structural requirements of cycloartane-type triterpenes from propolis as α-glucosidase inhibitors. An understanding of these requirements is deemed necessary to find a new type of α-glucosidase inhibitor from the cycloartane-type triterpenes or to improve those inhibitors that are known to help in the treatment of diabetes.

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Smita, Kumari. "EVALUATION OF α-GLUCOSIDASE INHIBITORY POTENTIAL OF METHANOLIC LEAF EXTRACT OF OCIMUM CANUM." International Journal of Pharmacy and Pharmaceutical Sciences 10, no. 1 (January 1, 2018): 126. http://dx.doi.org/10.22159/ijpps.2018v10i1.22268.

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Objective: The present investigation was designed to study the inhibitory effects of methanolic leaf extract of Ocimum canum (O. canum) on α-glucosidase using in vitro model followed by an assessment of bioactive compounds.Methods: The methanolic leaf extract was prepared by Soxhlet extraction method and partially purified by thin layer chromatography (TLC). Each band was subjected to α-glucosidase inhibition study. The positive bands were further characterized by high-performance liquid chromatography (HPLC) and quadrupole time of flight (Q-TOF) micro mass spectrometer.Results: Out of the several combinations of solvent systems, toluene, ethyl acetate and formic acid combination in the ratio of 7:2:1 revealed 5 bands on the TLC sheet. Among all the TLC bands, 2 bands (band A and B) showed the significant inhibitory effect on α-glucosidase activity. HPLC analysis of band A and B revealed the presence of two important polyphenolic compounds, namely rosmarinic acid (RA) and ursolic acid (UA). Q-TOF micromass spectrometer analysis revealed the percentage availability of RA, caffeic acid, tartaric acid, quercetin and other polyphenolic components in the bioactive bands.Conclusion: The study revealed that methanolic leaf extract of O. canum exhibits potent inhibition of α-glucosidase activity. Inhibition of α-glucosidase activity might be attributed to the presence of the polyphenolic compounds like RA and UA. Therefore, this finding can lead to the development of natural α-glucosidase inhibitors by the O. canum leaf extract.

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Vu, Phuong Thi Bach, Dai Minh Cao, and Phuong Ngo Diem Quach. "Effects of some precursors and elicitors on the growth and α-glucosidase inhibitory activity of in vitro Urena lobata L. hairy roots." Science and Technology Development Journal - Natural Sciences 4, no. 3 (September 11, 2020): First. http://dx.doi.org/10.32508/stdjns.v4i3.902.

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Recent studies have demonstrated the potential of in vitro Urena lobata L. hairy roots to inhibit α-glucosidase for supporting the treatment of type 2 diabetes. To increase the productivities of hairy roots with α-glucosidase inhibitory activity in in vitro culture conditions, this study focus on the effects of some metabolic factors such as precursors (L-phenylalanine, L-tyrosine) and elicitors (chitosan, methyl jasmonate, salicylic acid). They were added to the culture media to investigate the growth and α-glucosidase inhibitory activity of Urena lobata L. hairy roots. The results showed that for the effects of precursors, only phenylalanine (1 µM) increased root biomass with the highest of α-glucosidase inhibitory activity on the 25th day of culture. In contrast, tyrosine did not play any role in increasing the biomass and α-glucosidase inhibitory activity in Urena lobata L. hairy roots. For the effects of elicitors, only chitosan (50 mg/L) resulted in hairy roots with α-glucosidase inhibitory activity higher than the control after 3 days in culture medium. Other elicitors such as methyl jasmonate, salicylic acid had lower α-glucosidase inhibitory activity than the control. The results of this study demonstrated the potential of phenylalanine and chitosan in increasing the productivity of in vitro hairy roots with higher α-glucosidase inhibitory activity in Urena lobata L.

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Swain, Ayusman, and Hariprasad Puttaswamy. "α-Glucosidase Inhibition Kinetics and Molecular Docking Studies with the Bioactive Constituents from Canna indica L. Rhizome Extract." Asian Journal of Chemistry 32, no. 8 (2020): 1986–90. http://dx.doi.org/10.14233/ajchem.2020.22727.

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The present study investigated the phytochemical constituents from Canna indica rhizome acetone extract, which was earlier reported to possess α-glucosidase inhibiting potential. Different fractions were collected from column chromatography of the acetone extract and the in vitro enzyme inhibition and the kinetic study was performed with the active fraction. The active fraction exhibited competitive inhibition of α-glucosidase. HRLC-MS/MS technique was used to identify the lead compounds from the active fraction. The major compounds were psoromic acid, usnic acid and rosmarinic acid. Molecular docking study of the compounds with the crystal structure of α-glucosidase was performed using ParDOCK. Psoromic acid and usnic acid exhibited strong binding affinity with the active site nucleophiles Asp349 and Asp212, respectively. Usnic acid also stabilized the catalytic residue Glu274. Rosmarinic acid formed multiple hydrogen bonds with the catalytic residue Glu274 and also bonded to non-catalytic residues Gln276, Arg312 and Glu408. The study illustrated informative data on the phytochemical constituents from Canna indica rhizome as α-glucosidase inhibitor and as potential candidates for the development of antidiabetic drugs.

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Thakral, Samridhi, and Vikramjeet Singh. "2,4-Dichloro-5-[(N-aryl/alkyl)sulfamoyl]benzoic Acid Derivatives: In Vitro Antidiabetic Activity, Molecular Modeling and In silico ADMET Screening." Medicinal Chemistry 15, no. 2 (February 12, 2019): 186–95. http://dx.doi.org/10.2174/1573406414666180924164327.

