Enzyme
Microbial neutral proteinase is a zinc-containing metalloproteinase mainly produced by Bacillus and fungi. Its catalytic activity is highly dependent on divalent cations, and it remains active within the pH range of 5-8. Microbial neutral proteinase can specifically cleave peptide bonds within polypeptide chains, thereby degrading macromolecular proteins into small peptides or amino acids. It can be applied in various industrial fields including food processing, brewing, detergents, and light industry.
Recombinant enterokinase (rEK) is a serine protease and functions as the physiological activator of trypsinogen. Recombinant enterokinase plays a role of turning trypsinogen to its active form trypsin.
Phospholipase A2 (PLA2) is a calcium-dependent, heat-stable enzyme that catalyzes the hydrolysis of glycerophospholipids at the sn-2 position of cellular membranes, thereby releasing Arachidonic Acid (AA) (HY-109590). Phospholipase A2 is a key mediator in the biosynthesis of pro-inflammatory lipid mediators, critically involved in inflammatory processes. Phospholipase A2 can be used for cardiovascular and inflammatory diseases research.
TLCK-treated Chymotrypsin is a serine protease. Chymotrypsin cleaves protein chains at the carboxyl side of aromatic amino acids. TLCK treated to inactivate residual tryspin activity.
3-Hydroxybutyrate dehydrogenase (3-HBDH), a mitochondrial enzyme, is a key enzyme in the ketone body metabolism pathway. 3-Hydroxybutyrate dehydrogenase is the last enzyme for ketone synthesis in the liver and the first enzyme for ketone breakdown in extracellular tissues. The absence of 3-Hydroxybutyrate dehydrogenase leads to the inhibition of fatty acid oxidation in the liver during fasting in mice, resulting in lipid accumulation and the development of fatty liver.
Invertase, baker's yeast (S. cerevisiae) is a major enzyme present in plants and microorganisms, is often used in biochemical studies. Invertase catalyzes the hydrolysis of the disaccharide sucrose into glucose and fructose.
Endo-1,4-β-mannanase is an important catalyst that randomly cleaves the β-1,4-linkages in the main chain of mannan, releasing short-chain β-1,4-mannan and mannose. The catalytic activity of Endo-1,4-β-mannanase toward locust bean gum is enhanced by Mn2+, Co2+, Ca2+, Ba2+, Triton X-100, sodium azide and N-ethylmaleimide, completely inhibited by Hg2+ and N-bromosuccinimide, and partially inhibited by EDTA and Cu2+. Endo-1,4-β-mannanase can be used in studies related to plant hemicellulose degradation, biomass saccharification, elimination of anti-nutritional factors in feed, and manno-oligosaccharide prebiotics.
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.
Glyceraldehyde phosphate dehydrogenase (EC 1.2.1.12) is the target of anti-thymocyte and anti-apoptotic agents. Glyceraldehyde phosphate dehydrogenase catalyzes the chain oxidation of reduced nicotinamide adenine dinucleotide by perhydroxyl radicals.
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).
Acyl coenzyme A synthetase (ACS), namely acetyl coenzyme A synthetase, is often used in biochemical research. Acyl coenzyme A synthetase can catalyze the activation of fatty acids by coenzyme A through a two-step thioesterification reaction to produce acyl coenzyme A, and then participate in a variety of anabolic and catabolic lipid metabolism pathways, and participate in the TCA cycle in aerobic respiration.
Butyrylcholinesterase (BCHE), Horse Serum (BCHE, BuChE, PCHE, pseudocholinesterase, plasma cholinesterase, Acylcholine acyl-hydrolase, Choline esterase, butyryl) is a biological material or organic compound that can be used in life science research.
Deoxyribonuclease II (DNase II) is an endonuclease that hydrolyzes the phosphodiester bonds of deoxyribonucleotides in native and denatured DNA, producing 3' phosphate and 5'-hydroxyl termini. Deoxyribonuclease II works best at acidic pH and is commonly used in biochemical research.
Amyloglucosidase, Aspergillus niger (Amyloglucosidase, Aspergillus niger) is a starch-hydrolyzing enzyme with high catalytic efficiency towards soluble starch and raw starch. Amyloglucosidase, Aspergillus niger hydrolyzes α-1,4 and α-1,6 glycosidic linkages in starch and similar substrates, and primarily releases β-glucose molecules from the non-reducing ends. Amyloglucosidase, Aspergillus niger participates in glycogen metabolism and is associated with type II glycogen storage disease. Amyloglucosidase, Aspergillus niger converts starch into glucose, and is applicable to the industrial production of high-fructose syrup, ethanol and other fermented products.
Alkaline Phosphatase (Apase), Calf intestinal is an alkaline phosphatase from Calf intestinal, and is one of the most active alkaline phosphatases. Alkaline Phosphatase, Calf intestinal is an orally active membrane-bound glycoprotein that catalyzes the hydrolysis of phosphate monoesters at alkaline pH. Alkaline Phosphatase, Calf intestinal reduces myeloperoxidase activity and bacterial translocation. Alkaline Phosphatase, Calf intestinal improves survival rate of mice infected with E. coli. Alkaline Phosphatase, Calf intestinal improves TNBS-induced colon inflammation.
Protocatechuate 3,4-dioxygenase is a dioxygenase. Protocatechuate 3,4-dioxygenase belongs to the non-heme iron dioxygenase class. Protocatechuate 3,4-dioxygenase catalyzes the cleavage of the aromatic ring of 3,4-dihydroxybenzoate, attaching two atoms of molecular oxygen to the compound to generate β-carboxy-cis,cis-muconate. Protocatechuate 3,4-dioxygenase is a key enzyme in the β-ketoadipic acid pathway. It is found in marine bacteria associated with Roseobacter. Protocatechuate 3,4-dioxygenase can be isolated from Pseudomonas aeruginosa.
Creatininase, Microorganism (Creatinine amidohydrolase; CAH), namely creatinine amidohydrolase, from Pseudomonas putida, is a homohexameric enzyme commonly used in biochemical research. Creatininase acts on carbon-nitrogen bonds other than peptide bonds, and can catalyze the hydrolysis of creatinine to creatine, which can then be metabolized by creatinase to urea and sarcosine.
