Enantioselective transesterification catalysis by nanosized serine protease subtilisin Carlsberg particles in tetrahydrofuran
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چکیده
منابع مشابه
Obtaining higher transesterification rates with subtilisin Carlsberg in nonaqueous media.
Three phase partitioning (protein precipitate obtained as an interfacial layer between lower aqueous and upper t-butanol phases, formed by the addition of ammonium sulphate and t-butanol to the aqueous solution of protein) followed by lyophilization in the presence of two-component excipient resulted in 400-480x increases in transesterification activity of lyophilized powders of subtilisin Carl...
متن کاملAcylation of subtilisin Carlsberg by phenyl esters.
Approximate Hammett reaction constants rho calculated from k2/K8 values of several phenyl esters of N-acetyl-L-phenylalanine, hippuric acid, and beta-phenylpropionic acid are 0.0, 0.4, and 1.0 respectively. To determine whether the lack of substituent effect of k2/K8 with the N-acetyl-L-phenylalanine esters is a result of substituent-insensitive k2 or rate-limiting association of enzyme and sub...
متن کاملSubstrate Specificity of Aqualysin I, a Bacterial Thermophilic Alkaline Serine Protease from Thermus aquaticus YT-1: Comparison with Proteinase K, Subtilisin BPN' and Subtilisin Carlsberg.
Aqualysin I is the alkaline serine protease isolated from an extreme thermophile, Thermus aquaticus YT-1. We analyzed kinetic properties of aqualysin I, using sixteen kinds of chromogenic succinyl-tripeptide p-nitroanilides as substrates. And we compared the substrate specificity of aqualysin I with those of proteinase K, subtilisin BPN', and subtilisin Carlsberg. We found that aqualysin I had ...
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Histidine-containing peptides self-assemble on the surface of monolayer protected gold nanoparticles to form a catalytic system for transesterification reactions. Self-assembly is a prerequisite for catalysis, since the isolated peptides do not display catalytic activity by themselves. A series of catalytic peptides and substrates are studied in order to understand the structural parameters tha...
متن کاملArabidopsis PECTIN METHYLESTERASE17 is co-expressed with and processed by SBT3.5, a subtilisin-like serine protease.
BACKGROUND AND AIMS In Arabidopsis thaliana, the degree of methylesterification (DM) of homogalacturonans (HGs), the main pectic constituent of the cell wall, can be modified by pectin methylesterases (PMEs). In all organisms, two types of protein structure have been reported for PMEs: group 1 and group 2. In group 2 PMEs, the active part (PME domain, Pfam01095) is preceded by an N-terminal ext...
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ژورنال
عنوان ژورنال: Tetrahedron
سال: 2010
ISSN: 0040-4020
DOI: 10.1016/j.tet.2010.01.053