116644-59-8

Basic information

• Product Name: Dodecanoic acid, (1R)-1-phenylethyl ester
• CAS NO: 116644-59-8
• Molecular Formula: C20H32O2
• Molecular Weight: 304.473
• Mol File: 116644-59-8.mol
• Article Data: 12

Chemical Properties

• CAS DataBase Reference: Dodecanoic acid, (1R)-1-phenylethyl ester(CAS DataBase Reference)
• NIST Chemistry Reference: Dodecanoic acid, (1R)-1-phenylethyl ester(116644-59-8)
• EPA Substance Registry System: Dodecanoic acid, (1R)-1-phenylethyl ester(116644-59-8)

Safety Data

• Hazardous Substances Data: 116644-59-8(Hazardous Substances Data)

Upstream product

• 143-07-7 lauric acid 
• 98-85-1 1-Phenylethanol 
• 1517-69-7 (R)-1-phenylethanol 
• 2146-71-6 vinyl laurate 
• 97130-78-4 (R,S)-1-phenylethyl laurate 
• 112-16-3 n-dodecanoyl chloride 

Relevant articles and documents

The effect of the migrating group structure on enantioselectivity in lipase-catalyzed kinetic resolution?of?1-phenylethanol

We have studied the effects of the acyl moiety on the enantioselectivity of three lipases: Candida antarctica B, Pseudomonas cepacia and Candida cylindracea, frequently used in kinetic resolutions by acylation or hydrolysis. The size of the acyl group was examined using various enol esters during the transesterification of 1-phenylethanol and the hydrolysis of the corresponding phenylethylesters. C. antarctica-B lipase showed the highest selectivity in the transesterification of 1-phenylethanol with isopropenyl and vinyl acetate, vinyl decanoate, vinyl laurate, (E?>?200). The esters 1-phenyl -ethyl-acetate, decanoate and laurate are also hydrolyzed with high selectivities (E?>?150) with CAL-B. The results can be correlated to the three-dimensional form of each lipase. The effect of the migrating group on the reactivity and selectivity of the lipases are discussed for both reactions.

A Lipid-Coated Lipase as an Enantioselective Ester Synthesis Catalyst in Homogeneous Organic Solvents

A lipid-coated lipase was prepared, in which hydrophilic head groups of lipids interact with the hydrophilic surface of the enzyme and lipophilic alkyl chains extend away from its surface and solubilize the enzyme in hydrophobic organic solvents.Enantiose

Acid zeolites as alcohol racemization catalysts: Screening and application in biphasic dynamic kinetic resolution

Acid zeolites were screened as heterogeneous catalysts for racemization of benzylic alcohols. The most promising zeolites appeared to be H-Beta zeolites, for which the optimal reaction conditions were studied in further detail. The zeolite performance was

Easy and simple SiO2 immobilization of lipozyme CaLB-L: Its use as a catalyst in acylation reactions and comparison with other lipases

In this study, lipase from Candida antarctica B (Lipozyme CaLB-L) was successfully immobilized on SiO2 through adsorption and used to obtain (R)-(+)-esters derived from (R,S)-1-phenylethanol. The new immobilized enzyme was compared with commercially immobilized lipases (Novozyme 435, Lipozyme 435 and Pseudomonas cepacia (PSC-II and PSD-I)). Lipozyme CaLB-L adsorbed onto SiO2 was found to be a good catalyst and, under optimal conditions, esters could be obtained with conversion 44percent, enantiomeric excess of product (eep) > 99percent, enantiomeric excess of substract (ees) 77percent and enantiomeric ratio (E) > 200. The lipase maintained enantioselectivity under adverse conditions, such as in organic solvents, with an excess of substrate and at different temperatures. The immobilized lipase could be reused five times with no significant loss of the activity.