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> Chemicals & Drugs > Amino Acid > Glucosidase

Glucosidase

Glucosidase is a class of enzymes that catalyze the hydrolysis of glucosidic bonds, breaking down complex carbohydrates into simpler sugars.
These enzymes play a key role in various biological processes, including digestion, energy production, and glycosylation.
Glucosidases are found in a wide range of organisms, from microbes to plants and animals, and have diverse applications in fields such as biotechnology, medicine, and agriculture.
Understanding the function and regulation of glucosidases is crucial for developing effective treatments for metabolic disorders, optimizing biofuel production, and enhancing crop yields.
Reseachers can leverage PubCompare.ai's AI-driven platform to streamline their glucosidase research, locate the best protocols, and enhance reproducibility and accuracy.

Most cited protocols related to «Glucosidase»

1
Optimizing Switchgrass Enzymatic Hydrolysis
Cited 7 times
For all subsequent experiments described in this paper, AFEX was performed at the estimated optimal conditions determined from the above experiments. The same treatment method was used except that AFEX was performed in a 1.5 l reactor rather than a 22 ml reactor. Between 80 to 150 g dry switchgrass was used for each batch. The amount of switchgrass depended on the ammonia loading, as a practical limitation of the ammonia loading vessel was 160 g. Multiple batches of AFEX treatment were performed, and no significant differences (P < 0.05) were seen in sugar released through enzymatic hydrolysis between batches. All batches were then combined before proceeding with further experiments.
Four commercial enzymatic mixtures were used in these experiments: Accelerase, the b-glucosidase Novozyme 188 (Novozymes, Cambridge, MA, batch no. 058K1144), Multifect Xylanase (Genencor, batch no. 4900805391), and Multifect Pectinase (Genencor, batch no. 4010833580). Enzyme concentrations were determined by nitrogen analysis using a Skalar Primacs SN Total Nitrogen Analyser (Breda, The Netherlands), which uses the Dumas method of combusting all nitrogen to NOx. Enzyme loading varied between 5 to 20 mg/g biomass for Accelerase and 0 to 10 mg/g biomass for the other enzyme mixtures. A total of 48 hydrolysis experiments were run for each type of switchgrass, representing 25 different enzyme combinations determined using the Box-Behnken method [19 (link)]. Hydrolysis was performed in the manner stated above. Results were analysed with Minitab 15 using response surface methodology to determine the importance of each type of enzyme in releasing sugars.
Bals B., Rogers C., Jin M., Balan V, & Dale B. (2010). Evaluation of ammonia fibre expansion (AFEX) pretreatment for enzymatic hydrolysis of switchgrass harvested in different seasons and locations. Biotechnology for Biofuels, 3, 1.
Publication 2010
Ammonia Blood Vessel Carbohydrates Enzymes Glucosidase Hydrolysis Nitrogen Novozym 188 Panicum virgatum Polygalacturonase Sugars Vision
2
Structural-based Computational Screening of Enzyme Inhibitors
Cited 5 times
The following crystal structures of the target enzymes were retrieved from the protein data bank (https://www.rcsb.org/ (accessed on 1 June 2022)): AChE (PDB ID: 6O52) [57 (link)], BChE (PDB ID: 6EQP) [58 (link)], tyrosinase (PDB ID: 6QXD) [59 (link)], amylase (PDB ID: 2QMK) [60 (link)], and glucosidase (PDB ID: 7KBJ) [61 (link)]. In the absence of crystal structures of human tyrosinase and glucosidase, human sequences (UniProt IDs P14679 and P0DUB6, respectively) were used to build their homology models using these PDB structures as templates. The models were built using the ITASSER web-based tool (https://zhanggroup.org/I-TASSER/, accessed on 1 June 2022) [62 (link)] and validated using the PROCHECK server (https://www.ebi.ac.uk/thornton-srv/software/PROCHECK/, accessed on 1 June 2022) [63 (link)].
Each protein was protonated using the predicted pKa of the titratable residues at a physiological pH of 7.4 using an online server “Playmolecule proteinPrepare” (https://playmolecule.com/proteinPrepare/, accessed on 1 June 2022) [64 (link)]. The three-dimensional structure of each study ligand was retrieved from the PubChem database (https://pubchem.ncbi.nlm.nih.gov/, accessed on 1 June 2022), and its geometry was optimized using Frog2 [65 (link)].
