118149-43-2Relevant articles and documents
Enhancing the catalytic efficiency of subtilisin for transesterification by dual bioimprinting
Mukherjee, Joyeeta,Gupta, Munishwar N.
, p. 4397 - 4401 (2015)
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
Soluble, folded and active subtilisin in a protic ionic liquid
Falcioni, Francesco,Housden, Hazel R.,Ling, Zhenlian,Shimizu, Seishi,Walker, Adam J.,Bruce, Neil C.
, p. 749 - 751 (2010)
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.
Enhanced activity of α-chymotrypsin in organic media using designed molecular staples
Tremblay, Mélanie,C?té, Simon,Voyer, Normand
, p. 6824 - 6828 (2005)
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
The Effect of Crown Ethers on Enzyme-catalysed Reactions in Organic Solvents
Reinhoudt, David N.,Eendebak, Anke M.,Nijenhuis, Wilma F.,Verboom, Willem,Kloosterman, Marcel,Shoemaker, Hans E.
, p. 399 - 400 (1989)
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
Mukherjee, Joyeeta,Mishra, Prasant,Gupta, Munishwar N.
, p. 1976 - 1981 (2015)
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.
Dipole formation and solvent electrostriction in subtilisin catalysis
Michels, Peter C.,Dordick, Jonathan S.,Clark, Douglas S.
, p. 9331 - 9335 (1997)
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
NON-AQUEOUS ENZYME-POLYMER CONJUGATE SOLUTIONS AND RELATED METHODS
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Paragraph 0111-0113, (2018/01/11)
An enzyme-polymer conjugate shows increased activity and molecular dissolution in non-aqueous solvents enabling enzyme mediated catalysis in non-aqueous solutions. The inventions described in this specification relate to enzyme-polymer conjugates, organic