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Background: Postprandial hyperglycemia can be reduced by inhibiting major carbohydrate hydrolyzing enzymes, such as α-glucosidase and α-amylase which is an effective approach in both preventing and treating diabetes. Objective: The aim of this study was to synthesize a series of 2,4-dichloro-5-[(N-aryl/alkyl)sulfamoyl] benzoic acid derivatives and evaluate α-glucosidase and α-amylase inhibitory activity along with molecular docking and in silico ADMET property analysis. Method: Chlorosulfonation of 2,4-dichloro benzoic acid followed by reaction with corresponding anilines/amines yielded 2,4-dichloro-5-[(N-aryl/alkyl)sulfamoyl]benzoic acid derivatives. For evaluating their antidiabetic potential α-glucosidase and α-amylase inhibitory assays were carried out. In silico molecular docking studies of these compounds were performed with respect to these enzymes and a computational study was also carried out to predict the drug-likeness and ADMET properties of the title compounds. Results: Compound 3c (2,4-dichloro-5-[(2-nitrophenyl)sulfamoyl]benzoic acid) was found to be highly active having 3 fold inhibitory potential against α-amylase and 5 times inhibitory activity against α-glucosidase in comparison to standard drug acarbose. Conclusion: Most of the synthesized compounds were highly potent or equipotent to standard drug acarbose for inhibitory potential against α-glucosidase and α-amylase enzyme and hence this may indicate their antidiabetic activity. The docking study revealed that these compounds interact with active site of enzyme through hydrogen bonding and different pi interactions.

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22

Mia, Md Abdur Rashid, Qamar Uddin Ahmed, Sahena Ferdosh, Abul Bashar Mohammed Helaluddin, Md Shihabul Awal, Murni Nazira Sarian, Md Zaidul Islam Sarker, and Zainul Amiruddin Zakaria. "In Vitro, In Silico and Network Pharmacology Mechanistic Approach to Investigate the α-Glucosidase Inhibitors Identified by Q-ToF-LCMS from Phaleria macrocarpa Fruit Subcritical CO2 Extract." Metabolites 12, no. 12 (December 15, 2022): 1267. http://dx.doi.org/10.3390/metabo12121267.

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The fruit of Phaleria macrocarpa have been traditionally used as an antidiabetic remedy in Malaysia and neighbouring countries. Despite its potential for diabetes treatment, no scientific study has ever been conducted to predict the inhibitor interaction of the protein α-glucosidase identified in an extract prepared with a non-conventional extraction technique. Hence, the major aim of this research was to evaluate the in vitro antioxidant, the α-glucosidase inhibitors, and the molecular dynamic simulations of the α-glucosidase inhibitors identified by Quadrupole Time-of-Flight Liquid Chromatography Mass Spectrometry (Q-ToF-LCMS) analysis. Initially, dry fruit were processed using non-conventional and conventional extraction methods to obtain subcritical carbon dioxide extracts (SCE-1 and SCE-2) and heating under reflux extract (HRE), respectively. Subsequently, all extracts were evaluated for their in vitro antioxidative and α-glucosidase inhibitory potentials. Subsequently, the most bioactive extract (SCE-2) was subjected to Q-ToF-LCMS analysis to confirm the presence of α-glucosidase inhibitors, which were then analysed through molecular dynamic simulations and network pharmacology approaches to confirm their possible mechanism of action. The highest inhibitory effects of the 2,2-diphenyl-1-picrylhydrazyl (DPPH) radical and α-glucosidase on SCE-2 was found as 75.36 ± 0.82% and 81.79 ± 0.82%, respectively, compared to the SCE-1 and HRE samples. The Q-ToF-LCMS analysis tentatively identified 14 potent α-glucosidase inhibitors. Finally, five identified compounds, viz., lupenone, swertianolin, m-coumaric acid, pantothenic acid, and 8-C-glucopyranosyleriodictylol displayed significant stability, compactness, stronger protein-ligand interaction up to 100 ns further confirming their potential as α-glucosidase inhibitors. Consequently, it was concluded that the SCE-2 possesses a strong α-glucosidase inhibitory effect due to the presence of these compounds. The findings of this study might prove useful to develop these compounds as alternative safe α-glucosidase inhibitors to manage diabetes more effectively.

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Cherigo, Lilia, and Sergio Martínez-Luis. "α-Glucosidase Inhibitor Isolated from Blechum pyramidatum." Natural Product Communications 13, no. 4 (April 2018): 1934578X1801300. http://dx.doi.org/10.1177/1934578x1801300421.

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Blechum pyramidatum (Lam.) Urb. is a species of extensive medicinal use in the American continent. In fact, antidiabetic and anticancer preparations from this plant have been patented in Mexico, even though their active constituents are not yet known. It was recently discovered that B. pyramidatum inhibits the action of the α-glucosidase enzyme, thereby corroborating the antidiabetic properties attributed to this plant. The primary purpose of this study was to identify and characterize the α-glucosidase inhibitors from this species. Bioassay-guided fractionation of a crude extract of B. pyramidatum led to the isolation of a main α-glucosidase inhibitor, Palmitic acid (IC50 237.5). This compound was identified by both spectroscopic and spectrometric analysis. Its inhibitory activity was similar to that of the antidiabetic drug acarbose (IC50 241.6 μM), which was used as a positive control in our bioassay. Kinetic analysis established that palmitic acid acted as a competitive inhibitor. Docking analysis predicted that this compound binds to the same site as acarbose does in the human intestinal α-glucosidase (PDB: 3TOP). The presence of palmitic acid in B. pyramidatum and its potent inhibitory activity against α-glucosidase enzyme provides solid evidence to support the antidiabetic use of this plant in traditional medicine.

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24

Wu, Cheng-Rong, Shih-Yu Lee, Chien-Hung Chen, and Sheng-Dun Lin. "Bioactive Compounds of Underground Valerian Extracts and Their Effect on Inhibiting Metabolic Syndrome-Related Enzymes Activities." Foods 12, no. 3 (February 2, 2023): 636. http://dx.doi.org/10.3390/foods12030636.

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Extractions of the underground parts of valerian were prepared with water and ethanol (25–95%) at 25–75 °C. Extraction yields, bioactive compounds, and the 1,1-Diphenyl-2-picrylhydrazyl (DPPH) radical scavenging ability of lyophilized extracts were determined. The inhibitory effects of the extracts, valerenic acid derivatives and phenolic acids, on metabolic syndrome (MS)-related enzymes activities were further examined. Both roots and rhizomes extracted with 95% ethanol at 75 °C had the highest levels of bioactive compounds. The antioxidant capacity and inhibition of MS-related enzymes of the roots extract were better than those of the rhizomes. The roots extract more strongly inhibited pancreatic lipase (inhibition of 50% of enzyme activity (IC50), 17.59 mg/mL), angiotensin-converting enzyme (ACE, IC50, 3.75 mg/mL), α-amylase (IC50, 12.53 mg/mL), and α-glucosidase (IC50, 15.40 mg/mL). These four phenolic acids inhibited the activity of MS-related enzymes. Valerenic acid demonstrated more of an inhibitory ability for ACE (IC50, 0.225 mg/mL, except for caffeic acid) and α-glucosidase (IC50, 0.617 mg/mL) than phenolic acids. Valerian extract inhibited key enzyme activities that were associated with obesity (lipase), hypertension (ACE), and type 2 diabetes (α-amylase and α-glucosidase), suggesting that it is a potential candidate for the development of functional supplements.

