Relevant bibliographies by topics / Α -glucosidase

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  1. Journal articles
  2. Dissertations / Theses
  3. Book chapters
  4. Conference papers
  5. Reports

Academic literature on the topic 'Α -glucosidase'

Author: Grafiati
Published: 4 June 2021
Last updated: 20 February 2023

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Journal articles on the topic "Α -glucosidase"

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Schmidt, Sabine, Sandra Rainieri, Simone Witte, Ulrich Matern, and Stefan Martens. "Identification of aSaccharomyces cerevisiaeGlucosidase That Hydrolyzes Flavonoid Glucosides." Applied and Environmental Microbiology 77, no. 5 (January 7, 2011): 1751–57. http://dx.doi.org/10.1128/aem.01125-10.

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ABSTRACTBaker's yeast (Saccharomyces cerevisiae) whole-cell bioconversions of naringenin 7-O-β-glucoside revealed considerable β-glucosidase activity, which impairs any strategy to generate or modify flavonoid glucosides in yeast transformants. Up to 10 putative glycoside hydrolases annotated in theS. cerevisiaegenome database were overexpressed with His tags in yeast cells. Examination of these recombinant, partially purified polypeptides for hydrolytic activity with synthetic chromogenic α- or β-glucosides identified three efficient β-glucosidases (EXG1, SPR1, and YIR007W), which were further assayed with natural flavonoid β-glucoside substrates and product verification by thin-layer chromatography (TLC) or high-performance liquid chromatography (HPLC). Preferential hydrolysis of 7- or 4′-O-glucosides of isoflavones, flavonols, flavones, and flavanones was observedin vitrowith all three glucosidases, while anthocyanins were also accepted as substrates. The glucosidase activities of EXG1 and SPR1 were completely abolished by Val168Tyr mutation, which confirmed the relevance of this residue, as reported for other glucosidases. Most importantly, biotransformation experiments with knockout yeast strains revealed that only EXG1 knockout strains lost the capability to hydrolyze flavonoid glucosides.
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Fogarty, William M., Catherine T. Kelly, and Sunil K. Kadam. "Separation and characterization of an α-glucosidase and maltase from Bacillus amyloliquefaciens." Canadian Journal of Microbiology 31, no. 8 (August 1, 1985): 670–74. http://dx.doi.org/10.1139/m85-127.

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A novel α-glucosidase and a maltase were isolated from Bacillus amyloliquefaciens. The formation of both enzymes was induced by trehalose, sucrose, or lactose in the growth medium. Trehalose is by far the most efficient inducer of both systems. The α-glucosidase and maltase were separated and purified by ion-exchange chromatography on DEAE Bio-Gel A. Purified α-glucosidase hydrolysed p-nitrophenyl-α-D-glucoside, isomaltose, and isomaltotriose but sucrose, maltose, or related saccharides were not attacked. β-Glucosides and polymeric glucosides were not degraded. The optimum temperature for α-glucosidase activity was 40 °C and its pH optimum was 5.3. The molecular weight and isoelectric point (pI) of the enzyme were 27 000 and 4.6, respectively. Purified maltase attacked maltose and sucrose, while maltotriose and melezitose were hydrolysed at slower rates and p-nitrophenyl-α-D-glucoside was not degraded. Other properties of the maltase were as follows: optimum temperature for activity, 30 °C; pH optimum, 6.5; molecular weight, 64 000; and pI, 4.7.
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Li, Xun, Hua Xiang Gu, Hao Shi, and Fei Wang. "Overexpression and Phylogenetic Analysis of a Thermostable α-Glucosidase from Thermus thermophilus." Advanced Materials Research 1004-1005 (August 2014): 841–48. http://dx.doi.org/10.4028/www.scientific.net/amr.1004-1005.841.

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The α-glucosidase geneaglfromThermus thermophilusHB8 was cloned into expression vector pBV220. The phylogenetic trees of α-glucosidases were constructed using Neighbor-Joining (NJ) and Maximum-Parsimony (MP) methods. Evolution analysis indicated the α-glucosidase fromT. thermophileHB8 was distant from the other glycoside hydrolases 4 and 31 α-glucosidases. By weakening the mRNA secondary structure and replacing the rare codons for the N-terminal amino acids of the target protein, the expression level of theaglwas increased 30-fold. The recombinant AGL was purified by the heat treatment, and had a molecular mass of 61 kDa. The optimal activity was at pH 7.8 and 95°C over a 10 min assay. The purified enzyme was stable over a pH range of 5.4-8.6, and had a 1-h half life at 85°C. Kinetic experiments at 90°C withp-nitrophenyl-α-D-glucoside as substrate gave aKm, andVmaxof 0.072 mM and 400 U/mg. Thus, this report provides an industrial means to produce the recombinant α-glucosidase inE. coli.
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Baiya, Supaporn, Salila Pengthaisong, Sunan Kitjaruwankul, and James R. Ketudat Cairns. "Structural analysis of rice Os4BGlu18 monolignol β-glucosidase." PLOS ONE 16, no. 1 (January 20, 2021): e0241325. http://dx.doi.org/10.1371/journal.pone.0241325.

