68922-11-2

Usage

General Description

1-methyl-2-phenylethyl butyrate is a chemical compound with the molecular formula C13H18O2. It is an ester, which is a type of organic compound formed through the reaction of an alcohol and a carboxylic acid. This particular ester has a fruity, sweet aroma and is commonly used as a flavoring agent in the food and beverage industries. It can be found in a variety of products including confectionery, baked goods, and dairy products. Additionally, 1-methyl-2-phenylethyl butyrate is also used in the production of perfumes and fragrances due to its pleasant smell. 1-methyl-2-phenylethyl butyrate is considered safe for consumption and is approved for use as a food additive by regulatory agencies in many countries.

InChI:InChI=1/C13H18O2/c1-3-7-13(14)15-11(2)10-12-8-5-4-6-9-12/h4-6,8-9,11H,3,7,10H2,1-2H3

Upstream product

• 123-20-6 vinyl n-butyrate 
• 698-87-3 3-phenyl-2-propanol 
• 371-27-7 2,2,2-trifluoroethylbutyrate 
• 107-92-6 butyric acid 
• 71-43-2 benzene 

Relevant academic research and scientific papers

Discovery and Redesign of a Family VIII Carboxylesterase with High (S)-Selectivity toward Chiral sec-Alcohols

Highly enantioselective lipase has been widely utilized in the preparation of versatile enantiopure chiral sec-alcohols through kinetic or dynamic kinetic resolution. Lipase is intrinsically (R)-selective, and it is difficult to obtain (S)-selective lipase. Recent crystal structures of a family VIII carboxylesterase have revealed that the spatial array of its catalytic triad is the mirror image of that of lipase but with a catalytic triad that is distinct from lipase. We, therefore, hypothesized that the family VIII carboxylesterase may exhibit (S)-enantioselectivity toward sec-alcohols similar to (S)-selective serine protease, whose catalytic triad is also spatially arrayed as its mirror image. In this study, a homologous enzyme (carboxylesterase from Proteobacteria bacterium SG_bin9, PBE) of a known family VIII carboxylesterase (pdb code: 4IVK) was prepared, which showed not only moderate (S)-selectivity toward sec-alcohols such as 3-butyn-2-ol and 1-phenylethyl alcohol but also (R)-selectivity toward particular sec-alcohols among the substrates explored. Furthermore, the (S)-selectivity of PBE has been significantly improved by rational redesign based on molecular modeling. Molecular modeling identified a binding pocket composed of Ser381, Ala383, and Arg408 for the methyl substituent of (R)-1-phenylethyl acetate and suggested that larger residues may increase the enantioselectivity by interfering with the binding of the slow-reacting enantiomer. As predicted, substituting Ser381with larger residues (Phe, Tyr, and Trp) significantly improved the (S)-selectivity of PBE toward all sec-alcohols explored, even the substrates toward which the wild-type PBE exhibits (R)-selectivity. For instance, the enantioselectivity toward 3-butyn-2-ol and 1-phenylethyl alcohol was improved from E = 5.5 and 36.1 to E = 2001 and 882, respectively, by single mutagenesis (S381F).

Dual enzymatic dynamic kinetic resolution by Thermoanaerobacter ethanolicus secondary alcohol dehydrogenase and Candida antarctica lipase B

The immobilization of Thermoanaerobacter ethanolicus secondary alcohol dehydrogenase (TeSADH) using sol-gel method enables its use to racemize enantiopure alcohols in organic media. Here, we report the racemization of enantiopure phenyl-ring-containing secondary alcohols using xerogel-immobilized W110A TeSADH in hexane rather than the aqueous medium required by the enzyme. We further showed that this racemization approach in organic solvent was compatible with Candida antarctica lipase B (CALB)-catalyzed kinetic resolution. This compatibility, therefore, allowed a dual enzymatic dynamic kinetic resolution of racemic alcohols using CALB-catalyzed kinetic resolution and W110A TeSADH-catalyzed racemization of phenyl-ring-containing alcohols.