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25

Limanto, Agus, Adelina Simamora, Adit Widodo Santoso, and Kris Herawan Timotius. "Antioxidant, α-Glucosidase Inhibitory Activity and Molecular Docking Study of Gallic Acid, Quercetin and Rutin: A Comparative Study." Molecular and Cellular Biomedical Sciences 3, no. 2 (September 1, 2019): 67. http://dx.doi.org/10.21705/mcbs.v3i2.60.

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Background: Plant-phenolics and flavonoids, including gallic acid, quercetin and rutin, are considered as safe inhibitors for α-glucosidase. This study aimed to compare antioxidant and α-glucosidase inhibitory activities of gallic acid (GA), quercetin (QUE) and rutin (RUT).Materials and Methods: Pure compounds of GA, QUE, and RUT were used. Their antioxidant and inhibitory activity on α-glucosidase were investigated spectroscopically, including their kinetic analysis and interaction mechanism by docking simulation.Results: All the tested compounds (GA, QUE, and RUT) showed good antioxidant activity better than the standards ascorbic acid (AA) and butylated hydroxytoluene (BHT), with QUE showing the highest antioxidant activity based on 2,2-diphenyl1-picrylhydrazyl (DPPH) radical scavenging activity. Based on their reducing properties, the activities of the compounds follow the following order: AA > GA > BHT > QUE > RUT. Both GA and RUT induced a competitive type of inhibition, with activities stronger than acarbose (IC50 = 823 μg/mL), whereas QUE inhibited in a mixed type manner. The IC50 of GA, QUE, and RUT were 220.12, 65.52, and 224.55 μg/mL respectively. The results obtained from molecular docking indicate that all compounds have affinity in the active site pocket of α-glucosidase, with the hydrogen bond being the major force involved in each compound binding to the enzyme.Conclusion: In conclusion, QUE has better antioxidant and α-glucosidase inhibitory activity than GA and RUT. This work provides insights into the interactions between GA, QUE, and RUT and α-glucosidase.Keywords: docking, gallic acid, α-glucosidase, rutin, quercetin

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Liu, Jiang, Xiansheng Wang, Sheng Geng, Benguo Liu, and Guizhao Liang. "Inhibitory Mechanism of Taxifolin against α-Glucosidase Based on Spectrofluorimetry and Molecular Docking." Natural Product Communications 12, no. 11 (November 2017): 1934578X1701201. http://dx.doi.org/10.1177/1934578x1701201116.

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The α-glucosidase inhibitory activity and behavior of taxifolin was first investigated by spectrofluorimetry and molecular docking. It was found that taxifolin inhibits α-glucosidase in a competitive manner with the IC50 value of 0.16 mg/mL. The intrinsic fluorescence quenching of α-glucosidase in the presence of taxifolin was observed by the static quenching mechanism. According to the thermodynamic study, the complex of taxifolin and α-glucosidase was maintained by van der Waals and hydrogen bonding. The binding mode provided by molecular docking simulation indicated the existence of hydrogen bonding between taxifolin and the amino acid residues of α-glucosidase (Glu429, Asp 568 and Glu771), which coincided with the result of fluorescence analysis.

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27

Gaspersz, Nelson, Matthew Adi Honey Amos, Sitti Hardiyanti Kalauw, Indrid Harjuni, and Mario R. Sohilait. "Penambatan Molekuler Penghambatan Aktivitas Enzim α-Amilase dan α-Glukosidase oleh Senyawa Aktif Daun Kirinyuh (Chromolaena odorata L.)." KOVALEN: Jurnal Riset Kimia 8, no. 3 (December 29, 2022): 230–37. http://dx.doi.org/10.22487/kovalen.2022.v8.i3.16046.

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An in silico study was conducted to inhibit the active compound in Kirinyuh leaves (Chromolaena odorata L.) against α-amylase and α-glucosidase enzymes using a molecular docking approach. The docking was carried out on 19 active compounds that had been identified in Kirinyuh leaves and were optimized using the PM3 method. The best results in inhibit on of the α-amylase enzyme were shown by compounds from the flavanone group, namely genkwanin and sakuranetin with binding affinities of -8.3 kcal/mol and -8.1 kcal/mol, respectively, while the best results in inhibiting on of the α-glucosidase enzyme were shown by two compounds from the hydroxybenzoic acid group, namely p-coumaric acid and p-hydroxybenzoic acid with bond affinities of -5.7 kcal.mol and -5.5 kcal.mol, respectively. The interaction between α-amylase with genkwanin and sakuranetin produces one conventional hydrogen bond GLU 233 and GLN 63 respectively. The interaction between α-glucosidase with p-coumaric acid and p-hydroxybenzoic acid produces three conventional hydrogen bonds, HIS 112; GLN 182; ASP 352 and GU 277; GLN 279; ASP 352.

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28

Janatiningrum, Isra, Yulin Lestari, Dedy Duryadi Solihin, and Anja Meryandini. "Characterization of α-Glucosidase Inhibitor Streptomyces sp. IPBCC.a.29.1556 Aqueous Extract: An Endophyte of Indonesian Ficus deltoidea." Indonesian Journal of Chemistry 22, no. 6 (October 25, 2022): 1501. http://dx.doi.org/10.22146/ijc.72433.