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Monolignol glucosides are storage forms of monolignols, which are polymerized to lignin to strengthen plant cell walls. The conversion of monolignol glucosides to monolignols is catalyzed by monolignol β-glucosidases. Rice Os4BGlu18 β-glucosidase catalyzes hydrolysis of the monolignol glucosides, coniferin, syringin, and p-coumaryl alcohol glucoside more efficiently than other natural substrates. To understand more clearly the basis for substrate specificity of a monolignol β-glucosidase, the structure of Os4BGlu18 was determined by X-ray crystallography. Crystals of Os4BGlu18 and its complex with δ-gluconolactone diffracted to 1.7 and 2.1 Å resolution, respectively. Two protein molecules were found in the asymmetric unit of the P212121 space group of their isomorphous crystals. The Os4BGlu18 structure exhibited the typical (β/α)8 TIM barrel of glycoside hydrolase family 1 (GH1), but the four variable loops and two disulfide bonds appeared significantly different from other known structures of GH1 β-glucosidases. Molecular docking studies of the Os4BGlu18 structure with monolignol substrate ligands placed the glycone in a similar position to the δ-gluconolactone in the complex structure and revealed the interactions between protein and ligands. Molecular docking, multiple sequence alignment, and homology modeling identified amino acid residues at the aglycone-binding site involved in substrate specificity for monolignol β-glucosides. Thus, the structural basis of substrate recognition and hydrolysis by monolignol β-glucosidases was elucidated.
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Thanakosai, Wannisa, and Preecha Phuwapraisirisan. "First Identification of α-Glucosidase Inhibitors from Okra (Abelmoschus Esculentus) Seeds." Natural Product Communications 8, no. 8 (August 2013): 1934578X1300800. http://dx.doi.org/10.1177/1934578x1300800813.

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Infusion of roasted okra seeds has long been consumed in Turkey for diabetes mellitus therapy. Previous reports of a hypoglycemic effect observed in rats administrated with okra seed extract indicated a possible connection with inhibition of intestinal α-glucosidase. An attempt to identify active components was first herein conducted using α-glucosidase-inhibition-guided isolation, yielding two major flavonol glucosides named isoquercetin (2) and quercetin-3- O-β-glucopyranosyl-(1″′ →6″)-glucoside (3). They selectively inhibited rat intestinal maltase and sucrase, in which isoquercetin (2) was 6–10 times more potent than its related diglucoside 3. This result suggested that an increase in hydrophilicity by the additional glucose residue in 3 led to a significant decline in the inhibitory effect and raised the possible involvement of the free 3-OH in exerting the inhibition. Our postulation was evaluated by examining α-glucosidase inhibition of quercetin (1), and the aglycone of 2 and 3, whose 3-OH is free from any glucose moiety. Interestingly, 1 displayed a broad inhibitory effect toward rat intestinal and baker's yeast α-glucosidases, with improved potency. A kinetic study of 1 indicated that it inhibited maltase by two distinct mechanisms, in competitive ( K i 462 μM) and noncompetitive ( K i 2153 μM) manners, whereas the mechanism underlying the inhibition of sucrase was verified as being of a competitive behavior ( K i 218 μM).
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Flores-Bocanegra, Laura, Rafael Torres-Colín, Martin González-Andrade, José S. Calderón, and Rachel Mata. "In Vivo and In Vitro α-Glucosidase Inhibitory Activity of Perfoliatin a from Melampodium Perfoliatum." Natural Product Communications 14, no. 1 (January 2019): 1934578X1901400. http://dx.doi.org/10.1177/1934578x1901400102.

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As part of our effort to discover new α-glucosidase inhibitors from natural sources, it was found that an aqueous extract from Melampodium perfoliatum (Cavanilles) Kunth (Asteraceae) inhibited the activity of rat-intestinal α-glucosidases in a concentration dependent manner (IC50= 958 μg/mL). Fractionation of the active extract led to the isolation of perfoliatin A (1), which was active against the mammal α-glucosidases and a recombinant α-glucosidase with maltase-glucoamylase activity obtained from Ruminococcus obeum. Kinetic analysis revealed that the interaction of 1 with R. obeum-α-glucosidase was noncompetitive. The calculated Ki was 0.68 ± 0.034 mM. In vivo testing using an oral sucrose tolerance test, in healthy and hyperglycemic mice, revealed that perfoliatin A (1) reduced significantly the postprandial peak, consistent with its α-glucosidase inhibitory activity. The effect was comparable or better to that of acarbose, a therapeutically used α-glucosidase inhibitor. Altogether, these findings clearly supported the α-glucosidase inhibitory activity of melampolide-type of sesquiterpene lactones.
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Zhao, Lin, Yuqiong Pei, Guoxin Zhang, Jiayao Li, Yujie Zhu, Mingjun Xia, Ke Yan, et al. "Efficient Synthesis and In Vitro Hypoglycemic Activity of Rare Apigenin Glycosylation Derivatives." Molecules 28, no. 2 (January 5, 2023): 533. http://dx.doi.org/10.3390/molecules28020533.

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Apigenin is a natural flavonoid with significant biological activity, but poor solubility in water and low bioavailability limits its use in the food and pharmaceutical industries. In this paper, apigenin-7-O-β-(6″-O)-d-glucoside (AG) and apigenin-7-O-β-(6″-O-succinyl)-d-glucoside (SAG), rare apigenin glycosyl and succinyl derivatives formed by the organic solvent-tolerant bacteria Bacillus licheniformis WNJ02 were used in a 10.0% DMSO (v/v) system. The water solubility of SAG was 174 times that of apigenin, which solved the application problem. In the biotransformation reaction, the conversion rate of apigenin (1.0 g/L) was 100% at 24 h, and the yield of SAG was 94.2%. Molecular docking showed that the hypoglycemic activity of apigenin, apigenin-7-glucosides (AG), and SAG was mediated by binding with amino acids of α-glucosidase. The molecular docking results were verified by an in vitro anti-α-glucosidase assay and glucose consumption assay of active compounds. SAG had significant anti-α-glucosidase activity, with an IC50 of 0.485 mM and enhanced glucose consumption in HepG2 cells, which make it an excellent α-glucosidase inhibitor.
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Viigand, Katrin, Kristina Põšnograjeva, Triinu Visnapuu, and Tiina Alamäe. "Genome Mining of Non-Conventional Yeasts: Search and Analysis of MAL Clusters and Proteins." Genes 9, no. 7 (July 16, 2018): 354. http://dx.doi.org/10.3390/genes9070354.

