29701-43-7Relevant academic research and scientific papers
Optimal α-chymotrypsin-catalyzed synthesis of N-Ac-Phe-Gly-NH 2
Ju, Hen-Yi,Too, Jui-Rze,Chang, Cheng,Shieh, Chwen-Jen
, p. 403 - 408 (2009)
N-Acetyl-phenylalanine-glycinamide (N-Ac-Phe-Gly-NH2), a type of dipeptide derivative, was synthesized from N-acetyl phenylalanine ethyl ester and glycinamide and catalyzed by α-chymotrypsin, a protease, in a biphasic system. Response surface m
Chymotrypsin-catalyzed peptide synthesis in deep eutectic solvents
Maugeri, Zaira,Leitner, Walter,Dominguez De Maria, Pablo
supporting information, p. 4223 - 4228 (2013/07/26)
Deep eutectic solvents (DESs) are formed by mixing quaternary ammonium salts (e.g., choline chloride) and hydrogen-bond donors (e.g., glycerol or urea), which leads to biodegradable and readily available ionic solvents at room temperature. Analogous to other ionic liquids, DESs represent a promising reaction media if hydrophobic and hydrophilic substrates need to be combined. This paper assesses DESs as reaction media for chymotrypsin-catalyzed peptide synthesis. After careful determination of the reaction conditions (e.g., water content, enzyme loading), α-chymotrypsin displayed high activity for peptide synthesis in choline chloride/glycerol mixtures to afford productivities of ca. 20 g L-1 h-1 and with complete selectivity for the peptide, which is in contrast to the detrimental hydrolysis pathway observed in aqueous media. The nonimmobilized suspended enzyme could be reused several times by simple filtration with excellent to moderate activities. Overall, the results reported suggest that choline chloride based DESs may become promising neoteric solvents for peptide synthesis through biocatalysis. Copyright
Optimal covalent immobilization of α-chymotrypsin on Fe 3O4-chitosan nanoparticles
Ju, Hen-Yi,Kuo, Chia-Hung,Too, Jui-Rze,Huang, Hsin-Yi,Twu, Yawo-Kuo,Chang, Chieh-Ming J.,Liu, Yung-Chuan,Shieh, Chwen-Jen
experimental part, p. 9 - 15 (2012/07/13)
This study investigated the immobilization of α-chymotrypsin onto magnetic Fe3O4-chitosan (α-chymotrypsin-Fe 3O4-CS) nanoparticles by covalent binding. The response surface methodology (RSM) with a 3-factor-3-le
Carboxyl-Modified Amino Acids and Peptides as Protease Inhibitors
Thompson, Stewart A.,Andrews, Peter R.,Hanzlik, Robert P.
, p. 104 - 111 (2007/10/02)
Several types of carbonyl-modified amino acids and peptides were prepared in forms having N-terminal modifications (carrier fragments) suitable for one of several representative protease enzymes, and their inhibitory action toward those enzymes were evalu