Using Autodock Tools program (https://autodock.scripts.edu, accessed on 10 June 2022) [66 (link)], docking grid files were generated using the coordinates of the cocrystal ligand in each crystal. The details of the docking procedure have been described in our previous studies [67 (link),68 (link)]. The binding energy of the ligand poses were calculated, and protein–ligand interactions were examined using the Biovia DS Visualizer (Dassault Systèmes Biovia Software Inc, 2012, San Diego, CA, USA).
Omer H.A., Caprioli G., Abouelenein D., Mustafa A.M., Uba A.I., Ak G., Ozturk R.B., Zengin G, & Yagi S. (2022). Phenolic Profile, Antioxidant and Enzyme Inhibitory Activities of Leaves from Two Cassia and Two Senna Species. Molecules, 27(17), 5590.
Publication 2022
Amylase Enzymes Glucosidase Homo sapiens Ligands Monophenol Monooxygenase Pain physiology Proteins
3
Nitrogen Effects on Soil Enzyme Activities
Cited 5 times
We used Web of Science (http://apps.webofknowledge.com/), Google Scholar (http://scholar.google.com/), and China National Knowledge Infrastructure (www.cnki.net/) for an exhaustive search of articles published before March 2018. The keywords and phrases used for literature research were as follows: (i) “nitrogen addition,” “nitrogen amendment,” “nitrogen enrichment,” “nitrogen fertilizer,” “nitrogen elevated,” or “nitrogen deposition”; (ii) “glucosidase,” “cellobiosidase,” “xylosidase,” “peroxidase,” “phenol oxidase,” “polyphenol oxidase,” “lignin modifying enzymes,” or “cellulase”; (iii) “soil carbon”; and (iv) “terrestrial,” “soil,” or “land”.
To be included in our data set, articles had to meet several requirements. First, we only considered experiments that lasted at least 1 year. Second, control and N addition treatments had to be applied at the same experimental site; that is, the microclimate, vegetation, and soil types were similar between treatments. Third, SDs and replicates had to be reported or could be derived from the results. Fourth, details on N addition methods (rate, frequency, form, and duration) had to be provided. We identified 40 studies that met these criteria, and 9 of these studies reported soil C data from the matching studies (see Supplementary Materials and Methods and data S1).
For each study, we recorded LME activity and cellulase activity (see Supplementary Materials and Methods and table S1), site location (longitude and latitude) and climatic variables (MAP and MAT), elevation, BND, vegetation and soil types, and N addition methods (rate, duration, frequency, and form of N addition). If these data were not reported, we contacted the corresponding author for more information. Otherwise, we obtained MAT and MAP from the WorldClim database (www.worldclim.org/), BND from the Global N deposition database (http://webmap.ornl.gov/). We classified vegetation types according to the Whittaker Biome Diagram (38 ), and soil types according to the Food and Agriculture Organization taxonomy (www.fao.org/soils-portal/soil-survey/soil-classification/usda-soil-taxonomy/en). Where available, we also tabulated plant productivity, soil pH, soil C/N, microbial abundance, soil texture, and the size of the recalcitrant C pool (see Supplementary Materials and Methods and data S2 and S3). When results were presented graphically, we used Engauge Digitizer 4.1 (http://digitizer.sourceforge.net) to digitize the data.
Chen J., Luo Y., van Groenigen K.J., Hungate B.A., Cao J., Zhou X, & Wang R.W. (2018). A keystone microbial enzyme for nitrogen control of soil carbon storage. Science Advances, 4(8), eaaq1689.
Publication 2018
Biome Carbon Catechol Oxidase cellobiosidase Cellulase Climate CTSB protein, human Enzymes Food Glucosidase Lignin Microclimate Monophenol Monooxygenase Nitrogen Peroxidase Plants
4
Molecular Docking of Enzyme Inhibitors
Cited 4 times
The crystal structures of target enzymes were downloaded from the protein data bank (PDB) (https://www.rcsb.org/ accessed on 1 June 2022): human AChE (6O52) [62 (link)], BChE (6EQP) [63 (link)] and human pancreatic alpha-amylase (1B2Y) [64 (link)]. Since the crystal structures of human tyrosinase and glucosidase have not yet been elucidated, those of Priestia megaterium tyrosinase (6QXD) [65 (link)] and Mus musculus alpha-glucosidase (7KBJ) [66 (link)] were used as templates to build their human models using UniProt sequences P14679 and P0DUB6, respectively.
