118149-43-2

Upstream product

• 71-23-8 propan-1-ol 
• 4134-09-2 ethyl N-acetyl-DL-phenylalaninate 
• 2361-96-8 ethyl N-acetyl-(L)-phenylalaninate 
• 108395-58-0 acetyl L-phenylalanine chloroethyl ester 
• 173172-13-9 N-Acetyl-(D,L)-phenylalanine 2,2 2-trifluoroethyl ester 
• 2018-61-3 (S)-2-acetylamino-3-phenylpropanoic acid 
• 3618-96-0 (S)-N-acetylphenylalanine 
• 67-56-1 methanol 
• 14426-21-2 diethanolamine hydrochloride 
• 2901-75-9 (R,S)-N-acetyl phenylalanine 

Downstream Products

• 3618-96-0 (S)-N-acetylphenylalanine 

Relevant academic research and scientific papers

Enhancing the catalytic efficiency of subtilisin for transesterification by dual bioimprinting

Bioimprinting is a technique in which an aqueous solution of a protein molecule along with the imprint molecule is dried to remove bulk water. Subtilisin was dissolved in an aqueous buffer with a substrate analog and precipitated with the substrate alcoho

Inversion of enantioselectivity of serine proteases

The enantioselectivity of serine proteases in the transesterification of N-acetyl-(D,L)-phenylalanine esters with propan-1-ol in cyclohexane is strongly influenced by the leaving ability of the alcoholate group.Moreover the enantioselectivity is greatly influenced by the addition of small amounts (0.33 M) of organic additives.Addenda with a small molecular volume like e.g. ethanol and acetonitrile increase the rate for the L-enantiomer whereas alcohols with bulky alkyl groups like e.g. tert-butanol and 2-methylbutan-2-ol enhance the activity of the enzyme towards the D-enantiomer.This enables a rational tuning of the enantioselectivity as was demonstrated for four different proteases (α-chymotrypsin, subtilisin Carlsberg, Aspergillus oryzae protease, and elastase).

Soluble, folded and active subtilisin in a protic ionic liquid

The activity of proteases chymotrypsin and subtilisin dissolved in a range of protic hydroxylalkylammonium ionic liquids was tested against the model substrate APEE (N-acetyl-l-phenylalanine ethyl ester); activity was only observed for subtilisin in diethanolammonium chloride (DEA Cl), while chymotrypsin was not active in any PIL tested.

Structure and function of subtilisin BPN' solubilized in organic solvents

Enzyme structure and function have been studied for subtilisin BPN' solubilized in organic solvents by ion pairing with low concentrations of an anionic surfactant (Aerosol OT) in the absence of reversed micelles. Soluble subtilisin shows strikingly different behavior in octane and tetrahydrofuran (THF). In octane, the k(cat)/K(m) for the transesterification of N-acetyl-L-phenylalanine ethyl ester (APEE) is 370 M-1 s-1, within one order of magnitude of the enzyme's hydrolytic activity in water. Moreover, the observed half-life of the soluble enzyme in octane is nearly three orders of magnitude greater than in water, presumably because of the absence of autolysis in the organic solvent. In contrast, the catalytic efficiency of the enzyme dissolved in the polar solvent THF is 0.04 M-1 s-1, and the enzyme loses 99% of its activity within 10 min. Comparable enzyme inactivation could also be observed in octane, but only at elevated temperatures such as 70 °C. Therefore, the mechanisms of deactivation of the soluble enzyme were investigated in both octane and THF. Kinetic and spectroscopic (CD and EPR) studies support the existence of multiple inactive forms of the soluble enzyme in THF at 25 °C and in octane at 70 °C. Notably, in both cases a denatured form can be renatured in anhydrous octane at 25 °C, the first demonstration of enzyme renaturation in a bulk organic solvent. A model explaining the THF- and thermally-induced inactivation processes of soluble subtilisin BPN' is proposed, and the apparent reasons for the exceptionally high activity and stability of the soluble enzyme in octane are discussed.

Enhanced activity of α-chymotrypsin in organic media using designed molecular staples

We report the enhancement of α-chymotrypsin activity in organic solvents using modified peptides bearing two crown ethers. The transesterification of N-acetyl-l-phenylalanine ethyl ester with 1-propanol was used as model reaction. Co-lyophilization of cro

Methanol dramatically enhances serine protease activity under anhydrous conditions

The catalytic activity of rigorously dried lyophilised subtilisin Carlsberg and α-chymotrypsin in anhydrous solvents is enhanced dramatically on addition of dry methanol, while ethanol and propanol produce no effect.

The Effect of Crown Ethers on Enzyme-catalysed Reactions in Organic Solvents

Crown ethers considerably enhance the rate of the α-chymotrypsin-catalysed transesterification of N-acetyl-L-phenylalanine ethyl ester (N-Ac-L-Phe-OEt) with propan-1-ol in n-octane; with subtilisin the effect is somewhat less pronounced.

Urea treated subtilisin as a biocatalyst for transformations in organic solvents

Abstract Subtilisin lyophilized from its solution in aqueous buffer in the presence of 6 M urea showed up to 50-fold increase (as compared to lyophilized subtilisin not subjected to urea treatment) in its initial rate of a transesterification reaction in anhydrous n-hexane. The lyophilization time controlling the extent of 'drying' was an important parameter. The urea treated subtilisin had five times shorter half life during heating at 100 C in hexane. The change in conformation was also reflected in its 92-fold higher activity at 15 C as compared to merely 28-fold higher activity at 45 C. The comparative enantioselectivity of urea treated subtilisin during kinetic resolution of 1-phenylethanol was expectedly lower. Its enantioselectivity during kinetic resolution of a natural substrate N-acetyl-(R,S)-phenylalanine ethyl ester in hexane was higher. Urea treated subtilisin also showed higher catalytic promiscuity during an aldol condensation. CD studies in both far UV and near UV region were also carried out to compare the two structures.

Nanophase separated amphiphilic microbeads

The synthesis of nonporous nanophase separated amphiphilic microbeads was investigated. The synthesis was performed with a mixture of α,ω- methacrylate-terminated poly-dimethylsiloxane (MA-PDMS-MA), trimethylsilylated 2-hydroxyethylacrylate (TMSOEA) and t

Dipole formation and solvent electrostriction in subtilisin catalysis

The transition state for subtilisin-catalyzed transesterification was probed by high-pressure kinetic studies in solvents spanning a wide range of dielectric constants. The electrostatic model of Kirkwood described the solvent effects and gave a lower lim