Enzimas em Proteínas Recombinantes

<p>Acetylcholinesterase is an enzyme that breaks down acetylcholine</p>

<p>Endoproteinase Glu-C (Glutamyl endopeptidase, V8 protease, GluV8, EC 3.4.21.19) is a protease that hydrolyzes peptide bonds at the carboxylic side of either exclusively Glu, or Glu and Asp residues, depending on the buffer conditions. One unit of endoproteinase Glu-C will generate 1.0 μmole of p-nitroaniline from Z-Phe-Leu-Glu-pNA peptide mimic substrate per minute at pH 7.8 and 25 °C. Z-Phe-Leu-Glu-pNA substrate is available here.molecular weight ~ 27000.</p>

<p>Glucosidases are enzymes belonging to the family of oxidoreductases. They catalyse the hydrolysis of starches to simple sugars. Glucosidase is widely used in the food, carbohydrate and biofuels industries. In recent years, its applicability has expanded to biotechnology for its potential application in bioenzymatic fuel cells.</p>

Carboxypeptidase Y (EC 3.4.16.1) is an exopeptidase enzyme. It hydrolyzes peptide bonds of C-terminal residues and it remains active in the presence of urea at low to moderate concentrations. One unit of the Carboxypeptidase Y will hydrolyze 1.0 μmole of a chromogenic peptide substrate, releasing C-terminal alanine and generating a light-absorbing product.

Lyticase is a lysing enzyme that is designed to lyse cells in a biological sample. It contains an optimized wild-type guanine nucleotide-binding protein and has been shown to have high enzyme activities. Lyticase has also been shown to be active against opportunistic fungal strains, such as Candida glabrata, by disrupting their cell membranes. Lyticase is classified as a signal peptide with nuclear DNA, which allows it to be used in wastewater treatment applications. The enzyme can also be used for the analysis of the Toll-like receptor (TLR) response of microbes due to its electrochemical impedance spectroscopy properties.

<p>E. coli recombinant sialic acid aldolase (EC 4.1.3.3) from Pasteurella multocida.  One unit is defined as the amount of enzyme that catalyses the formation of 1 umol Neu5Ac from ManNAc and Pyruvate per minute at 37 ℃.Activity: 9U/mg</p>

<p>Butyrylcholinesterase is an enzyme made in the liver and found mainly in blood plasma. Butyrylcholinesterase (EC 3.1.1.8), also known as BChE or BuChE, is a nonspecific cholinesterase enzyme that hydrolyses choline-based esters. One unit of Butyrylcholinesterase will hydrolyze 1.0 μmole of butyrylcholine to choline and butyrate per minute at pH 8.0 and 37 °C.</p>

Endo-β-1,4-Mannanase (other names Mannan endo-1,4-β-mannosidase, endo-β-1,4-mannase, β-mannanase B, β-1, 4-mannan 4-mannanohydrolase, endo-β-mannanase, β-D-mannanase, 1,4-β-D-mannan mannanohydrolase; EC 3.2.1.78) is an enzyme, catalyzing the hydrolysis of -1, 4-mannosidic linkages in mannans, glucomannans and galactomannans. One unit of Endo-β-1,4-Mannanase will release 1.0 µmole of mannose reducing-sugar per minute from a 3mg/ml mannan solution at pH 5.5 and 37degC.  Expressed in U/g.

α-Glucosidase is a glycoside hydrolase enzyme that hydrolyzes α-1,4-linked D-glucose residues to produce α-D-glucose. This enzyme has been isolated from Bacillus stearothermophilus and is used as an industrial catalyst in the production of glucose syrups.  One Unit of α-Glucosidase will release 1.0 µmole of p-nitrophenol from the chromogenic substrate mimic 4-nitrophenyl α-D-glucopyranoside per minute under optimum conditions.

beta-Galactosidase (EC 3.2.1.23, shortly beta-Gal, also know as lactase) catalyses the hydrolysis of beta-d-galactoside in the presence of water to galactose and alcohol, or lactose into glucose and galactose. beta-Gal has a molecular weight of 540,000 and is composed of four identical subunits of MW 135,000, each with an independent active site. The enzyme has divalent metals as cofactors, with chelated Mg2+ ions required to maintain active site conformation. The molecule contains numerous sulfhydryl groups and is glycosylated.

<p>Superoxide dismutase is an enzyme that catalyzes the conversion of harmful superoxide into hydrogen peroxide and oxygen.</p>

selectively deamidates gluten peptides, which results in strongly enhanced T cell-stimulatory activity.  It has also been used in a study to improve quantifiable assays to fully characterize the role of transglutaminase in diseases such as Huntington′s disease and Alzheimer′s disease.

Lysozyme is a bacteriolytic enzyme, which is primarily derived from hen egg whites. It functions by hydrolyzing the β-1,4-glycosidic linkages in the peptidoglycan layer of bacterial cell walls, particularly in Gram-positive bacteria. This enzymatic activity results in the lysis and subsequent death of the bacterial cells, providing a potent antimicrobial effect.

75u/mg - Glyceraldehyde 3-phosphate dehydrogenase (GAPDH; EC 1.2.1.12) is an enzyme that catalyzes the following reaction:  glyceraldehyde 3-phosphate + NAD+ + Pi ⇌ glycerate 1,3-bisphosphate + NADH + H+  One unit of GAPDH will convert 1.0 μmole of glyceraldehyde 3-phosphate into glycerate 1,3-bisphosphate per minute at pH 8.5 and 37 °C in the presence of NAD+ and phosphate. NAD+ is available here.

<p>Invertase is an enzyme that catalyzes the hydrolysis of sucrose to glucose and fructose and can be found in plants and microorganisms</p>

<p>Protease enzymes break down proteins and are essential for many biological processes, including digestion, cellular regulation and blood clotting. They are also used in many industrial and biotechnological applications for example in food processing and in detergents.</p>

<p>E. coli recombinant α-2,6 sialyltransferase from Neisseria meningitidis. One unit is defined as the amount of enzyme that catalyses the formation of 1 μmol CMP-Neu5Ac from CTP and Neu5Ac per minute at 37 ºC.Activity: 100U/mg</p>

Myokinase (Adenylate kinase, EC 2.7.4.3) catalyzes interconversion between ATP, ADP and AMP by catalyzing the following reaction:ATP + AMP ⇌ 2 ADPOne unit of Myokinase will convert 1.0 µmol ATP and 1.0 µmol AMP to 2.0 µmol ADP per min at 25°C and pH 7.5.

Nucleoside phosphorylase (Purine nucleoside phosphorylase, PNP, PNPase, inosine phosphorylase, inosine-guanosine phosphorylase; EC 2.4.2.1) is an enzyme that catalyzes the following reaction:  purine nucleoside + Pi ⇌ purine + alpha-D-ribose 1-phosphate  One unit of nucleoside phosphorylase will phosphorylate 1.0 micromole of inosine to hypoxanthine and alpha-D-ribose 1-phosphate per min at pH 7.4 and 25°C.

<p>Oxalate Oxidase, freeze-dried, is an enzymatic preparation that serves as a catalyst in biochemical reactions. This enzyme is derived from wheat, a common plant source, ensuring a naturally occurring origin. Its primary mode of action is the oxidation of oxalate into carbon dioxide and hydrogen peroxide. This biochemical activity is significant in various scientific applications, specifically in the breakdown of oxalate, which plays a crucial role in metabolic and environmental processes.</p>