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Filamentous bacteria have been known as actinobacteria which could produce various secondary metabolites, including an α-glucosidase inhibitor. The α-glucosidase inhibitor has been identified to be potentially valuable for the treatment of diabetes mellitus. Endophytic actinobacteria are able to produce bioactive compounds that are similar to their hosts. Indonesian Ficus deltoidea is one of the medicinal plants which has the activity of the α-glucosidase inhibitor. The α-glucosidase inhibitor has been characterized by optimizing compound production, fractionation, analysis using TLC and LC-MS, and identifying inhibitor mechanisms. The α-glucosidase inhibitor substance is present in Streptomyces sp. IPBCC.a.29.1556 aqueous extract. The aqueous extract was separated and fraction 1 had an IC50 value of 58.8 μg/mL, which is better than acarbose (IC50 = 90.4 μg/mL). Kinetic studies revealed that this fraction inhibited the enzyme through a non-competitive mechanism. Chemical profile based on LC-MS, fraction 1 showed the presence of Phenylpropynal, Butyric acid, 2-(2-Ethoxyethoxy)ethanolate, 1,1-Diethoxyethane acetate, N,N-dimethyl-3-oxide-1H-Benzotriazole-1-propanamine, p-coumaric acid, and isoquinolinium which might contribute individually or synergistically to the observed α-glucosidase inhibitor activity. These results suggest that fraction 1 from the aqueous extract of Streptomyces sp. IPBCC.a.29.1556 is the potential source to produce an α-glucosidase inhibitor for the management of postprandial hyperglycemia.

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29

Ibrahim, Mohammed Auwal, James Dama Habila, Neil Anthony Koorbanally, and Md Shahidul Islam. "α-Glucosidase and α-Amylase Inhibitory Compounds from three African Medicinal Plants: An Enzyme Inhibition Kinetics Approach." Natural Product Communications 12, no. 7 (July 2017): 1934578X1701200. http://dx.doi.org/10.1177/1934578x1701200731.

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The quest to find new lead compounds with anti-diabetic effects via the inhibition of α-glucosidase and α-amylase had led us to conduct bioassay guided isolation of three African medicinal plants which resulted in the identification of bicyclo[2.2.0]hexane-2,3,5-triol (1), 3β- O-acetyl betulinic acid (2) and 2,7-dihydroxy-4 H-1-benzopyran-4-one (3), as the bioactive compounds. The compounds demonstrated a significant (P < 0.05) inhibitory effect on α-glucosidase and α-amylase activities than acarbose. Steady state kinetic analysis revealed that compounds 1 and 2 inhibited both α-amylase and α-glucosidase in non-competitive patterns whilst compound 3 was an uncompetitive inhibitor of α-glucosidase and a non-competitive inhibitor of α-amylase. In conclusion, the study has identified three new active α-glucosidase and α-amylase inhibitory compounds that could have the potential to retard postprandial hyperglycemia.

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30

Liu, Bin, Ji-Mei Ma, Hang-Wei Chen, Zi-Long Li, Lin-Hao Sun, Zhen Zeng, and Hong Jiang. "α-Glucosidase inhibitory activities of phenolic acid amides with l-amino acid moiety." RSC Advances 6, no. 56 (2016): 50837–45. http://dx.doi.org/10.1039/c6ra08330g.

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31

Muhammad Alfarabi, Maria Bintang, Suryani, Mega Safithri, and Waras Nurcholis. "Kinetics of α -glucosidase inhibitory activity and phytochemical analysis of Piper crocatum Ruiz & Pav. leaves ethanol extract." International Journal of Research in Pharmaceutical Sciences 11, SPL4 (December 21, 2020): 2032–36. http://dx.doi.org/10.26452/ijrps.v11ispl4.4416.

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α-Glucosidase is an enzymes group that playing essential roles in the digestion of polysaccharide. Inhibitor of a-glucosidase can decrease polysaccharide digestion rate and therefore plays a significant function in preventing the development of diabetes (type 2). Piper crocatum Ruiz & Pav. is an essential herb applied traditionally in Indonesia to treat diabetes mellitus. This work evaluated the a-glucosidase inhibitory activity of P. crocatum leaves ethanol extract. Phytochemical component of the extract was also analyzed. The α-glucosidase inhibitory activity of the P. crocatum leaves ethanol extract was examined by reacting its different concentrations with α-glucosidase and p-nitrophenyl glucopyranoside. Kinetics of the α-glucosidase inhibition was determined using a Lineweaver-Burke plot. Phytochemical in the extract was determined using GC-MS. Ethanol extract of P. crocatum leaves exhibited moderate α-glucosidase inhibitory activity compared with acarbose. Phytochemical analyses showed the presence of stilbene, linolenic acid, phenol, phytosteroid, and α-tocopherol. The competitive action of P. crocatum leaves ethanol extract is due to its inhibitory effects on α-glucosidase. The stilbene and phenol compounds indicated responsible for anti-diabetic activity from P. crocatum leaves ethanol extract.

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Cao, Weiguo, and Don L. Crawford. "Carbon nutrition and hydrolytic and cellulolytic activities in the ectomycorrhizal fungus Pisolithus tinctorius." Canadian Journal of Microbiology 39, no. 5 (May 1, 1993): 529–35. http://dx.doi.org/10.1139/m93-075.

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Four strains of an ectomycorrhizal fungus, Pisolithus tinctorius, were investigated for carbon nutrition, and for production of hydrolytic and cellulolytic enzymes. Glucose, mannose, and cellobiose supported rapid mycelial growth of all four strains. Fructose was utilized by two strains, SMF and S359. Of the 10 hydrolytic enzymes examined, acid phosphatase, acid α-galactosidase, acid esterase, and acid β-glucosidase were found in all four strains. β-Galactosidase was only observed in strain S359. α-Mannosidase, β-mannosidase, α-glucosidase, β-xylosidase, and proteinase were not detected in any of the four strains. Isozyme patterns of β-glucosidase and esterase in the four strains were compared by activity staining after native gradient gel electrophoresis. The isozyme pattern of β-glucosidase showed three major forms in all four strains. In addition, two more isoforms were found in strain S370. All strains shared two esterase bands, while strain S370 had three more isoforms. Study on strain SMF indicated that acid β-glucosidase was expressed constitutively, with increased activity in cellobiose-containing media. Under nitrogen-limiting conditions, a low level of endoglucanase and exoglucanase activity was observed in strains SMF and S359. Further study on S359 showed that high concentrations of nitrogen repressed the cellulolytic activity. When cellobiose served as carbon source, higher cellulolytic activity was observed. Cellulose did not induce higher activity.Key words: Pisolithus, ectomycorrhizal, β-glucosidase, hydrolytic enzymes, cellulolytic enzymes.