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Genomic clustering of functionally related genes is rare in yeasts and other eukaryotes with only few examples available. Here, we summarize our data on a nontelomeric MAL cluster of a non-conventional methylotrophic yeast Ogataea (Hansenula) polymorpha containing genes for α-glucosidase MAL1, α-glucoside permease MAL2 and two hypothetical transcriptional activators. Using genome mining, we detected MAL clusters of varied number, position and composition in many other maltose-assimilating non-conventional yeasts from different phylogenetic groups. The highest number of MAL clusters was detected in Lipomyces starkeyi while no MAL clusters were found in Schizosaccharomyces pombe and Blastobotrys adeninivorans. Phylograms of α-glucosidases and α-glucoside transporters of yeasts agreed with phylogenesis of the respective yeast species. Substrate specificity of unstudied α-glucosidases was predicted from protein sequence analysis. Specific activities of Scheffersomycesstipitis α-glucosidases MAL7, MAL8, and MAL9 heterologously expressed in Escherichia coli confirmed the correctness of the prediction—these proteins were verified promiscuous maltase-isomaltases. α-Glucosidases of earlier diverged yeasts L. starkeyi, B. adeninivorans and S. pombe showed sequence relatedness with α-glucosidases of filamentous fungi and bacilli.
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Giblin, Mary, Catherine T. Kelly, and William M. Fogarty. "Thermostable α-glucosidase produced by Bacillus caldovelox DSM411." Canadian Journal of Microbiology 33, no. 7 (July 1, 1987): 614–18. http://dx.doi.org/10.1139/m87-107.

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Bacillus caldovelox produces an intracellular α-glucosidase (EC 3.2.1.20). It is the most thermostable microbial α-glucosidase reported to date and a number of its properties are outlined here. It was purified by treatment with protamine sulphate and gel filtration on Sephadex G-150 and gave a single band on SDS–PAGE. The enzyme had highest activity on p-nitrophenyl-α-D-glucoside, which was 2.04 times higher than the activity on maltose, and it was inactive towards isomaltose. It had a molecular weight of 30 000 and an isoelectric point of pH 5.0. The enzyme operated most efficiently at pH 5.5–6.0 and at 50–60 °C. It possessed considerable pH stability, retaining 80% or more activity in the range pH 4.0–9.0. α-Glucosidases tend to be very unstable, but this enzyme was fully stable up to 60 °C for 1 h and retained 51% of its original activity on incubation at 70 °C over the same period. The presence of histidine, cysteine, and manganous ions improved the thermal stability of the enzyme considerably. EDTA, α,α′-dipyridyl, o-phenanthroline, barium, strontium, manganous ions, and glucose stimulated activity, while Tris, ribose, glucono-δ-lactone, and phenyl-α-D-glucoside inhibited activity.
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Alarico, Susana, Milton S. da Costa, and Nuno Empadinhas. "Molecular and Physiological Role of the Trehalose-Hydrolyzing α-Glucosidase from Thermus thermophilus HB27." Journal of Bacteriology 190, no. 7 (January 25, 2008): 2298–305. http://dx.doi.org/10.1128/jb.01794-07.

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ABSTRACT Trehalose supports the growth of Thermus thermophilus strain HB27, but the absence of obvious genes for the hydrolysis of this disaccharide in the genome led us to search for enzymes for such a purpose. We expressed a putative α-glucosidase gene (TTC0107), characterized the recombinant enzyme, and found that the preferred substrate was α,α-1,1-trehalose, a new feature among α-glucosidases. The enzyme could also hydrolyze the disaccharides kojibiose and sucrose (α-1,2 linkage), nigerose and turanose (α-1,3), leucrose (α-1,5), isomaltose and palatinose (α-1,6), and maltose (α-1,4) to a lesser extent. Trehalose was not, however, a substrate for the highly homologous α-glucosidase from T. thermophilus strain GK24. The reciprocal replacement of a peptide containing eight amino acids in the α-glucosidases from strains HB27 (LGEHNLPP) and GK24 (EPTAYHTL) reduced the ability of the former to hydrolyze trehalose and provided trehalose-hydrolytic activity to the latter, showing that LGEHNLPP is necessary for trehalose recognition. Furthermore, disruption of the α-glucosidase gene significantly affected the growth of T. thermophilus HB27 in minimal medium supplemented with trehalose, isomaltose, sucrose, or palatinose, to a lesser extent with maltose, but not with cellobiose (not a substrate for the α-glucosidase), indicating that the α-glucosidase is important for the assimilation of those four disaccharides but that it is also implicated in maltose catabolism.
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Dissertations / Theses on the topic "Α -glucosidase"

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Louro, Patrícia Isabel Ramos. "Avaliação e caracterização da ação inibitória de iminociclitóis na atividade alfa-glucosidase de células de mamífero." Master's thesis, Universidade de Évora, 2014. http://hdl.handle.net/10174/10890.

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Os inibidores das α-glucosidases, entre os quais se enquadram os iminociclitóis, são agentes de elevado interesse terapêutico uma vez que podem contribuir para a diminuição da absorção intestinal de glucose e, consequentemente, para um desagravamento da hiperglicemia em condições patológicas como a diabetes. Neste trabalho procurou-se estudar a ação de alguns compostos novos da família iminociclitol na atividade α-glucosidase de enterócitos de mamífero. Dos quatro compostos estudados (S,S) e (R,R) (3,4)-1-benzilpirrolidina-3,4-diol e (3R,4R)-pirrolidina-3,4-diol provocaram uma diminuição significativa da atividade enzimática α-glucosidase, sendo os IC50 inferiores a 5,8 mM. Os resultados apontam ainda para um mecanismo de inibição do tipo misto com valores e KI inferior a 1,2 mM. Os compostos estudados revelaram ser pouco tóxicos. Os resultados sugerem que estes compostos não constituem fármacos promissores enquanto inibidores de α-glucosidases, de mamífero. Contudo, dada a sua baixa toxicidade não são de excluir outras aplicações nomeadamente, agroindustriais; ### Abstract: “Evaluation and characterization of inhibitory action of iminociclitols on alpha-glucosidase activity in mammal’s cells.” Iminocyclitols as α-glucosidases inhibitors, are agents with high therapeutical interest since they contribute to diminish intestinal glucose absorption and consequently, to ameliorate hyperglycimia in pathological conditions such as diabetes. The aim of this work was to study the inhibitory effect of several iminocyclitol compounds on the α-glucosidase activity from enterocytes. Among the compounds studied, three, (S,S) and (R,R) (3,4)-1-benzilpyrrolidine-3,4-diol and (3R,4R)-pyrrolidine-3,4-diol had significant inhibitory action over α-glucosidase enzymatic activity with IC50 under 5,8 mM. It also show that the KI under 1,2 mM. Moreover, the compounds presented negligible toxicity effects.
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Bothon, Fifa. "Phytochimie et propriétés biologiques d'extraits de plantes antidiabétiques utilisées au Bénin." Thesis, Clermont-Ferrand 1, 2012. http://www.theses.fr/2012CLF1PP05.

