72377-05-0

Basic information

• Product Name: (S)-2-Ethylhexanoic acid
• Synonyms: (2S)-2-Ethylhexanoic acid;[S,(+)]-2-Ethylhexanoic acid;Hexanoic acid, 2-ethyl-, (2S)-
• CAS NO: 72377-05-0
• Molecular Formula: C₈H₁₆O₂
• Molecular Weight: 144.21
• Mol File: 72377-05-0.mol

Chemical Properties

• Boiling Point: 228°Cat760mmHg
• Flash Point: 116.6°C
• Appearance: /
• Density: 0.926g/cm³
• PKA: 4.82±0.25(Predicted)
• CAS DataBase Reference: (S)-2-Ethylhexanoic acid(CAS DataBase Reference)
• NIST Chemistry Reference: (S)-2-Ethylhexanoic acid(72377-05-0)
• EPA Substance Registry System: (S)-2-Ethylhexanoic acid(72377-05-0)

Safety Data

• Hazardous Substances Data: 72377-05-0(Hazardous Substances Data)

Usage

Uses

Used in Pharmaceutical Industry:
(S)-2-Ethylhexanoic acid is used as a chemical intermediate for the production of various pharmaceuticals. Its role in this industry is crucial as it aids in the synthesis of different medicinal compounds, contributing to the development of new drugs and therapies.
Used in Plasticizer Production:
In the plastics industry, (S)-2-Ethylhexanoic acid serves as a key intermediate in the creation of plasticizers. These are additives that increase the flexibility and workability of plastics, making them more suitable for a wide range of applications, from packaging to construction materials.
Used in Fragrance Industry:
(S)-2-Ethylhexanoic acid is utilized as a precursor in the synthesis of various fragrances. Its fruity odor makes it a valuable component in the development of perfumes, colognes, and other scented products, enhancing the sensory experience for consumers.
Used in Paint and Lubricant Industries:
(S)-2-Ethylhexanoic acid is used as a precursor for the synthesis of metal soaps, which are essential components in the formulation of paint driers and lubricants. These metal soaps help improve the performance and longevity of paints and lubricants, making them more efficient and durable in their respective applications.

Upstream product

• 149-57-5 2-Ethylhexanoic acid 

Downstream Products

• 2983-37-1 (+)(S)-heptane-carboxylic acid-⁽³⁾-ethyl ester 
• 760-67-8 (2S)-ethylhexanoyl chloride 
• 143058-56-4 bis<(S)ethyl-2-hexyl> maleate 
• 577-11-7 bis<(S)ethyl-2-hexyl> sodium sulfosuccinate 
• 2983-37-1 (-)-3-Ethoxycarbonyl-heptan 
• 143005-71-4 (S)ethyl-2-hexan-1-ol (R)-<2-methoxy-2-phenyl-2-(trifluoromethyl)acetic> ester 
• 1314864-59-9 S(+)-2-(2-ethylhexanamido)benzamide 
• 4164-92-5 (+)(S)-heptane-carboxylic acid-(3)-amide 
• 1974-05-6 (S)-3-bromo-heptane 

Relevant articles and documents

Iterative saturation mutagenesis accelerates laboratory evolution of enzyme stereoselectivity: Rigorous comparison with traditional methods

Efficacy in laboratory evolution of enzymes is currently a pressing issue, making comparative studies of different methods and strategies mandatory. Recent reports indicate that iterative saturation mutagenesis (ISM) provides a means to accelerate directed evolution of stereoselectivity and thermostability, but statistically meaningful comparisons with other methods have not been documented to date. In the present study, the efficacy of ISM has been rigorously tested by applying it to the previously most systematically studied enzyme in directed evolution, the lipase from Pseudomonas aeruginosa as a catalyst in the stereoselective hydrolytic kinetic resolution of a chiral ester. Upon screening only 10 000 transformants, unprecedented enantioselectivity was achieved (E = 594). ISM proves to be considerably more efficient than all previous systematic efforts utilizing error-prone polymerase chain reaction at different mutation rates, saturation mutagenesis at hot spots, and/or DNA shuffling, pronounced positive epistatic effects being the underlying reason.

Directed evolution of an enantioselective lipase with broad substrate scope for hydrolysis of α-substituted esters

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.