The details of the model construction has been described elsewhere [67 (link)]. The prepared protein structures were taken from previous work [68 (link)]. The 3D structures of selected ligands were downloaded from the PubChem database (https://pubchem.ncbi.nlm.nih.gov/ accessed on 1 June 2022) and their geometry was optimized using Frog2 [69 (link)]. The respective cocrystal ligand of each complex was used to define the docking grid box dimension and binding coordinates using AutoDockTools 1.5.6, and docking was performed using AutoDock 4.2.6 (https://autodock.scripts.edu, accessed on 1 June 2022) [70 (link)]. The details of the docking, including the Lamarckian genetic algorithm employed and the number of runs, have been described previously [71 (link),72 (link),73 (link),74 (link)]. The docking score of each ligand was calculated, and the protein–ligand interactions were visualized using Biovia Discovery Studio Visualizer (Dassault Systèmes Biovia Software Inc, 2012).
Llorent-Martínez E.J., Ruiz-Medina A., Zengin G., Ak G., Jugreet S., Mahomoodally M.F., Emre G., Orlando G., Libero M.L., N.i.l.o.f.a.r., Acquaviva A., Di Simone S.C., Menghini L., Ferrante C., Brunetti L., Recinella L., Leone S., Shariati M.A., Uba A.I, & Chiavaroli A. (2022). New Biological and Chemical Evidences of Two Lamiaceae Species (Thymbra capitata and Thymus sipyleus subsp. rosulans): In Vitro, In Silico and Ex Vivo Approaches. Molecules, 27(24), 9029.
Publication 2022
alpha-Amylase, Pancreatic alpha Glucosidase Bacillus megaterium Enzymes Glucosidase Homo sapiens Ligands Mice, House Monophenol Monooxygenase Pain Proteins Reproduction
5
Screening of Korean Medicinal Plant Extracts for α-Glucosidase Inhibition
Cited 4 times
Plant material
The dried and matured plant parts of thirty Korean medicinal herbs were obtained from “Korean Collection of Herbal Extracts” a Biotech company in Korea. A collection of voucher specimen is available with the company (Korea Collection of Herbal Extracts, 2000).
Extraction
The dried plant parts individually were chopped into small pieces and pulverized into a fine powder. The powdered plant materials (100 g, dry weight) were kept for extensive decoction in 80% methanol for 3 days at room temperature. The extracts were then concentrated using rotary vacuum evaporator at 20-30°C to obtain the dried crude extracts.
Reagents
α-Glucosidase (from Saccharomyces cerevisiae type I) and 4-nitrophenyl α-D-glucopyranoside were purchased from Sigma-Aldrich (St. Louis, MO, USA). Other commercially available reagents and solvents were used as received.
α-Glucosidase assay
The enzyme inhibition activity for α-glucosidase was evaluated according to the method previously reported by Shibano et al. (7 (link)) with minor modifications. The reaction mixture consisted of 50 μL of 0.1 M phosphate buffer (with pH of 7.0), 25 μL of 0.5 mM 4-nitrophenyl α-D-glucopyranoside (dissolved in 0.1 M phosphate buffer, with pH of 7.0), 10 μL of test sample and 25 μL of α-glucosidase solution (a stock solution of 1 mg/mL in 0.01 M phosphate buffer, with pH of 7.0 was diluted to 0.1 Unit/mL with the same buffer, with pH of 7.0 just before assay). This reaction mixture was then incubated at 37°C for 30 min. Then, the reaction was terminated by the addition of 100 μL of 0.2 M sodium carbonate solution. The enzymatic hydrolysis of substrate was monitored by the amount of p-nitrophenol released in the reaction mixture at 410 nm using microplate reader. Individual blanks were prepared for correcting the background absorbance, where the enzymes were replaced with buffer. Controls were conducted in an identical manner replacing the plant extracts with methanol. 1, 2, 3, 4, 6-penta-O-galloyl-β-D-glucose was used as positive control. All experiments were carried out in triplicates. The inhibition percentage of α-glucosidase was assessed by the following formula:
I α-glucosidase% = 100 X (ΔAControl - ΔASample) / ΔAControlΔAControl = ΔATest - ΔABlankΔASample = ΔATest - ΔABlankStatistical analyses
All assays were performed at least three times with triplicate samples. All results are expressed as mean ± SD. IC50 values were only determined for the plant extracts with inhibition ≥ 50% at 5 mg/mL by plotting a percent inhibition versus concentration curve, in which the concentration of sample required for 50% inhibition was determined and expressed as IC50 value.
Sancheti S., Sancheti S., Lee S.H., Lee J.E, & Seo S.Y. (2011). Screening of Korean Medicinal Plant Extracts for α-Glucosidase Inhibitory Activities. Iranian Journal of Pharmaceutical Research : IJPR, 10(2), 261-264.
Publication 2011
4-nitrophenyl alpha Glucosidase Biological Assay Buffers Complex Extracts enzyme activity Enzymes Exhaling Glucose Glucosidase Hydrolysis Koreans Medicinal Herbs Methanol Nitrophenols Phosphates Plants Psychological Inhibition Saccharomyces cerevisiae sodium carbonate Solvents Specimen Collection Tetranitrate, Pentaerythritol Vacuum

