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Targeted therapy! The Capetin Prize winning "Click Chemistry" can be used like this!Targeted therapy! The Nobel Prize winning "Click Chemistry" can be used like this!2025-02-06
80 Results for "
glycoside hydrolase
" in MedChemExpress (MCE) Product Catalog:
Products (80)
80 Results for "glycoside hydrolase" in MCE Product Catalog:
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Miglitol (BAY-m1099) is an orally active antidiabetic compound that inhibits the breakdown of glycoconjugates into glucose. Miglitol inhibits glycoside hydrolase enzymes called α-glucosidases. Miglitol inhibits oxidative stress-induced apoptosis and mitochondrial ROS over-production in endothelial cells by enhancement of AMP-activated protein kinase. Dietary supplementation with Miglitol from pre-onset stage in OLETF rats delays the onset and development of diabetes and preserves the insulin secretory function of pancreatic islets .
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β-Glucosidase, almond is the rate-limiting enzyme in cellulose degradation. β-Glucosidase is a major group among glycoside hydrolases. β-Glucosidase is involved in the degradation of cellulose in soils and has potential for monitoring soil quality .
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Beta-glucuronidase (bovine liver) is a glycoside hydrolase that hydrolyzes β-glucuronic acid and sulfate esters in urine and other biological fluids, thereby releasing β-glucuronides. Beta-glucuronidase (bovine liver) cannot effectively hydrolyze Estriol glucuronide. Beta-glucuronidase (bovine liver) can be used in studies related to systemic gangliosidosis .
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β-Galactosidase, E. coli (EC 3.2.1.23; GAL) is a glycoside hydrolase that hydrolyzes the β-glycosidic bonds formed between galactose and its organic moieties. β-Galactosidase, E. coli can hydrolyze lactose to form glucose and galactose, and enter glycolysis; it can also catalyze the transgalactosylation of lactose into allolactose; allolactose can be cracked into monosaccharides .
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Hemicellulase is a hemicellulose-targeting hydrolase that breaks down the binding of glucose and polymers to water molecules present in plant fibers. Hemicellulase specifically degrades hemicellulose (such as xylan and mannan) in plant cell walls by hydrolyzing β-1,4-xylosidic bonds and ester bonds (such as acetyl and ferulic acid ester bonds). Hemicellulase relies on the synergistic action of the glycoside hydrolase (GH) and carbohydrate esterase (CE) families to achieve efficient hydrolysis through acid-base catalysis (such as Glu/Asp residues) and substrate binding pockets. Hemicellulase can be used in the food industry (such as improving bread texture)， biofuel production (lignocellulose pretreatment) and paper industry (biobleaching) .
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Endo-1,4-β-xylanase (Xylanase) is an arabinoxylan (AX) degrading enzyme and a glycoside hydrolase, is often used in biochemical studies. Endo-1,4-β-xylanase cleaves the β-xylosidic bond between two d-xylopyranosyl residues linked in β-(1,4) .
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Pullulanase (R-enzyme) is a key starch debranching enzyme that specifically hydrolyzes α-1,6-glycosidic linkages in polysaccharides such as amylopectin and pullulan, facilitating the efficient degradation of starch into fermentable sugars .
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β1-3 Galactosidase is a GH42 exoglycosidase that specifically hydrolyzes terminal β1-3-linked galactose. β1-3 Galactosidase uses Glu164 as the acid/base catalyst and Glu324 as the catalytic nucleophile to hydrolyze β1-3 galactosidic linkages. β1-3 Galactosidase can be used for research on galactoside metabolism .
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Dextranase, Trichoderma reesei belongs to glycoside hydrolase family 49. It catalyzes the hydrolysis of α-1,6-glycosidic linkages in dextran via a single-displacement reaction, ultimately releasing shorter isomaltooligosaccharides. Dextranase, Trichoderma reesei reduces the molecular size of dextran, inhibits the formation of insoluble dextran and dental plaque, and decreases the viscosity of dextran-contaminated sugar juice. Dextranase, Trichoderma reesei can be used in relevant research in fields such as chemical production, including beer manufacturing, feed additives, and toothpaste formulations .
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α-Galactosidase, Aspergillus niger (EC 3.2.1.22), that is, α-galactosidase, is a glycoside hydrolase that widely exists in animals, plants and microorganisms, and is often used in biochemical research. α-Galactosidase catalyzes the hydrolysis of α-1,6-linked terminal galactose residues, including galactooligosaccharides, galactomannans, and galactolipids. Catalyzes many catabolic processes including cleavage of glycoproteins, glycolipids and polysaccharides .