Functional expression of Serratia marcescens H30 lipase in Escherichia coli for efficient kinetic resolution of racemic alcohols in organic solvents

A lipase from Serratia marcescens H30 was cloned and functionally expressed in E. coli in soluble form (more than 80%). The recombinant lipase activity reached 25,000 U/L after optimization. Different carriers were used to immobilize the recombinant S. marcescens lipase (SmL), and LH-EP was found to be the most ideal carrier. LH-EP immobilized SmL could catalyze enantioselective resolution of racemic alcohols. Using 4-phenyl-2-butanol as the model alcohol, the effects of temperature, organic solvent, water activity, acyl donor and substrate molar ratio on the LH-EP immobilized SmL catalyzed kinetic resolution were investigated. All of these factors influenced the resolution effect to some extent. At last, a high E value of more than 200 was achieved, with ee S > 99% and a conversion of 49.9%. Further studies showed that the LH-EP immobilized SmL could also catalyze the kinetic resolution of other structure similar racemic alcohols. These results indicate that the SmL is useful for biocatalytic production of chiral alcohols. This work is the first attempt of using SmL in this field, and it further broadens the application field of SmL.

Kinetic and chemical resolution of different 1-phenyl-2-propanol derivatives

Seven chiral target molecules containing a hydroxy group have been resolved by both biocatalytic and chemical means. The lipase-catalyzed acylation mainly yielded the acylated derivative of the (R)-alcohols with moderate enantiomeric excess and the enantiopure (S)-alcohols. In the course of the chemical resolution, first the dicarboxylic acid monoesters of the target molecules were synthesized and the resolution of these monoesters was attempted by different homochiral bases. By re-resolution and/or optimization of the reaction time and/or recrystallization, respectively, each molecule was produced in very high enantiomeric purity.

Synthesis of aromatic alcohols and their alkanoic acid esters

The reaction of benzene with ethylene and propylene oxides in a helium atmosphere with aluminum chloride as a catalyst and the esterification of the resulting alcohols with saturated monocarboxylic acids in the presence of the heterogeneous catalyst KU-2-8 were studied. Pleiades Publishing, Inc., 2006.

METHOD OF PREPARATION OF OPTICALLY ACTIVE ALCOHOLS

The present invention relates to a method for preparing chiral alcohol having optical activity. More specifically, the present invention relates to a method for preparing (S)-chiral alcohol with a high yield and a high optical purity by mixing achiral substrates such as racemic alcohol or ketone with metal catalyst and protein hydrolase to perform a dynamic kinetic resolution reaction.

(S)-selective dynamic kinetic resolution of secondary alcohols by the combination of subtilisin and an aminocyclopentadienylruthenium complex as the catalysts

A new procedure for the dynamic kinetic resolution (DKR) of racemic alcohols into single enantiomers is described. This procedure employs surfactant-treated subtilisin as an (S)-selective resolving catalyst and an aminocyclopentadienylruthenium complex as a racemizing catalyst. The DKR is performed best in the presence of an acyl donor such as trifluoroethyl butyrate in THF at room temperature. Eight simple secondary alcohols have been efficiently resolved with high optical purities and good yields. The subtilisin-based DKR is complementary in stereoselectivity to its lipase-based counterpart. For an acyl-carrying alcohol, both subtilisin- and lipase-based DKRs have proceeded equally well to give a pair of enantiomeric products (>99.5% ee each) with opposite optical rotations in high yields (94-95%). Copyright

Activity enhancement of pig liver esterase in organic solvents by colyophilization with methoxypolyethylene glycol: Kinetic resolution of alcohols

Colyophilization of pig liver esterase with methoxypolyethylene glycol gave a catalyst, PLE/MPEG, which showed an enhanced activity in organic solvents. The PLE/MPEG catalyzed transesterification of the alcohols rac-1a- d with vinyl propionate in toluene proceeded with good to high selectivities. The addition of up to 1% of water to the reaction mixture resulted in a significant increase in enantioselectivity. Immobilization of PLE/MPEG for the batch-wise resolution was accomplished by its spontaneous adsorption on an ultrafiltration membrane.