Most recents protocols related to «Glucosidase»

1
In Vitro SGSH-Fc Fusion Protein Activity Assay
Not available on PMC !

Example 8

This example provides an alternative in vitro activity assay for SGSH-Fc fusion proteins. The assay is adapted from Karpova et al., J. Inherit. Metab. Dis., 19:278-285 (1996).

The standard reaction mixtures consisted of 10-15 μg of protein and 20 μL MU-α-GlcNS (5 or 10 mmol/L, respectively) in Michaelis' barbital sodium acetate buffer, pH 6.5 (29 mmol/L sodium barbital, 29 mmol/L sodium acetate, 0.68% (w/v) NaCl, 0.02% (w/v) sodium azide; adjusted to pH 6.5 with HCl) and the reaction mixtures were incubated for 17 h at 37° C. MU-α-GcNS is available from Moscerdam Substrates. After the first incubation, 6 μl twice-concentrated McIlvain's phosphate/citrate buffer, pH 6.7, containing 0.02% sodium azide and 10 μl (0.1 U) yeast a-glucosidase (Sigma) in water were added and a second incubation of 24 h at 37° C. was carried out. Long incubations at 37° C. (17-24 h) were carried out in 96-well plates which were sealed airtight with broad sticky tape, limiting evaporation to <15%. Next, 200 μL 0.5 mol/L Na2CO3/NaHCO3, pH 10.7, was added, and the fluorescence of the released 4-methylumbelliferone (MU) was measured on a Fluoroskan (Titertek) fluorimeter. Protein was determined as described previously (van Diggelen et al., Clin. Chim. Acta., 187:131-139 (1990)).