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Le présent travail rend compte des études phytochimiques et biologiques d'extraits non volatils de quatre plantes utilisées au Bénin dans le traitement du diabète. La première partie passe en revue la bibliographie sur les plantes sujettes à notre étude. Dans cette partie, la systématique, l'importance en pharmacopée ainsi que les travaux déjà effectués sur ces plantes ont été présentés. La deuxième partie présente le mode d'extraction et les études chimiques des extraits et les résultats obtenus. La spectrophotométrie a permis de déterminer quelques grandes familles de composés présents dans les extraits : les polyphénols totaux, les flavonoïdes et les tanins tandis que la GC/MS et la LC/MS ont servi à mettre en exergue la présence de composés volatils et non volatils. La troisième partie décrit les tests biologiques in vitro et ex vitro effectués sur les extraits. Les extraits ont montré de manière générale des activités : inhibitrice de l' α-glucosidase, antioxydantes (DPPH, FRAP, ORAC), antimicrobiennes et l'une (Bridelia ferruginea) une activité cytotoxique sur les cellules cancéreuses (PA1, MCF7, PC3, DU-145), avec une efficacité variable d'une plante à une autre. La quatrième partie discute de manière générale des résultats issus des études phytochimiques et des tests biologiques. Parmi les quatre échantillons de plantes sélectionnées pour notre étude, seul l'extrait semi-éthanolique des racines de Ceiba pentandra a une faible teneur en familles de composés dosés et présente des activités biologiques (ci-dessus citées) faibles comparativement aux extraits de Bridelia ferruginea, de Pseudocedrela kotschyi et de Polygonum senegalensis. L'ensemble des résultats tant sur le plan chimique que biologique met en évidence les potentialités des extraits de plantes étudiées, pour une exploitation à des fins thérapeutiquesfutures
The present work had reported on the phytochemical and biological studies of non-volatile extracts of four plants used in Benin for diabetes treatment. The first part reviewed the bibliography of investigated plants in our study. In this part, the systematic, the importance in the pharmacopoeia and the previous works done on these plants were presented. The second part has presented the extraction method and chemical studies of the extracts and results obtained. The spectrophotometry has permitted to identify some important families of compounds in the extracts: the total polyphenols, flavonoids and tannins whereas the GC / MS and LC/MS were used to highlight the presence of volatile and non-volatile compounds. The third part described the biological tests in vitro and ex vitro carried out on the extracts. The extracts showed in general activities: α-glucosidase inhibition, antioxidant (DPPH, FRAP, ORAC), antimicrobial, and one of them (Bridelia ferruginea) were cytotoxic on cancer cells (PA1, MCF7, PC3, DU-145), with a variable efficiency from one plant to another. The fourth part had discussed in general about the results obtained from phytochemical studies and biological tests. Among the four plants samples selected for our study, only the semi-alcoholic extract of Ceiba pentandra roots had a low-dosed compounds families and presented of this biological activities (cited below) low comparatively to Bridelia ferruginea, Pseudocedrela kotschyi and Polygonum senegalensis extracts. Both of the chemical and biological results highlight the potential of certain species for future exploitation of their non-volatile extract for therapeutic purposes
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Shai, LJ, JN Eloff, N. Boaduo, AM Mogale, SR Magano, MP Mokgotho, and P. Masoko. "Yeast alpha glucosidase inhibitory and antioxidant activities of six medicinal plants collected in Phalaborwa, South Africa." Elsevier, 2010. http://encore.tut.ac.za/iii/cpro/DigitalItemViewPage.external?sp=1001248.

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Abstract Recent decades have experienced a sharp increase in the incidence and prevalence of diabetes mellitus. One antidiabetic therapeutic approach is to reduce gastrointestinal glucose production and absorption through the inhibition of carbohydrate-digesting enzymes such as α- amylase and α-glucosidase and α-amylase. The aim of the current study was to screen six medicinal plant species, with alleged antidiabetic properties for α-glucosidase inhibitory activities. Powdered plant materials were extracted with acetone, and tested for ability to inhibit baker's yeast α-glucosidase and α-amylase activities. The largest mass (440 mg from 10 g) of the extract was obtained from Cassia abbreviata, while both Senna italica and Mormordica balsamina yielded the lowest mass of the extracts. Extracts of stem bark of C. abbreviata inhibited baker's yeast α-glucosidase activity with an IC50 of 0.6 mg/ml. This plant species had activity at low concentrations, with 1.0 mg/ml and above resulting in inhibition of over 70%. The other five plant extracts investigated had IC50 values of between 1.8 and 3.0 mg/ml. Senna italica only managed to inhibit the activity of enzyme-glucosidase at high concentrations with an IC50 value of 1.8 mg/ml, while Tinospora fragosa extracts resulted in about 55% inhibition of the activity of the enzyme at a concentration of 3.5 mg/ml, with an estimated IC50 value of 2.8 mg/ml. The bark extract of C. abbreviata was the most active inhibitor of the enzyme, based on the IC50 values (0.6 mg/ml). The bark extract of C. abbreviata contains non-competitive inhibitor(s) of α-glucosidase, reducing Vmax value of this enzyme from 5 mM·s–1 to 1.67 mM·s–1, while Km remained unchanged at 1.43 mMfor para-nitrophenyl glucopyranoside. Antioxidant activity of the extracts was also investigated. The C. abbreviata extract was more active as an antioxidant than the positive control, trolox. The extracts did not inhibit alphaamylase activity more than about 20% at the highest concentration tested.
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4

Giudicelli, Jean. "L'alpha-glucosidase neutre : structure et fonction de la protéine." Paris 11, 1988. http://www.theses.fr/1988PA112140.