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33

Van Hove, Johan, Helen Yang, Letealia Oliver, Mark Pennybacker, and Yuan-Tsong Chen. "Purification of recombinant human precursor acid α-glucosidase." IUBMB Life 43, no. 3 (October 1997): 613–23. http://dx.doi.org/10.1080/15216549700204421.

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Radin, N. S., A. Shukla, G. S. Shukla, and A. Sano. "Heat-stable protein that stimulates acid α-glucosidase." Biochemical Journal 264, no. 3 (December 15, 1989): 845–49. http://dx.doi.org/10.1042/bj2640845.

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A hot-water extract of bovine spleen and guinea pig liver exhibited the ability to enhance acid alpha-glucosidase activity, with methylumbelliferyl alpha-glucoside, glycogen or maltose as substrate. The level of activator required for maximal stabilization was similar for all three substrates, indicating direct action on the enzyme rather than on substrate. The stimulator was partially purified by chromatography with gel-permeation (apparent Mr 20,000-24,000), ion-exchange and C4 reverse-phase columns. It was retained by a narrow-pore dialysis tubing and destroyed by treatment with Pronase, and is presumably a protein. The stimulating protein protected the enzyme against denaturation by heat or incubation with a buffer of high ionic strength in the absence of substrate. RNA inhibited the enzyme, and the activator protein was able to counteract the effect. Activating material was found in a variety of mouse and rat tissues, as well as human urine.

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GAO, Hong, Yi-Na HUANG, Bo GAO, and Jun KAWABATA. "Chebulagic Acid Is a Potent α-Glucosidase Inhibitor." Bioscience, Biotechnology, and Biochemistry 72, no. 2 (February 23, 2008): 601–3. http://dx.doi.org/10.1271/bbb.70591.

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Nishimoto, Junji, Koji Inui, Shintaro Okada, Wataru Ishigami, Setsuo Hirota, Tunekazu Yamano, and Hyakuji Yabuuchi. "A family with pseudodeficiency of acid α-glucosidase." Clinical Genetics 33, no. 4 (June 28, 2008): 254–61. http://dx.doi.org/10.1111/j.1399-0004.1988.tb03446.x.

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Banno, Yoshiko, Noboru Sasaki, Thikako Yoshino, Yukio Okano, Kunimitsu Kaya, and Yoshinori Nozawa. "Species-specific antibodies of Tetrahymena acid α-glucosidase." Comparative Biochemistry and Physiology Part B: Comparative Biochemistry 100, no. 1 (January 1991): 31–35. http://dx.doi.org/10.1016/0305-0491(91)90080-w.

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38

Cardullo, Nunzio, Vera Muccilli, Vincenzo Cunsolo, and Corrado Tringali. "Mass Spectrometry and 1H-NMR Study of Schinopsis lorentzii (Quebracho) Tannins as a Source of Hypoglycemic and Antioxidant Principles." Molecules 25, no. 14 (July 17, 2020): 3257. http://dx.doi.org/10.3390/molecules25143257.

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The ethyl acetate extract of the commercial tannin Tan’Activ QS-SOL (from Schinopsis lorentzii wood), employed for the production of red wine, was subjected to chromatography on Sephadex LH-20, providing nine fractions (A-1–A-9), which were estimated for total phenols content (GAE), antioxidant activity (DPPH, ORAC), and hypoglycemic activity (α-glucosidase and α-amylase inhibition). All the fractions were analyzed by means of HPLC/ESI-MS/MS and 1H-NMR to identify the principal active constituents. Fractions A-1 and A-3 showed the highest antioxidant activity and gallic acid (1), pyrogallol (3), eriodictyol (6), catechin (12), and taxifolin (30) were identified as the major constituents. The highest α-glucosidase and α-amylase inhibitory activity was observed in fractions A-7–A-9 containing condensed (9′, 15, 18, 19, 23, and 27) hydrolysable tannins (13 and 32) as well as esters of quinic acid with different units of gallic acid (5, 11, 11′, 14, and 22). This last class of gallic acid esters are here reported for the first time as α-glucosidase and α-amylase inhibitors.

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Puspitasari, Yunita Eka, Hardoko Hardoko, Titik Dwi Sulistiyati, Alifah Nur Fajrin, and Hezkiel Oktorully Tampubolon. "Identifikasi Senyawa Fitokimia dari Daun Mangrove Sonneratia alba dan Analisis In Silico Sebagai Antidiabetes." Jurnal Perikanan dan Kelautan 27, no. 2 (June 14, 2022): 241. http://dx.doi.org/10.31258/jpk.27.2.241-248.

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Mangrove plant, Sonneratia alba, can be found abundantly in Indonesia. Some previous studies reported phytochemical screening and bioactivity test of Sonneratia sp. as anti-diabetic (in vitro and in vivo analysis). However, phytochemical identification of S. alba leaves and inhibitory activity of α-glucosidase as anti-diabetic have not been reported. The purpose of this study are to identify phytochemical compounds of methanolic extracts S. alba leaves, and to predict inhibitory mechanisms of S. alba leaves against α-glucosidase through in silico analysis. In this study, the research method consists of two steps namely identification phytochemical compounds of methanolic extracts S. alba leaves, and prediction inhibitory activities of phytochemical compounds of methanolic extracts S. alba leaves against α-glucosidase by molecular docking (in silico) analysis. Methanolic extracts S. alba leaves contained orientin, vitexin, luteolin, oleanolic acid and reserpine. Reserpine was identified for the first time in S. alba leaves. Based on in silico analysis, binding energy of orientin, vitexin, luteolin, oleanolic acid, reserpine and acarbose (positive control) against α-glucosidase were -9,7; -9,7; -9,2; -8,6; -10,0 dan -8,3 kcal/mol. This result indicated that compounds inhibited α-glucosidase activities and can be considered as antidiabetic agent.