US11866742B2. Fusion proteins comprising enzyme replacement therapy enzymes (2024-01-09). Denali Therapeutics Inc. [US]. Inventors: Anastasia Henry [US], Mihalis S. Kariolis [US], Cathal S. Mahon [US], Adam P. Silverman [US], Ankita Srivastava [US], Julie Ullman [US].
Patent 2024
Barbital Bicarbonate, Sodium Biological Assay Buffers Citrate Fluorescence Glucosidase Hymecromone Phosphates Proteins Sodium Sodium Acetate Sodium Azide Sodium Chloride Yeast, Dried
2
Goat Meat Extract's α-Glucosidase Inhibition
To measure the degree to which goat meat extract inhibits the digestion and
absorption of monosaccharides, the α-glucosidase enzyme reaction of
the extracts was evaluated according to the methods developed by Kim et al. (2021) (link) and Si et al. (2010) (link). Briefly, 50-μL
aliquots of HE, HWE, and EE were mixed with 50 μL of
α-glucosidase (Sigma-Aldrich, St. Louis, MO, USA) in 50 μL of
200 mM potassium phosphate buffer (pH 6.5; Sigma-Aldrich). The mixtures were
incubated at 37°C for 10 min before adding 3 mM p-nitrophenyl
α-D-glucopyranoside (Thermo Fisher Scientific, Waltham, MA, USA) as a
substrate and continuing the reaction at 37°C for 10 min. The
reaction was stopped by adding 750 μL of 0.1 M
Na2CO3 and centrifuged at 12,000×g and
4°C for 10 min. The supernatant was transferred to a 96-well
microtiter plate, and the absorbance at 405 nm was measured with a
microplate spectrophotometer (Epoch, BioTek, Winooski, VT, USA) to measure
the p-nitrophenol released from the substrate. α-Glucosidase
inhibitory activity was calculated as follows:
where A is the absorbance of sample, and B is the absorbance of control.
Kang J., Kim S., Lee Y., Oh J, & Yoon Y. (2023). Effects on Goat Meat Extracts on α-Glucosidase Inhibitory Activity, Expression of Bcl-2-Associated X (BAX), p53, and p21 in Cell Line and Expression of Atrogin-1, Muscle Atrophy F-Box (MAFbx), Muscle RING-Finger Protein-1 (MuRF-1), and Myosin Heavy Chain-7 (MYH-7) in C2C12 Myoblsts. Food Science of Animal Resources, 43(2), 359-373.
Publication 2023
alpha Glucosidase Buffers Cardiac Arrest Digestion Enzymes EPOCH protocol Glucosidase Goat Meat Monosaccharides Nitrophenols potassium phosphate
3
Characterizing Soil Properties and Enzymes
After the harvest of potatoes, a total of 15 bulk soil samples (three treatments × five replicates) were collected with a 2-cm-diameter auger on 14 October 2021. For the bulk soils, 10 topsoil samples (0–20 cm) were randomly collected from each replicate plot and combined into a single sample (a replicate). Each composite sample (a replicate) was divided into two parts, where the first part was stored at –80°C before DNA extraction, and the second part was air-dried at room temperature for determining soil chemical properties [pH, total nitrogen (TN), alkali hydrolyzable nitrogen (AN), organic matter (SOM), total phosphorus (TP), and available phosphorus (AP)], enzyme activities [β-1,4-N-acetyl-glucosaminidase (NAG), β-1,4-glucosidase (β-GC), and alkaline phosphatase (ALP)].
Li Q.M., Zhang D., Zhang J.Z., Zhou Z.J., Pan Y., Yang Z.H., Zhu J.H., Liu Y.H, & Zhang L.F. (2023). Crop rotations increased soil ecosystem multifunctionality by improving keystone taxa and soil properties in potatoes. Frontiers in Microbiology, 14, 1034761.
Publication 2023
Alkalies chemical properties Dietary Fiber DNA Replication enzyme activity Glucosaminidases Glucosidase Nitrogen Phosphorus Solanum tuberosum
4
Enzymatic Saccharification of Atriplex crassifolia
The enzymatic saccharification of pre-treated biomass Atriplex crassifolia was carried out by adding 0.25 g of pre-treated substrate in a screw-capped reagent bottle. For enzymatic hydrolysis, Endo-1,4- β -glucanase (200 U) was added to both experimental and control (without substrate) reagent bottles. Both the reagent bottles were incubated at 75°C in a shaking water bath with rpm set at 50 for a period of 2 h. Next, Exo-1,4- β -glucanase (400 U) was added to the same reagent bottles and after incubating the mixture for another 2 h, β -1,4-glucosidase (1000 U) was added to both the reagent bottles. The samples (1 mL) were withdrawn after regular intervals of 1 h to note the release of reducing sugars via DNS method, using straight line equation obtained from the standard curve. The percentage saccharification was determined by using Vallander and Eriksson (1987) (link) proposed equation; % Saccharification=R.S×V×F1M×F2×100
Nawaz A., Qadoos K., Haq I.U., Feng Y., Mukhtar H., Huang R, & Jiang K. (2023). Effect of pretreatment strategies on halophyte Atriplex crassifolia to improve saccharification using thermostable cellulases. Frontiers in Bioengineering and Biotechnology, 11, 1135424.
Publication 2023
Atriplex Bath endometriosis protein-1 Enzymes Glucosidase Hydrolysis Sugars
5
Sequential Cellulase Addition for Halophyte Biomass Hydrolysis
In sequential addition of cellulases, beginning with the addition of Endo-1,4- β -glucanase (200 U) to the screw-capped reagent bottle enclosing the pre-treated substrate i.e., halophyte Atriplex crassifolia (0.25 g), the reaction was carried out in a shaking water bath set at 75°C and 50 rpm. After 2 h of incubation time, Exo-1,4- β -glucanase (400 U) was added to the same reagent bottle for another 2 h. Next, the cellulase i.e., β -1,4-glucosidase was added to the same reagent bottle and incubated for a period of 2 h. In this way, in sequential addition of cellulases, each cellulase was added one after the other and each was incubated for a period of 2 h.
Nawaz A., Qadoos K., Haq I.U., Feng Y., Mukhtar H., Huang R, & Jiang K. (2023). Effect of pretreatment strategies on halophyte Atriplex crassifolia to improve saccharification using thermostable cellulases. Frontiers in Bioengineering and Biotechnology, 11, 1135424.
Publication 2023
Atriplex Bath Cellulase Cellulases Endoglucanase E endometriosis protein-1 Glucosidase Halophytes