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L’ α-D-glucosidase neutre du rein de cheval (α -D-glucoside glucohydrolase EC 3. 2. 1. 20) a été purifiée sous une forme protéolytique par chromatographie d’ affinité. Les propriétés moléculaires, immunologiques et catalytiques de l'enzyme ont été déterminées. Un modèle minimum décrivant le fonctionnement du site actif a été proposé. L' enzyme a également été purifiée sous sa forme intégrale, sa nature amphipatique a été clairement établie. L’étude de la susceptibilité de la protéine vis-à-vis de différentes enzymes protéolytiques a permis de démontrer que l' α -D-glucosidase neutre possède un peptide intermédiaire de 2 à 5 nm. Une technique de préparation de protéoliposomes, constitués par des lécithines et des protéines intégrales de la membrane de bordure en brosse du rein de cheval, a été mise au point. Cette méthode permet d’obtenir des vésicules qui ont conservé les caractéristiques essentielles du transport du glucose et de la L-alanine, notamment la dépendance vis-à-vis des ions sodium. Cette méthode permet d'insérer l' α-D-glucosidase neutre sous sa forme intégrale, seule ou en association avec d'autres protéines. Une intégration asymétrique de la protéine, dans l'orientation qu'elle possède au sein de la membrane native ainsi qu' une topologie identique sont retrouvées dans les protéoliposomes formés. L'utilisation de ce modèle artificiel permet d'étudier le rôle de l'enzyme dans le transport du glucose. Les résultats obtenus avec du glucose libre ou du glucose produit par hydrolyse du maltose démontrent l'absence de toute participation de cette protéine dans le transfert transmembranaire de ce soluté
Neutral a-0-glucosidase which is purified after solubilization by Triton X-100 can easely be integrated in artificial vesicles. The fact that this enzyme bound to native and artificial membrane vesicles, exhibited the same antibodies-binding which is equivalent to that of the proteolytic form, demonstrated the free accessibility of the antigenic sites to specific antibody. Neutral a-0-glucosidase activity, associated with both membrane system, presented the same single activation energy and a Q10 as that observed for the proteolytic form of the enzyme, over the temperature range studied. This result which could be correlated with the external location of the bulk of the hydrophilic part of the enzyme was confirmed by proteolytic treatments using proteinases of various shapes. Findings allow us to conclude that the topology of the enzyme integrated in artificial membrane vesicles is the same as that of the native membrane bound enzyme. Horse kidney Neutral a-0-glucosidase integrated in native membranes or in proteoliposomes exhibited its hydrophilic part separated, out of the membrane surfaces, by a 2-5 nm junctional polypeptide segment
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5

Chen, Xian Qiang. "Study on the chemical constituents of ganoderma resinaceum and their α-glucosidase inhibitory activities." Thesis, University of Macau, 2018. http://umaclib3.umac.mo/record=b3952488.

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6

Nguyen, The Dương, Thanh Hoang Le, and Thi Tuyen Do. "Optimization of culture medium for the cultivation of Actinoplanes sp. mutant strains and purification of acarbose." Saechsische Landesbibliothek- Staats- und Universitaetsbibliothek Dresden, 2017. http://nbn-resolving.de/urn:nbn:de:bsz:14-qucosa-227839.

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In order to improve the production of acarbose, the fermentation medium of acarbose-producing strain Actinoplanes sp. KCTC 9161 – L14 mutant was optimized in this internship. Fractional factorial design was employ to investigate the influences of glucose, maltose and corn power on acarbose production (by a-glucosidase inhibitory ability). Two significant factors: glucose and maltose have significant and positive effects on acarbose amount. In addition, a model was obtained from the regression results of fractional factorial experiment. Other success, we demonstrated that chromatography by active charcoal column can used to purify acarbose from fermentation broth. Acarbose amount in purification solution was 191.5 g/L and an acarbose - purification process was inducted
Nhằm mục đích nâng cao khả năng sinh tổng hợp hoạt chất acarbose từ chủng đột biến Actinoplanes sp. KCTC 9161-L14, môi trường lên men của chủng dùng để sản xuất acarbose đã được tối ưu hóa. Một phần mềm thiết kế đã được thiết lập để khảo sát ảnh hưởng của glucose, maltose và bột ngô đến khả năng sản xuất acarbose (thông qua hoạt tính ức chế a-glucosidase). Kết quả đã cho thấy, hai yếu tố glucose và maltose có ý nghĩa quan trọng và ảnh hưởng trực tiếp đến khả năng sinh tổng hợp acarbose. Một phương trình đã được hình thành từ kết quả tối ưu. Bên cạnh đó, chúng tôi đã chứng minh được cột sắc ký sử dụng than hoạt tính có thể tinh sạch acarbose từ dịch lên men. Hàm lượng acarbose trong dung dịch tinh sạch đạt 191,5 g/l và một quy trình tinh sạch acarbose được đề xuất
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Ryan, Caroline Mary. "Anti-Diabetic and Anti-Obesity Activities of Cocoa (Theobroma cacao) via Physiological Enzyme Inhibition." Thesis, Virginia Tech, 2016. http://hdl.handle.net/10919/75003.