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Zhang, Yu, Bing Bai, Yu Yan, Juan Liang, and Xiao Guan. "Bound Polyphenols from Red Quinoa Prevailed over Free Polyphenols in Reducing Postprandial Blood Glucose Rises by Inhibiting α-Glucosidase Activity and Starch Digestion." Nutrients 14, no. 4 (February 9, 2022): 728. http://dx.doi.org/10.3390/nu14040728.

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Inhibiting α-glucosidase activity is important in controlling postprandial hyperglycemia and, thus, helping to manage type-2 diabetes mellitus (T2DM). In the present study, free polyphenols (FPE) and bound polyphenols (BPE) were extracted from red quinoa and their inhibitory effects on α-glucosidase and postprandial glucose, as well as related mechanisms, were investigated. HPLC-MS analysis showed that the components of FPE and BPE were different. FPE was mainly composed of hydroxybenzoic acid and its derivatives, while BPE was mainly composed of ferulic acid and its derivatives. BPE exhibited stronger DPPH and ABTS antioxidant activities, and had a lower IC50 (10.295 mg/mL) value in inhibiting α-glucosidase activity. The inhibition kinetic mode analysis revealed that FPE and BPE inhibited α-glucosidase in a non-competitive mode and an uncompetitive mode, respectively. Furthermore, compared to FPE, BPE delayed starch digestion more effectively. BPE at 50 mg/kg reduced postprandial glucose increases comparably to acarbose at 20 mg/kg in ICR mice. These results could provide perspectives on the potential of BPE from red quinoa, as a functional food, to inhibit α-glucosidase activity, delay postprandial glucose increases and manage T2DM.

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Umapathysivam, Kandiah, John J. Hopwood, and Peter J. Meikle. "Determination of Acid α-Glucosidase Activity in Blood Spots as a Diagnostic Test for Pompe Disease." Clinical Chemistry 47, no. 8 (August 1, 2001): 1378–83. http://dx.doi.org/10.1093/clinchem/47.8.1378.

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Abstract Background: Pompe disease is an autosomal recessive disorder of glycogen metabolism that is characterized by a deficiency of the lysosomal acid α-glucosidase. Enzyme replacement therapy for the infantile and juvenile forms of Pompe disease currently is undergoing clinical trials. Early diagnosis before the onset of irreversible pathology is thought to be critical for maximum efficacy of current and proposed therapies. In the absence of a family history, the presymptomatic detection of these disorders ideally can be achieved through a newborn-screening program. Currently, the clinical diagnosis of Pompe disease is confirmed by the virtual absence, in infantile onset, or a marked reduction, in juvenile and adult onset, of acid α-glucosidase activity in muscle biopsies and cultured fibroblasts. These assays are invasive and not suited to large-scale screening. Methods: A sensitive immune-capture enzyme activity assay for the measurement of acid α-glucosidase protein was developed and used to determine the activity of this enzyme in dried-blood spots from newborn and adult controls, Pompe-affected individuals, and obligate heterozygotes. Results: Pompe-affected individuals showed an almost total absence of acid α-glucosidase activity in blood spots. The assay showed a sensitivity and specificity of 100% for the identification of Pompe-affected individuals. Conclusions: The determination of acid α-glucosidase activity in dried-blood spots is a useful, noninvasive diagnostic assay for the identification of Pompe disease. With further validation, this procedure could be adapted for use with blood spots collected in newborn-screening programs.

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Rasool, Nasir, Muhammad Abid Rashid, Saleha Suleman Khan, Zulfiqar Ali, Muhammd Zubair, Viqar Uddin Ahmad, Shamsun Nahar Khan, M. Iqbal Choudhary, and Rasool Bakhsh Tareen. "Novel α-Glucosidase Activator from Pulicaria undulata." Natural Product Communications 8, no. 6 (June 2013): 1934578X1300800. http://dx.doi.org/10.1177/1934578x1300800618.

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A new ent –kaurane type diterpene glucoside, pulicarside (1), together with three known terpenoids, paniculoside IV (2, diterpene), ent–16, 17-dihydroxy-(-)-kauran-19–oic acid (3, diterpene), and 2α–hydroxy alantolactone (4, sesquiterpene) have been isolated from Pulicaria undulata L. Their structures were determined with the help of spectral studies. Pulicarside (1) showed α-glucosidase activator activity, whereas its hydrolyzed product ent-16, 17-dihydroxy-(-)-kauran-19-oic acid (3) exhibited strong α-glucosidase inhibitory activity. Paniculoside IV (2) also shows high inhibitory potency compared with the standard drug acarbose.

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Nakagawa, Toshinori, Ahmed Ashour, Yhiya Amen, Yurie Koba, Koichiro Ohnuki, and Kuniyoshi Shimizu. "α-Glucosidase Inhibitory Activity of Resin From Sakhalin fir Tree (Abies sachalinensis) and its Bioactive Compounds." Natural Product Communications 14, no. 6 (June 2019): 1934578X1985846. http://dx.doi.org/10.1177/1934578x19858460.

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This study investigated in vitro the α-glucosidase inhibitory activity of resin from the Sakhalin fir tree ( Abies sachalinensis). The resin showed extremely high activity (IC50 of 17.3 µg/mL). We isolated 8 compounds from the resin and identified them. All of the compounds isolated from A. sachalinensis resin are reported for the first time in the present study. In an α-glucosidase inhibitory assay, 6 compounds—(holophyllane C (1), (−) -(24 E)-23-oxo-3,4- seco-9β H-lanosta-4(28),6,8(14),24-tetraen-3,26-dioic acid (2), abiesonic acid (3), (−) -(24 E)-23-oxo-3,4- seco-9β H-lanosta-4(28),7,24-triene-3,26-dioic acid (4), 3,4- seco-4(28),6,8(14),22Z,24-mariesapentaen-26,23-olide-3-oic acid (5), and (−) -abiesonic acid 3-methyl ester (6))—showed high activity (their IC50 values were 25.1, 20.9, 82.4, 20.5, 27.3, and 20.5 µg/mL, respectively). These compounds should contribute to the resin’s α-glucosidase inhibitory activity. From an industrial point of view, these findings provide new data to support that the resin of A. sachalinensis is a rich source of α-glucosidase inhibitors, which are highly valuable for their potential to be developed as functional health foods.