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α-L-Arabinofuranosidase is a kind of glycoside hydrolase. It hydrolyzes the non-reducing ends of α-L-arabinofuranosyl residues to form the side chains of arabinoxylan, arabinogalactan and arabinan .
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Maltose phosphorylase is a dimerase which catalyzes the transformation of maltose and inorganic phosphate into β-D-glucose-1-phosphate and glucose. Maltose phosphorylases have been classified in family 65 of the glycoside hydrolases .
Cat. No.: HY-W039915
CAS No.: 48149-72-0
Cat. No.: HY-E70104
CAS No.: 37288-35-0
Synonyms: α-L-Rhamnosidase
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α-Rhamnosidase (α-L-Rhamnosidase) is a kind of glycoside hydrolase. α-Rhamnosidase exhibits activity against Naringin (HY-N0153), 4-NRP, flavonoid glycosides and flavanone rhamnosides, and can hydrolyze the corresponding glycosidic bonds to release L-Rhamnose (Rhamnose) (HY-N1420) and other products. α-Rhamnosidase promotes the release of total flavonoids, ginkgolides and aroma components from ginkgo tea, while also enhancing the free radical scavenging capacity of the leachate, inhibiting inflammatory cell activation and increasing its cytotoxicity against tumor cells. α-Rhamnosidase can be used in research related to bacillary dysentery and cancer .
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α-Glucosidase, rice is a GH31 glycoside hydrolase in rice seeds, with high selectivity for α-1,4-glycosidic bonds. α-Glucosidase, rice can be inhibited by rice husk extracts (IC50 = 1.25 μg/mL) and steroidal components (IC50 = 1.83 μg/mL). α-Glucosidase, rice exists in two major isoforms, among which isoform II is more sensitive to inhibitors. α-Glucosidase, rice can directly bind to and degrade starch granules in rice seeds. α-Glucosidase, rice can form ONG2-I and ONG2-II via post-translational proteolysis. α-Glucosidase, rice can be used in type 2 diabetes research .
Cat. No.: HY-E70013A
CAS No.: 37288-51-0
Synonyms: EC 3.2.1.73
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Licheninase (EC 3.2.1.73) is a glycoside hydrolase that acts on the β-glucan cell walls of cereals, fungal and seaweeds. Licheninase specifically hydrolyzes the β(1→4) linkages in mixed-linkage β(1→3)/β(1→4)-glucans. Licheninase promotes cellulose degradation .
Cat. No.: HY-132177H
CAS No.: 9037-65-4
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exo-α-Fucosidase, Bacteroides fragilis (EC 3.2.1.51) is a glycoside hydrolase that would release free fucose .
Cat. No.: HY-N8279
CAS No.: 62213-14-3
Synonyms: Endo-β-1,3-1,4-glucanase
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β-1,3-1,4-glucanase (Endo-β-1,3-1,4-glucanase) is a glycoside hydrolase family 16 enzyme (some members belong to subfamily 25). β-1,3-1,4-glucanase shows high substrate specificity toward mixed‑linked β‑glucans and cleaves β‑1,4 glycosidic bonds adjacent to β‑1,3 linkages in an endo‑type pattern. β-1,3-1,4-glucanase can be used in industrial enzyme applications and monogastric animal feed supplementation .
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β-Galactosidase, Sweet almond is a glycoside hydrolase that hydrolyzes the β-glycosidic bonds formed between galactose and its organic moieties. β-Galactosidase, Sweet almond can hydrolyze lactose to form glucose and galactose, and enter glycolysis; it can also catalyze the transgalactosylation of lactose into allolactose; allolactose can be cracked into monosaccharides .
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β1-3,6 Galactosidase, Xanthomonas manihotis is an exoglycosidase that catalyzes the hydrolysis of terminal β(1-3)- and β(1-6)-linked galactose residues .
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Protocols
Targeted therapy! The Capetin Prize winning "Click Chemistry" can be used like this!Targeted therapy! The Nobel Prize winning "Click Chemistry" can be used like this!A suitable model is crucial in drug screening experiments. Organs can mimic the three-dimensional functional structure of internal organs, have similar spatial organization to corresponding organs, maintain some key characteristics, and reproduce some physiological functions. They are widely used for modeling and personalized drug screening physiological functions.2025-02-06