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Fermentation and roasting of cocoa (Theobroma cacao) decrease levels of polyphenolic flavanol compounds. However, it is largely unknown how these changes in polyphenol levels caused by processing affect cocoa's anti-diabetic and anti-obesity bioactivities, such as inhibition of certain enzymes in the body. Polyphenol profiles, protein-binding abilities, presence of compounds termed oxidative polymers, and abilities to inhibit α-glucosidase, pancreatic α-amylase, lipase, and dipeptidyl peptidase-IV (DPP4) in vitro were compared between unfermented bean (UB), fermented bean (FB), unfermented liquor (UL), and fermented liquor (FL) cocoa extracts. Overall, there were significant decreases (p<0.05) in total polyphenols, flavanols, and anthocyanins between the two sets of unfermented and fermented cocoa extracts (CEs). All CEs effectively inhibited α-glucosidase (lowest IC50 = 90.0 ug/mL for UL) and moderately inhibited α-amylase (lowest IC50=183 ug/mL for FL), lipase (lowest IC25=65.5 ug/mL for FB), and DPP4 (lowest IC25=1585 ug/mL for FB) in dose-dependent manners. Fermentation and roasting of the samples affected inhibition of each enzyme differently (both processes enhanced α-amylase inhibition). Improved α-glucosidase and α-amylase inhibitions were correlated with presence of different classifications of oxidative polymers, suggesting that these compounds could be contributing to the bioactivities observed. Some α-glucosidase inhibition might be due to non-specific protein-binding. Improved DPP4 inhibition was strongly correlated to increased CE degree of polymerization. In conclusion, potential enzyme inhibition activities of cocoa were not necessarily negatively affected by the large polyphenol losses that occur during fermentation and roasting. Additionally, it is possible that more complex compounds could be present in cocoa that contribute to its potential anti-diabetic and anti-obesity bioactivities.
Master of Science in Life Sciences
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Hogan, Shelly Patricia. "Grape Extracts for Type 2 Diabetes Treatment Through Specific Inhibition of α-Glucosidase and Antioxidant Protection." Diss., Virginia Tech, 2009. http://hdl.handle.net/10919/26725.

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Research was conducted to investigate the effect of phenolic compounds derived from inherently rich antioxidant grape extracts (GE) on α-glucosidase inhibitory activity in vitro and in vivo blood glucose control, oxidative stress, and inflammation associated with obesity-induced type 2 diabetes. Because intestinal α-glucosidase plays a key role in the digestion and absorption of complex carbohydrates, the inhibition of this enzyme is a metabolic target for managing diabetes by improving post-prandial blood glucose control. Initially, red Norton wine grape (Vitis aestivalis) and pomace extracts were evaluated and determined to have notable phenolic content and antioxidant properties. Next, grape skin (GSE) and pomace extract (GPE) were tested and both had in vitro yeast and mammalian α-glucosidase inhibitory activity. The GSE was 32-times more potent at inhibiting yeast α-glucosidase than acarbose, a commercial oral hypoglycemic agent. From HPLC and LC-MS analysis, three phenolics from the GSE (resveratrol, ellagic acid, and catechin) were identified as active inhibitory compounds. The acute administration of GPE (400 mg/kg bw) to mice reduced postprandial blood glucose level by 35% following an oral glucose tolerance test compared to the control. The daily supplementation (250 mg/kg bw) of GSE and GPE for 12-weeks to mice affected fasting blood glucose levels, oxidative stress, and inflammatory biomarkers associated with obesity and type 2 diabetes. At the end of the study, the GSE group gained significantly (P < 0.05) more weight (24.6 g) than the control, high fat, or GPE groups (11.2, 20.2, 19.6 g, respectively). Both GSE and GPE groups had lower fasting blood glucose levels (119.3 and 134.2 mg/dL, respectively) compared to the high fat group (144.6 mg/dL). The 12-week supplementation of GSE was associated with a higher plasma oxygen radical absorbance capacity (ORAC), lower liver lipid peroxidation as measure by TBARS, and lower levels of inflammation as measured by plasma C-reactive protein compared to the high fat group. In conclusion, our collective observations from these studies provide insight into the potential effects of antioxidant rich grape extracts on diabetes-related biomarkers through a dual mechanism of antioxidant protection and specific inhibition of intestinal α-glucosidases.
Ph. D.
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Albert, Heidemarie. "Studies on the α-glucosidase enzyme of Bacillus stearothermophilus, ATCC 7953, a biological indicator test organism." Thesis, University of Bath, 1995. https://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.295444.

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Pacheco, Simone Muniz. "Frutos da família Myrtaceae: Caracterização físicoquímica e potencial inibitório da atividade das enzimas digestivas." Universidade Federal de Pelotas, 2015. http://repositorio.ufpel.edu.br:8080/handle/prefix/3055.

