56006-48-5 Usage
General Description
[R,(-)]-2-Ethylhexanoic acid, also known as 2-ethylhexanoic acid, is a saturated carboxylic acid with the chemical formula C8H16O2. It is a colorless, viscous liquid that is insoluble in water but soluble in organic solvents. This chemical is commonly used as a raw material in the production of metal carboxylates, which are used as catalysts in the manufacturing of polyurethanes and other polymers. Additionally, 2-ethylhexanoic acid is used as a chemical intermediate in the production of various products such as plasticizers, lubricants, and surfactants. It is also used in the synthesis of pharmaceuticals and agrochemicals. Despite its various uses, 2-ethylhexanoic acid can be harmful if ingested, inhaled, or absorbed through the skin, and precautions should be taken when handling this chemical.
Check Digit Verification of cas no
The CAS Registry Mumber 56006-48-5 includes 8 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 5 digits, 5,6,0,0 and 6 respectively; the second part has 2 digits, 4 and 8 respectively.
Calculate Digit Verification of CAS Registry Number 56006-48:
(7*5)+(6*6)+(5*0)+(4*0)+(3*6)+(2*4)+(1*8)=105
105 % 10 = 5
So 56006-48-5 is a valid CAS Registry Number.
56006-48-5Relevant articles and documents
Directed evolution of an enantioselective lipase with broad substrate scope for hydrolysis of α-substituted esters
Engstroem, Karin,Nyhlen, Jonas,Sandstroem, Anders G.,Baeckvall, Jan-E.
supporting information; experimental part, p. 7038 - 7042 (2010/07/05)
A variant of Candida antarctica lipase A (CalA) was developed for the hydrolysis of α-substituted p-nitrophenyl esters by directed evolution. The E values of this variant for 7 different esters was 45-276, which is a large improvement compared to 2-20 for the wild type. The broad substrate scope of this enzyme variant is of synthetic use, and hydrolysis of the tested substrates proceeded with an enantiomeric excess between 95-99%. A 30-fold increase in activity was also observed for most substrates. The developed enzyme variant shows (R)-selectivity, which is reversed compared to the wild type that is (S)-selective for most substrates.