Top products related to «Glucosidase»

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Q sepharose high performance column by GE Healthcare
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The Q SEPHAROSE® High Performance column is a versatile ion exchange chromatography medium designed for high-resolution separation and purification of biomolecules. It features a strong anion exchange resin with a high dynamic binding capacity and excellent chemical and physical stability, making it suitable for a wide range of applications in the biopharmaceutical and research industries.
2
α amylase by Merck Group
Sourced in United States, Germany, China, Italy, Poland, United Kingdom, India, France, Switzerland, Singapore, Spain, Sao Tome and Principe, Canada, Sweden, Australia
α-amylase is an enzyme commonly used in laboratory settings. It functions by catalyzing the hydrolysis of starch, glycogen, and related polysaccharides into smaller carbohydrate units such as maltose and glucose.
3
Acarbose by Merck Group
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Acarbose is a prescription medication used to help manage blood sugar levels in individuals with diabetes. It works by slowing the breakdown and absorption of carbohydrates in the digestive system, which can help control postprandial (after-meal) blood glucose levels. Acarbose is an enzyme inhibitor that targets alpha-glucosidase, an enzyme responsible for breaking down complex carbohydrates.
4
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Pepsin is a proteolytic enzyme produced by the chief cells in the stomach lining. It functions to break down proteins into smaller peptides during the digestive process.
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Cellic ctec2 by Novozymes
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Cellic® CTec2 is a commercial enzyme product developed by Novozymes. It is a cellulase enzyme complex designed for the hydrolysis of cellulosic biomass. The product contains a blend of cellulolytic enzymes that work synergistically to break down cellulose into fermentable sugars.
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α glucosidase by Merck Group
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α-glucosidase is an enzyme that catalyzes the hydrolysis of α-1,4-glucosidic linkages in oligosaccharides and disaccharides. It is commonly used in laboratory settings for various analytical and research applications.
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2 2 diphenyl 1 picrylhydrazyl (dpph) by Merck Group
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DPPH is a chemical compound used as a free radical scavenger in various analytical techniques. It is commonly used to assess the antioxidant activity of substances. The core function of DPPH is to serve as a stable free radical that can be reduced, resulting in a color change that can be measured spectrophotometrically.
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More about "Glucosidase"

Glucosidases are a class of enzymes that play a crucial role in the hydrolysis of glucosidic bonds, breaking down complex carbohydrates into simpler sugars.
These versatile enzymes are found in a wide range of organisms, including microbes, plants, and animals, and are essential for various biological processes such as digestion, energy production, and glycosylation.
Understanding the function and regulation of glucosidases is of great importance in several fields, including biotechnology, medicine, and agriculture.
Researchers can leverage the AI-driven platform of PubCompare.ai to streamline their glucosidase research, locate the best protocols from literature, preprints, and patents, and enhance the reproducibility and accuracy of their experiments.
Glucosidases can be further categorized into α-glucosidases and β-glucosidases, based on the stereospecificity of the glycosidic bond they target.
These enzymes have diverse applications, such as in the production of biofuels, the development of treatments for metabolic disorders, and the optimization of crop yields.
To explore glucosidase research in depth, researchers can utilize techniques like Q SEPHAROSE® High Performance column chromatography, which is commonly used for the purification and characterization of these enzymes.
Additionally, the use of α-amylase, Acarbose, and Pepsin can provide insights into the interactions and inhibition mechanisms of glucosidases.
Cutting-edge tools like Cellic® CTec2, SpectraMax M5, and Synergy H1 can further enhance the analysis and optimization of glucosidase activities, while DPPH assays can be employed to assess the antioxidant properties of these enzymes.
By leveraging the comprehensive resources and AI-driven capabilities of PubCompare.ai, researchers can streamline their glucosidase research, access the best protocols, and improve the reproducibility and accuracy of their findings, ultimately advancing our understanding and applications of these versatile enzymes.