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Conselho Nacional de Pesquisa e Desenvolvimento Científico e Tecnológico - CNPq
As espécies vegetais Campomanesia xanthocarpa (guabiroba), Eugenia uniflora (pitanga), Eugenia pyriformis (uvaia), Psidium cattleianum (araçá) e Syzygium cumini (jambolão) estão presentes na Floresta Atlântica e são utilizadas pela população, para tratar diversas patologias, especialmente o diabetes melito tipo 2. Entretanto, a eficácia destes tratamentos e o mecanismo envolvido ainda não foram totalmente elucidados. Neste contexto, o presente estudo teve como objetivo principal avaliar o potencial dos compostos naturais destes frutos em inibir as enzimas α-amilase e α- glicosidase que estão envolvidas no metabolismo de carboidratos. Estes frutos também foram avaliados físico-quimicamente, realizando-se dentre outras análises a quantificação dos compostos fenólicos totais e a determinação da atividade antioxidante (métodos ABTS e DPPH). Os extratos metanólicos de P. cattleianum (acesso 44), S. cumini e E. pyriformis (acessos 11 e 15) inibiram de forma significativa a atividade da α-amilase. Os extratos metanólicos de P. cattleianum (acessos 44 e 87) também inibiram a atividade da α-glicosidase, utilizando-se os substratos maltose e sacarose. Em virtude da atividade antioxidante, da elevada quantidade de compostos fenólicos e da capacidade de inibição das enzimas digestivas do metabolismo de carboidratos, os frutos de P. cattleianum (acessos 44 e 87), S. cumini e E. pyriformis (acessos 11 e 15) podem apresentar potencial uso no manejo da hiperglicemia pós-prandial.
Campomanesia xanthocarpa (guabiroba), Eugenia uniflora (pitanga), Eugenia pyriformis (uvaia), Psidium cattleianum (araçá) and Syzygium cumini (jambolão) grow in the Brazilian Atlantic Forest and their fruits are commonly used as medicine to treat diseases related to carbohydrate metabolism, such as diabetes. The effectiveness of these treatments has not been demonstrated neither the biochemical mechanism involved. Therefore this study was devised to evaluate the potential of natural compounds of these fruits to inhibit key enzymes α-amylase and α- glucosidase involved in the carbohydrate metabolism. The fruits were also subjected to physicochemical characterization, quantification of phenolics compounds and antioxidant activity (ABTS and DPPH methods). The methanolic extracts of P. cattleianum (access 44), S. cumini, E. pyriformis (accesses 11 and 15) distinctively inhibited α-amylase activity. The methanolic extracts of P. cattleianum. (accesses 44 and 87) also inhibited α-glycosidase activity, with either maltose or sucrose as substrate. By having antioxidant activities, a fairly content of phenolic compounds, and capacity to inhibit carbohydrate digestive enzymes, P. cattleianum (access 44 and 87), S. cumini and E. pyriformis (accesses 11 and 15) could be good candidates to be used in the management of postprandial hyperglycemia.
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Book chapters on the topic "Α -glucosidase"

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Leroux-Stewart, Josée, Rémi Rabasa-Lhoret, and Jean-Louis Chiasson. "α-Glucosidase inhibitors." In International Textbook of Diabetes Mellitus, 673–85. Chichester, UK: John Wiley & Sons, Ltd, 2015. http://dx.doi.org/10.1002/9781118387658.ch45.

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Scharnagl, Hubert, Winfried März, Markus Böhm, Thomas A. Luger, Federico Fracassi, Alessia Diana, Thomas Frieling, et al. "Acid α-Glucosidase Deficiency." In Encyclopedia of Molecular Mechanisms of Disease, 11. Berlin, Heidelberg: Springer Berlin Heidelberg, 2009. http://dx.doi.org/10.1007/978-3-540-29676-8_8622.

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Leung, Alexander K. C., William Lane M. Robson, Carsten Büning, Johann Ockenga, Janine Büttner, Hartmut Schmidt, Antonio V. Delgado-Escueta, et al. "Lysosomal α-Glucosidase Deficiency." In Encyclopedia of Molecular Mechanisms of Disease, 1240. Berlin, Heidelberg: Springer Berlin Heidelberg, 2009. http://dx.doi.org/10.1007/978-3-540-29676-8_8623.

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Nairn, Alison V., and Kelley W. Moremen. "Glucosidase, Alpha Neutral AB; Glucosidase II Subunit Beta (GANAB, PRKCSH, α-Glucosidase II)." In Handbook of Glycosyltransferases and Related Genes, 1283–95. Tokyo: Springer Japan, 2014. http://dx.doi.org/10.1007/978-4-431-54240-7_140.

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Schreckinger, Maria, Mary Ann Lila, Gad Yousef, and Elvira de Mejia. "Inhibition of α-Glucosidase and α-Amylase byVaccinium floribundumandAristotelia chilensisProanthocyanidins." In ACS Symposium Series, 71–82. Washington, DC: American Chemical Society, 2012. http://dx.doi.org/10.1021/bk-2012-1109.ch006.

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Creutzfeldt, W. "Panel Discussion: Future Aspects of α-Glucosidase Inhibition." In Acarbose for the Treatment of Diabetes Mellitus, 183–93. Berlin, Heidelberg: Springer Berlin Heidelberg, 1988. http://dx.doi.org/10.1007/978-3-642-73583-7_62.

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Su, Yanfang, Bing Gao, Tao Qin, Zhijing Gao, Wei Wang, and Jie Zhang. "Plant Secondary Metabolites with α-Glucosidase Inhibitory Activity." In Structure and Health Effects of Natural Products on Diabetes Mellitus, 179–95. Singapore: Springer Singapore, 2021. http://dx.doi.org/10.1007/978-981-15-8791-7_10.

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Bhatnagar, Aditi, and Abha Mishra. "α-Glucosidase Inhibitors for Diabetes/Blood Sugar Regulation." In Natural Products as Enzyme Inhibitors, 269–83. Singapore: Springer Nature Singapore, 2022. http://dx.doi.org/10.1007/978-981-19-0932-0_12.

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Truscheit, E., I. Hillebrand, B. Junge, L. Müller, W. Puls, and D. Schmidt. "Microbial α-Glucosidase Inhibitors: Chemistry, Biochemistry, and Therapeutic Potential." In Progress in Clinical Biochemistry and Medicine, 17–99. Berlin, Heidelberg: Springer Berlin Heidelberg, 1988. http://dx.doi.org/10.1007/978-3-642-73461-8_2.

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Schomburg, Dietmar, and Ida Schomburg. "hesperidin 6-O-α-l-rhamnosyl-β-d-glucosidase 3.2.1.168." In Class 2–3.2 Transferases, Hydrolases, 631–33. Berlin, Heidelberg: Springer Berlin Heidelberg, 2013. http://dx.doi.org/10.1007/978-3-642-36240-8_122.

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Conference papers on the topic "Α -glucosidase"

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"Determination of Antioxidant Property, Total Phenolics Content, and α-Glucosidase Inhibitory Activity of Different Solvent Extracts of Defatted and Non-Defatted Peanut Skins." In 4th International Conference on Biological & Health Sciences (CIC-BIOHS’2022). Cihan University, 2022. http://dx.doi.org/10.24086/biohs2022/paper.781.

