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Effect of Polycarboxylate Blocks on the Amidase Activity of Trypsin through Complexation with PEG/Polycarboxylate Block Ionomers

✍ Scribed by Atsushi Harada; Yuriko Yoshioka; Akifumi Kawamura; Chie Kojima; Kenji Kono


Book ID
102470907
Publisher
John Wiley and Sons
Year
2007
Tongue
English
Weight
155 KB
Volume
7
Category
Article
ISSN
1616-5187

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✦ Synopsis


Abstract

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 p__K__~a~ values of the polycarboxylate block in block ionomers.

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