Extract

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.

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).

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.

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.

Driselase, Basidiomycetes sp, a complex mixt. of wall-digesting enzymes, is a specific commercial fungal protoplasting enzyme preparation. Driselase can be used in combination with lyase to promote protoplast formation in fungi. Driselase is by far the most potent of the enzymes tested for polysaccharide digestion and greatly increases both tensile and indentation compliances, yet it does not induce wall creep, even after 6 h of digestion.

Collagenase (Type A, animal free) is a proteolytic enzyme targeting collagen, capable of releasing corneal endothelial cells (CECs) without damaging cell junctions.

Aspartate aminotransferase (EC 2.6.1.1), porcine heart is a metabolic regulator with the highest activity in the heart, liver and skeletal muscle. Aspartate aminotransferase, porcine heart comprises two isozymes: the cytoplasmic form (AST1) and the mitochondrial form (AST2). By catalyzing reversible transamination reactions between oxaloacetate, L-glutamate and other substances, it is deeply involved in key physiological processes such as amino acid metabolism, the tricarboxylic acid cycle and neurotransmitter synthesis. Aspartate aminotransferase, porcine heart also provides substrate support for the synthesis of urea and purines/pyrimidines. Aspartate aminotransferase, porcine heart is a serum marker reflecting cardiac and hepatic injury, and its abnormal levels are also closely associated with myocardial infarction, cardiovascular diseases and various cancers.

Formate dehydrogenase is a class of oxidoreductases widely distributed in bacteria, fungi, plants and animals. Formate dehydrogenase catalyzes the reversible conversion between formic acid and carbon dioxide, accompanied by redox reactions of the coenzyme NAD⁺/NADH or other electron carriers.

Pyruvate Kinase, Microorganism (PK) is a glycolytic enzyme that catalyzes the conversion of phosphoenolpyruvate and ADP to pyruvate and ATP.

Formaldehyde dehydrogenase is a widely occuring enzyme that can catalyze S-hydroxymethylglutathione in the presence of NAD. Formaldehyde dehydrogenase detoxifies formaldehyde within cells through capturing and limiting it from reaching a toxic level. Formaldehyde dehydrogenase can be studied in research on M. tuberculosis.

Micrococcal nuclease is a secreted nuclease from Staphylococcus aureus. It digests single-stranded and double-stranded DNA (ssDNA and dsDNA) as well as RNA, cleaves oligonucleotide linkers with T-T sites, and cuts neutrophil extracellular traps and biofilm extracellular DNA into mononucleotides and dinucleotides. Micrococcal nuclease stimulates the formation of Staphylococcus aureus biofilms and mediates immune evasion. It triggers on-demand release of antibiotics from hydrogel coatings, prolongs the formation of neutrophil extracellular traps, and promotes the dissemination and survival of MRSA during infection. Micrococcal nuclease is applicable to research and characterization related to Staphylococcus aureus infection.

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.

5α-reductase, Rat (Sprague-Dawley) Liver is an enzyme involved in steroid metabolism and participates in the androgen metabolic pathway. 5α-reductase, Rat (Sprague-Dawley) Liver catalyzes the conversion of testosterone to 5α-dihydrotestosterone (DHT). DHT plays important roles in the development of male sex organs, hair growth, prostate function, and other aspects.

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.

Alanine aminotransferase, Porcine heart is a pyridoxal enzyme that catalyzes the reversible interconversion of L-alanine and 2-oxoglutalate to pyruvate and L-glutamate.

Uricase, Microorganism (Uox, Microorganism) is a uricase (urate oxidase) derived from Microorganism. Uricase, Microorganism converts uric acid into allantoin. The absence of Uricase in mammals causes kidney diseases resulting from uric acid accumulation. Uricase, Microorganism can be used for research on chronic refractory gout and hyperuricemia.