Enzima

Lipase from *Candida antarctica* is an enzyme-based biocatalyst, which is derived from the yeast *Candida antarctica*. This enzyme operates via a catalytic mechanism that involves the hydrolysis of ester bonds in lipid substrates, thereby facilitating the breakdown of fats into glycerol and free fatty acids. Its catalytic efficiency and stability in various conditions make it highly versatile for industrial applications.

Phospholipases D belong to the family of esterases and act on phosphatidylcholine in the plasma membrane to release phosphatidic acid (PA) and choline. Phospholipases D can be used as versatile tools in hydrolysis and transphosphatidylation reactions for industrial, chemical and food applications. The Phospholipase D Kit contains 4 enzymes with a broad pH range for transphosphatidylation activity.

Superoxide dismutase coupled to polyethylene glycol. Superoxide dismutase (EC 1.15.1.1) is an enzyme that catalyzes the following reaction:  2 H+ + 2 O2− → O2 + H2O2  thus converting an extremely reactive and cytotoxic superoxide radical into oxygen and (significantly less reactive) hydrogen peroxide.

Specific activity: >500 units/mg-protein.Unit definition: One unit will polymerize 1.0 micro mole of ADP, releasing 1.0 micro mole of inorganic phosphate in 15 minutes at pH 9.1 at 37 °C.

Alcohol dehydrogenase (EC 1.1.1.1) is the enzyme that catalyzes interconversion between alcohols and aldehydes or ketones, using NAD+/NADH as a cofactor in the following reaction: CH3CH2OH + NAD+ ⇔ CH3CHO + NADH + H+     One unit of alcohol dehydrogenase will convert 1.0 µmol of ethanol to acetaldehyde per minute at pH 8.8 and 25 °C.

Glucose-6-phosphate isomerase (GPI, phosphoglucose isomerase/phosphoglucoisomerase, PGI, phosphohexose isomerase, PHI; EC 5.3.1.9) is an enzyme that catalyses isomerisation between Glucose-6-phosphate and Fructose-6-phosphate:  G6P ⇌ F6P  One unit of GPI will convert 1.0 mmole of Fructose-6-phosphate to Glucose-6-phosphate per minute at pH 7.4 and 25 °C.

Aspartic acid proteinase is a type of proteolytic enzyme, which originates from various biological sources including humans, fungi, and plants. It is characterized by its action via two critical aspartic acid residues in the active site, which facilitate the hydrolysis of peptide bonds in proteins. This enzyme operates optimally in acidic environments, making it crucial in processes like digestion and protein processing within cellular compartments such as lysosomes.

Neuron-specific enolase human (ENO2, Enolase 2, Neural enolase, Gamma-enolase, Phosphopyruvate hydratase, 2-phospho-D-glycerate hydro-lyase; EC 4.2.1.11) is the enzyme that is catalyzes the following reaction:  2-phospho-D-glycerate ⇌ phosphoenolpyruvate + H2O  One unit of enolase will convert 1.0 μmole of 2-phosphoglycerate to phosphoenolpyruvate per min.