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Shanak, Siba, Najlaa Bassalat, Raghad Albzoor, Sleman Kadan, and Hilal Zaid. "In Vitro and In Silico Evaluation for the Inhibitory Action of O. basilicum Methanol Extract on α-Glucosidase and α-Amylase." Evidence-Based Complementary and Alternative Medicine 2021 (July 6, 2021): 1–9. http://dx.doi.org/10.1155/2021/5515775.

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Diabetes mellitus is a metabolic disease that predominates, nowadays. It causes hyperglycemia and consequently major health complications. Type II diabetes is the most common form and is a result of insulin resistance in the target tissues. To treat this disease, several mechanisms have been proposed. The most direct route is via inhibiting the intestinal enzymes, e.g., α-glucosidase and α-amylase, responsible for intestinal polysaccharide digestion that therefore would reduce the absorption of monosugars through the intestinal walls. In this study, we shed the light on this route by testing the inhibitory effect of Ocimum basilicum extract on the enzymes α-glucosidase and α-amylase in vitro and in silico. Experimental procedures were performed to test the effect of the O. basilicum methanol extract from aerial parts followed by the in silico docking. 500 μg/mL of the extract led to 70.2% ± 8.6 and 25.4% ± 3.3 inhibition on α-glucosidase and α-amylase activity, respectively. Similarly, the effect of caffeic acid, a major extract ingredient, was also tested, and it caused 42.7% ± 3.0 and 47.1% ± 4.0 inhibition for α-amylase and α-glucosidase, respectively. Docking experiments were performed to predict the phytochemicals responsible for this robust inhibitory activity in the O. basilicum extracts. Several compounds have shown variable levels of inhibition, e.g., caffeic acid, pyroglutamic acid, and uvasol. The results indicated that O. basilicum can be a potent antidiabetic drug.

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Zhang, Wengang, Yongli Lan, Bin Dang, Jie Zhang, Wancai Zheng, Yan Du, Xijuan Yang, and Zhonghong Li. "Polyphenol Profile and In Vitro Antioxidant and Enzyme Inhibitory Activities of Different Solvent Extracts of Highland Barley Bran." Molecules 28, no. 4 (February 9, 2023): 1665. http://dx.doi.org/10.3390/molecules28041665.

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Five different solvent extracts of highland barley bran were analyzed and compared for their polyphenol profile, antioxidant activity, and α-glucosidase and α-amylase inhibitory activities. The highland barley bran acetone extract had the highest total phenolic content, total flavonoid content, and antioxidant capacity. It was followed by the methanol and ethanol extracts, while n-butanol and ethyl acetate extracts exhibited lower measured values. Diosmetin, luteolin, protocatechuic acid, vanillic acid, ferulic acid, phlorogucinol, diosmin, isoquercitrin, catechin, and isovitexin were among the most abundant phenolic compounds identified in different solvent extracts, and their concentrations varied according to the solvent used. The highest α-glucosidase and α-amylase inhibitory activity were observed in the ethyl acetate extract of highland barley bran, followed by the acetone and methanol extracts. In contrast, n-butanol and ethanol extracts exhibited lower measured values. The different solvent extracts were effective inhibitors for α-glucosidase and α-amylase with activity reaching to 34.45–94.32% and 22.08–35.92% of that of positive control acarbose, respectively. There were obvious correlations between the phenolic content and composition of different solvent extracts and their in vitro antioxidant activity, α-glucosidase inhibition activity and α-amylase inhibition activity. Black barley bran is an excellent natural raw material for developing polyphenol-rich functional foods and shows good antioxidant and hypoglycemic potential to benefit human health.

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Zheng, Yuxue, Jinhu Tian, Wenhan Yang, Shiguo Chen, Donghong Liu, Haitian Fang, Huiling Zhang, and Xingqian Ye. "Inhibition mechanism of ferulic acid against α-amylase and α-glucosidase." Food Chemistry 317 (July 2020): 126346. http://dx.doi.org/10.1016/j.foodchem.2020.126346.

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SIMAMORA, ADELINA, ADIT WIDODO SANTOSO, and KRIS HERAWAN TIMOTIUS. "α-Glucosidase Inhibitory Effect of Fermented Fruit Juice of Morinda Citrifolia L and Combination Effect with Acarbose." Current Research in Nutrition and Food Science Journal 7, no. 1 (April 1, 2019): 218–26. http://dx.doi.org/10.12944/crnfsj.7.1.21.

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Fermented fruit juice of M.citrifoliais supposed to be the future nutraceutical beverage due to its antidiabetic and antioxidant activities. The purposes of this study were to characterize the fermented juice microbiologically and chemically and to evaluate itsα-glucosidase inhibition and radical scavenging activities in vitro. The fruit of M.citrifolia was fermented and the fruit juice was obtained and evaluated for its radical scavenging activity based on a DPPH assay. It's in vitroanti diabetic activity on α-glucosidase inhibition was investigated, including its combined effect with acarbose by a Chou-Talalay method. The inhibition mode was evaluated by Line weaver-Burk plots. The juice was identified for its microbiome with 16S sequencing method and pictured with SEM. The bioactive compounds were analysed with LC-MS. The main microbiome was yeast and tentatively identified as Candida. The yeast was not able to grow in the normal growth medium for yeast, such as sabouroud agar. The TPC of the juice was 1,193 μg GAE/ml. The main compounds identified by an LC-MS were short-chain fatty acids (α-ketoglutaric acid and malic acid). The fermented fruit juice showed good α-glucosidase inhibitory and antioxidant activities with IC50 of 28.99 and 14.09μgGAE/ml, respectively. The kinetic study showed a non-competitive inhibition on α-glucosidase. The combination of the juice with acarbose at higher concentrations produced an additive effect on α-glucosidase. However, at lower concentrations, an antagonistic effect was observed. The fermented fruit juice of M.citrifoliais a good beverage with strong antidiabetic and antioxidant effects.

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Medina-Pérez, Gabriela, José Antonio Estefes-Duarte, Laura N. Afanador-Barajas, Fabián Fernández-Luqueño, Andrea Paloma Zepeda-Velásquez, Melitón Jesús Franco-Fernández, Armando Peláez-Acero, and Rafael Germán Campos-Montiel. "Encapsulation Preserves Antioxidant and Antidiabetic Activities of Cactus Acid Fruit Bioactive Compounds under Simulated Digestion Conditions." Molecules 25, no. 23 (December 4, 2020): 5736. http://dx.doi.org/10.3390/molecules25235736.

