98409-21-3

Basic information

• Product Name: (2R)-2-hydroxyoctan-3-one
• CAS NO: 98409-21-3
• Molecular Formula: C₈H₁₆O₂
• Molecular Weight: 144.2114
• Mol File: 98409-21-3.mol
• Article Data: 4

Chemical Properties

• Boiling Point: 187.7°C at 760 mmHg
• Flash Point: 72°C
• Density: 0.926g/cm³
• Vapor Pressure: 0.172mmHg at 25°C
• Refractive Index: 1.435
• CAS DataBase Reference: (2R)-2-hydroxyoctan-3-one(CAS DataBase Reference)
• NIST Chemistry Reference: (2R)-2-hydroxyoctan-3-one(98409-21-3)
• EPA Substance Registry System: (2R)-2-hydroxyoctan-3-one(98409-21-3)

Safety Data

• Hazardous Substances Data: 98409-21-3(Hazardous Substances Data)

Upstream product

• 7699-00-5 (R)-Ethyl lactate 
• 110-53-2 1-Bromopentane 
• 108-05-4 vinyl acetate 
• 52279-26-2 2-hydroxy-3-octanone 
• 17223-97-1 2-(tetrahydropyran-2-yloxy)-3-octanone 
• 338-69-2 D-Alanine 
• 3525-31-3 n-pentyl lithium 

Relevant articles and documents

New and Convenient Chemoenzymatic Syntheses of (S)-2-Hydroxy-3-octanone, the Major Pheromone Component of Xylotrechus spp., and Its R-Enantiomer

New and efficient chemoenzymatic approaches for the synthesis of both enantiomers of 2-hydroxy-3-octanone in good yields and excellent enantioselectivity are presented. The S-enantiomer is a pheromone component of economically important pests in Japan, India, China, and other Asian countries. The enzymatic approaches involve transesterification of the racemic acyloin with vinyl acetate in the presence of Candida antarctica lipase B (CAL B) in 99% ee of both enantiomers (E = 167-618), or hydrolysis of the acetylated acyloin by double kinetic resolution with CAL B and C. antarctica lipase A (CAL A) in 96-98% ee of either enantiomer (E = 458). CAL A and CAL B induce reverse enantioselectivity.

Deracemization of (±)-2,3-disubstituted oxiranes via biocatalytic hydrolysis using bacterial epoxide hydrolases: Kinetics of an enantioconvergent process

Asymmetric biocatalytic hydrolysis of (±)-2,3-disubstituted oxiranes leading to the formation of vicinal diols in up to 97% ee at 100% conversion was accomplished by using the epoxide hydrolase activity of various bacterial strains. The mechanism of this deracemization was elucidated by 18OH2-labelling experiments using a partially purified epoxide hydrolase from Nocardia EH1. The reaction was shown to proceed in an enantioconvergent fashion by attack of OH- at the (S)-configured oxirane carbon atom with concomitant inversion of configuration. A mathematical model developed for the description of the kinetics was verified by the determination of the four relative rate constants governing the regio- and enantio-selectivity of the process.