1245821-69-5

Basic information

• Product Name: (S)-1-phenyl-hexyl acetate
• Synonyms: (S)-1-phenyl-hexyl acetate
• CAS NO: 1245821-69-5
• Molecular Weight: 220.312
• Mol File: 1245821-69-5.mol
• Article Data: 5

Chemical Properties

• CAS DataBase Reference: (S)-1-phenyl-hexyl acetate(CAS DataBase Reference)
• NIST Chemistry Reference: (S)-1-phenyl-hexyl acetate(1245821-69-5)
• EPA Substance Registry System: (S)-1-phenyl-hexyl acetate(1245821-69-5)

Safety Data

• Hazardous Substances Data: 1245821-69-5(Hazardous Substances Data)

Upstream product

• 108-05-4 vinyl acetate 
• 4471-05-0 1-phenylhexan-1-ol 
• 942-92-7 caprophenone 
• 108-22-5 Isopropenyl acetate 

Relevant articles and documents

Expanding substrate scope of lipase-catalyzed transesterification by the utilization of liquid carbon dioxide

Secondary alcohols having bulky substituents on both sides of the chiral center are often poor substrates for most lipases. Here we reported that substrate scopes of two of the most used lipases, Candida antarctica lipase B and Burkholderia cepacia lipase, were found to be expanded toward more bulky secondary alcohols such as 1-phenyl-1-dodecanol and 2-methyl-1-phenyl-1-propanol by simply using them in liquid carbon dioxide as a solvent. The effects of solvents, reaction pressure, and pre-treatment of the enzyme with liquid CO2on this acceleration phenomenon were also studied.

Ionic-surfactant-coated Burkholderia cepacia lipase as a highly active and enantioselective catalyst for the dynamic kinetic resolution of secondary alcohols

With a coat for activity: A highly active enzyme was prepared by coating Burkholderia cepacia lipase with an ionic surfactant for use in dynamic kinetic resolution (DKR). Important features of this enzyme include: the fastest DKR of 1-phenylethanol, the h

Rational creation of mutant enzyme showing remarkable enhancement of catalytic activity and enantioselectivity toward poor substrates

Catalytic activity and enantioselectivity of lipase toward poor substrates bearing bulky substituents on both sides have been dramatically improved by rational design; the E value for a poor substrate was increased from 5 (wild-type enzyme) to >200 (I287F