Effect of polycarboxylate blocks on the amidase activity of trypsin through complexation with PEG/polycarboxylate block ionomers.
The amidase reaction of trypsin, which is a member of the serine proteinase family, is accelerated by its complexation with block ionomers containing a polycarboxylate block, such as PEG-PAA, PEG-PGA, or PEG-PMA. PEG-PAA and PEG-PGA had similar effects, causing an increase in the k(cat) value and a shift in the pH profile to a lower pH region. On the other hand, PEG-PMA showed not only an increase in the k(cat) value, but also a decrease in the activation energy; however, there was no shift in the pH dependence of the initial reaction rate. Such differences might be induced by the difference in pK(a) values of the polycarboxylate block in block ionomers.
Harada
Atsushi
A
Department of Applied Chemistry, Graduate School of Engineering, Osaka Prefecture University, Sakai, Osaka, Japan. harada@chem.osakafu-u.ac.jp
Yoshioka
Yuriko
Y
Kawamura
Akifumi
A
Kojima
Chie
C
Kono
Kenji
K
D000581:Amidohydrolases / Q000378:metabolism*; D000818:Animals; D006863:Hydrogen-Ion Concentration; D008422:Materials Testing; D015394:Molecular Structure; D010455:Peptides / Q000737:chemistry*; D011092:Polyethylene Glycols / Q000737:chemistry*; D011099:Polyglutamic Acid / Q000737:chemistry*; D011109:Polymethacrylic Acids / Q000737:chemistry*; D014357:Trypsin / Q000378:metabolism*
D010455:Peptides; D011109:Polymethacrylic Acids; C030613:polymethacrylic acid; D011099:Polyglutamic Acid; C017645:polyaspartate; D011092:Polyethylene Glycols; D014357:Trypsin; D000581:Amidohydrolases; C019665:amidase