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Peanut skins are by-product with little economic value. The effect of different solvents, on the total phenolic content (TPC), antioxidant property and in vitro antidiabetic activity of defatted and non-defatted peanut skins was determined. TPC was estimated using Folin-Ciocalteau reagent. Antioxidant property was evaluated using ferric reducing antioxidant power (FRAP) and 2, 2-diphenyl-1- picrylhydrazyl (DPPH) radical scavenging capacity methods, α-glucosidase inhibition was evaluated using 4- nitrophenyl α-D-glucopyranoside (pNPG) method. Peanut skin of the defatted extracted with ethanol had the much of the content of total phenolics (391.76 mg/g GAE). Highest DPPH scavenging property was found in the methanolic extract of defatted peanut skins with IC50 value of 15.00 ± 1.00 μg/mL, while highest FRAP value was found in the aqueous extract of non-defatted extracts. Aqueous extracts demonstrated stronger inhibitory property against α-glucosidase and had IC50 of 16.33 ± 1.15 and 16.33 ± 8.50 μg/mL for defatted and non-defatted extracts, respectively. The finding of the present shows that peanut skins are important by-product for utilization as natural antioxidant and α-glucosidase inhibitors.
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Li, T., KT Kongstad, and D. Staerk. "High-resolution α-glucosidase inhibition profiling combined with HPLC-HRMS-SPE-NMR for identification of α-glucosidase inhibitors in Machilus litseifolia (Lauraceae)." In GA 2017 – Book of Abstracts. Georg Thieme Verlag KG, 2017. http://dx.doi.org/10.1055/s-0037-1608251.

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Wu, Meifu, and Hongli Zhou. "INHIBITORY EFFECT AND ENZYMOLYSIS KINETICS OF LENTINAN ON Α-GLUCOSIDASE." In International Conference on New Materials and Intelligent Manufacturing (ICNMIM). Volkson Press, 2018. http://dx.doi.org/10.26480/icnmim.01.2018.312.314.

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Min, BS, M. T. Ha, J. A. Kim, and J. S. Choi. "PTP1B and α-glucosidase inhibitory activities of Hedera rhombea compounds." In GA – 70th Annual Meeting 2022. Georg Thieme Verlag KG, 2022. http://dx.doi.org/10.1055/s-0042-1759268.

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Ambarwati, Neneng, Berna Elya, Putu Mahayasih, Muhamad Awang, Hanita Omar, Islamudin Ahmad, and Dwi Atmanto. "In-vitro α-Glucosidase Inhibitory Activity of Litsea petiolata Hk. f." In Proceedings of the 1st International Conference on Health Science, ICHS 2020, 26-27 October 2020, Jakarta, Indonesia. EAI, 2021. http://dx.doi.org/10.4108/eai.26-10-2020.2311312.

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"Progress of α-Glucosidase Inhibitor in Mulberry Leavesand Its Hypoglycemic Effect." In 2022 International Conference on Biotechnology, Life Science and Medical Engineering. Clausius Scientific Press, 2022. http://dx.doi.org/10.23977/blsme.2022026.

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Ishartati, Erny, Dyah Roeswitawati, Sukardi, Saefur Rohman, and Sudiadi. "α-Glucosidase and α -Amylase Inhibitory Activities of Jambolan (Syzygium cumini (L.) SKEELS) Fruit and Seed." In 3rd KOBI Congress, International and National Conferences (KOBICINC 2020). Paris, France: Atlantis Press, 2021. http://dx.doi.org/10.2991/absr.k.210621.043.

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Srećković, N., N. Mihailović, and V. Mihailović. "Lysimachia vulgaris L. aerial part and root methanol extracts as potential α-amylase and α-glucosidase inhibitors." In GA – 70th Annual Meeting 2022. Georg Thieme Verlag KG, 2022. http://dx.doi.org/10.1055/s-0042-1759175.

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Indrianingsih, Anastasia Wheni, and Amalia Indah Prihantini. "In vitro antioxidant and α-glucosidase inhibitory assay of Zingiber cassumunar roxb." In 2ND INTERNATIONAL CONFERENCE ON CHEMISTRY, CHEMICAL PROCESS AND ENGINEERING (IC3PE). Author(s), 2018. http://dx.doi.org/10.1063/1.5064965.

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Saprudin, D., I. Batubara, and N. P. Putri. "Endosperm of Indramayu mango (Mangifera indica) as α-glucosidase inhibitor and antioxidant." In THE 8TH INTERNATIONAL CONFERENCE OF THE INDONESIAN CHEMICAL SOCIETY (ICICS) 2019. AIP Publishing, 2020. http://dx.doi.org/10.1063/5.0001080.

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Reports on the topic "Α -glucosidase"

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Farazi, Mena, Michael Houghton, Margaret Murray, and Gary Williamson. Systematic review of the inhibitory effect of extracts from edible parts of nuts on α-glucosidase activity. INPLASY - International Platform of Registered Systematic Review and Meta-analysis Protocols, August 2022. http://dx.doi.org/10.37766/inplasy2022.8.0061.

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Review question / Objective: The aim of this review is to examine inhibitory effect of functional components in extracts from edible nuts on α-glucosidase activity. At the end of this review the following questions will be addressed by summarizing data of in-vitro studies: which nut extract has the strongest inhibitory effect? Which functional component (e.g. polyphenols) has the strongest inhibitory effect against α-glucosidase? Are there any differences between inhibition of α-glucosidase from different sources (e.g. yeast and mammalian)? Condition being studied: Any papers looking at inhibition of α-glucosidase activity (a carbohydrate digestive enzyme; includes sucrase, maltase and isomaltase activities) by extracts of edible parts of nut will be included in this review. Papers looking at other parts of nut plants and other enzymes will be excluded.
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Turner, Joshua, Lizabeth Thomas, and Sarah Kennedy. Structural Analysis of a New Saccharomyces cerevisiae α-glucosidase Homology Model and Identification of Potential Inhibitor Enzyme Docking Sites. Journal of Young Investigators, October 2020. http://dx.doi.org/10.22186/jyi.38.4.27-33.

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