90846-39-2Relevant academic research and scientific papers
Protease-Catalyzed Peptide Formation under High Pressure
Kunugi, Shigeru,Tanabe, Kazuo,Yamashita, Kouji,Morikawa, Yoshio,Ito, Takanobu,et al.
, p. 514 - 518 (2007/10/02)
The effect of high pressure on peptide formation by the catalysis of carboxypeptidase Y (substitution of ester or peptide by amino acid derivative) or by thermolysin (condensation of N-acylamino acid and amino acid amide) was studied.The carboxypeptidase Y-catalyzed substitution reaction of N-phenylalanine ethyl ester with glycinamide or phenylalaninamide showed a six-fold higher total peptide yield at 200 MPa than at atmospheric pressure.In the case of the reaction of N-acyldipeptide and amino acid amide, both the peptide yield and substitution efficiency were improved at elevated pressure and the wasteful hydrolysis of the substrate was highly depressed by increasing pressure.The pressure was also effective to get rid of the substrate inhibition by the amino acid ester inthe reaction between the N-acylamino acid ester and the amino acid ester and to yield much dipeptide ester at high pressure.An improvement of the peptide yield by pressure for the reaction of thermolysin was observed in a combination of less specific substrates, N-benzyloxycarbonyl-L-aspartic acid and phenylalanine methyl ester, since the high catalytic activity of this enzyme under elevated pressure was significant only in the case that the peptide yield was kinetic-controlled.
Wheat Carboxypeptidase-Catalyzed Peptide Synthesis by Aminolysis of N-Acyl Amino Acid Ester. Indication of the Acyl-Enzyme Mechanism
Shima, Hiroshi,Fukuda, Mitsuhiro,Tanabe, Kazuo,Ito, Takanobu,Kunugi, Shigeru
, p. 1403 - 1406 (2007/10/02)
Dipeptide synthesis from N--acylated (Fua-) amino acid ethyl ester and amino acid amide catalyzed by wheat bran carboxypeptidase (carboxypeptidase W) was studied.The optimum pH for peptide formation was at pH 8; more than 60 percent of the initial N-Fua-L-phenylalanine ethyl ester was converted to N-Fua-L-phenylalnylglycinamide under optimum conditions.The dependence of peptide formation on the concentration of amino acid amide showed an apparent saturation; this could be successfully explained by a reaction scheme which involved an acylated enzyme attacked by an enzyme-bound amine.The results for a reaction in the presence of two different amine components also supported this mechanism.Gly-NH2 had a better affinity to the acylated carboxypeptidase and the apparent dissociation constants (KN(app)) was about 50 mM.These results were compared with those for those reactions catalyzed by carboxypeptidases from yeast and malt.