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Cactus acid fruit (Xoconostle) has been studied due its content of bioactive compounds. Traditional Mexican medicine attributes hypoglycemic, hypocholesterolemic, anti-inflammatory, antiulcerogenic and immunostimulant properties among others. The bioactive compounds contained in xoconostle have shown their ability to inhibit digestive enzymes such as α-amylase and α-glucosidase. Unfortunately, polyphenols and antioxidants in general are molecules susceptible to degradation due to storage conditions, (temperature, oxygen and light) or the gastrointestinal tract, which limits its activity and compromises its potential beneficial effect on health. The objectives of this work were to evaluate the stability, antioxidant and antidiabetic activity of encapsulated extract of xoconostle within double emulsions (water-in-oil-in-water) during storage conditions and simulated digestion. Total phenols, flavonoids, betalains, antioxidant activity, α-amylase and α-glucosidase inhibition were measured before and after the preparation of double emulsions and during the simulation of digestion. The ED40% (treatment with 40% of xoconostle extract) treatment showed the highest percentage of inhibition of α-glucosidase in all phases of digestion. The inhibitory activity of α-amylase and α-glucosidase related to antidiabetic activity was higher in microencapsulated extracts than the non-encapsulated extracts. These results confirm the viability of encapsulation systems based on double emulsions to encapsulate and protect natural antidiabetic compounds.

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Heydari, Zahra, Maryam Mohammadi-Khanaposhtani, Somaye Imanparast, Mohammad A. Faramarzi, Mohammad Mahdavi, Parviz R. Ranjbar, and Bagher Larijani. "Pyrano[3,2-c]quinoline Derivatives as New Class of α-glucosidase Inhibitors to Treat Type 2 Diabetes: Synthesis, in vitro Biological Evaluation and Kinetic Study." Medicinal Chemistry 15, no. 1 (January 7, 2019): 8–16. http://dx.doi.org/10.2174/1573406414666180528110104.

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Background: Pyrano[3,2-c]quinoline derivatives 6a–n were synthesized via simple two-step reactions and evaluated for their in vitro α-glucosidase inhibitory activity. Methods: Pyrano[3,2-c]quinoline derivatives 6a–n derivatives were prepared from a two-step reaction: cycloaddition reaction between 1-naphthyl amine 1 and malonic acid 2 to obtain benzo[h]quinoline-2(1H)-one 3 and reaction of 3 with aryl aldehydes 4 and Meldrum’s acid 5. The anti- α-glucosidase activity and kinetic study of the synthesized compounds were evaluated using α-glucosidase from Saccharomyces cerevisiae and p-nitrophenyl-a-D-glucopyranoside as substrate. The α-glucosidase inhibitory activity of acarbose was evaluated as positive control. Results: All of the synthesized compounds, except compounds 6i and 6n, showed more inhibitory activity than the standard drug acarbose and were also found to be non-cytotoxic. Among the synthesized compounds, 1-(2-bromophenyl)-1H-benzo[h]pyrano[3,2-c]quinoline-3,12(2H,11H)-dione 6e displayed the highest α-glucosidase inhibitory activity (IC50 = 63.7 ± 0.5 µM). Kinetic study of enzyme inhibition indicated that the most potent compound, 6e, is a non-competitive inhibitor of α-glucosidase with a Ki value of 72 µM. Additionally, based on the Lipinski rule of 5, the synthesized compounds were found to be potential orally active drugs. Conclusion: Our results suggest that the synthesized compounds are promising candidates for treating type 2 diabetes.

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Jin, Hui-Min, Bin Dang, Wen-Gang Zhang, Wan-Cai Zheng, and Xi-Juan Yang. "Polyphenol and Anthocyanin Composition and Activity of Highland Barley with Different Colors." Molecules 27, no. 11 (May 25, 2022): 3411. http://dx.doi.org/10.3390/molecules27113411.

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In this research, the composition of free phenols, bound phenols, and anthocyanins and their in vitro antioxidant activity and in vitro α-glucosidase inhibiting activity were observed in different barley colors. The outcomes revealed that the contents of total phenols (570.78 mg/100 gDW), total flavonoids (47.08 mg/100 gDW), and anthocyanins (48.07 mg/100 g) were the highest in purple barley. Furthermore, the structure, composition, and concentration of phenolics differed depending on the colors of barley. The types and contents of bound total phenolic acids and flavonoids were greater than those of free total phenolic acids and flavonoids. The main phenolic acids in blue barley were cinnamic acid polyphenols, whereas in black, yellow, and purple barley, benzoic acid polyphenols were the main phenolic acids, and the main types of flavonoids in black and blue barley were chalcones and flavanones, respectively, whereas flavonol was the main type of flavonoid in yellow and purple barley. Moreover, cornflower pigment-3-glucoside was the major anthocyanin in blue, yellow, and purple barley, whereas the main anthocyanin in black barley was delphinidin-3-glucoside. The dark color of barley indicated richness in the anthocyanins. In addition, the free polyphenol fractions had stronger DPPH and ABTS radical scavenging capacity as compared to the bound ones. In vitro α-glucosidase-inhibiting activity was greater in bound polyphenols than in free polyphenols, with differences between different varieties of barley. Purple barley phenolic fractions had the greatest ABTS radical scavenging and iron ion reduction capacities, as well as the highest α-glucosidase-inhibiting activity. The strongest DPPH radical scavenging capacity was found in yellow barley, while the strongest in vitro α-glucosidase-inhibiting activity was found in anthocyanins isolated from black barley. Furthermore, in different colors of barley, there was a strong association between the concentration of specific phenolic compounds and antioxidant and α-glucosidase-inhibiting activities. The outcomes of this study revealed that all colored barley seeds tested were high in phenolic compounds, and had a good antioxidant impact and α-glucosidase-inhibiting activity. As a result, colored barley can serve as an antioxidant and hypoglycemic food. Polyphenols extracted from purple barley and anthocyanins extracted from black barley stand out among them.

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Journal articles on the topic 'Acid α-glucosidase'

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