Improved complementary polymer pair system: switching for enzyme activity by PEGylated polymers.
The development of technology for on/off switching of enzyme activity is expected to expand the applications of enzyme in a wide range of research fields. We have previously developed a complementary polymer pair system (CPPS) that enables the activity of several enzymes to be controlled by a pair of oppositely charged polymers. However, it failed to control the activity of large and unstable α-amylase because the aggregation of the complex between anionic α-amylase and cationic poly(allylamine) (PAA) induced irreversible denaturation of the enzyme. To address this issue, we herein designed and synthesized a cationic copolymer with a poly(ethylene glycol) backbone, poly(N,N-diethylaminoethyl methacrylate)-block-poly(ethylene glycol) (PEAMA-b-PEG). In contrast to PAA, α-amylase and β-galactosidase were inactivated by PEAMA-b-PEG with the formation of soluble complexes. The enzyme/PEAMA-b-PEG complexes were then successfully recovered from the complex by the addition of anionic poly(acrylic acid) (PAAc). Thus, dispersion of the complex by PEG segment in PEAMA-b-PEG clearly plays a crucial role for regulating the activities of these enzymes, suggesting that PEGylated charged polymer is a new candidate for CPPS for large and unstable enzymes.
Graduate School of Pure and Applied Sciences, University of Tsukuba, Tsukuba, Ibaraki, Japan.
Takaaki
T
Kurinomaru
Shunsuke
S
Tomita
Shinpei
S
Kudo
Sumon
S
Ganguli
Yukio
Y
Nagasaki
Kentaro
K
Shiraki
D008962:Models, Theoretical; D011092:Polyethylene Glycols / Q000737:chemistry*; D011108:Polymers / Q000737:chemistry*; D000516:alpha-Amylases / Q000378:metabolism; D001616:beta-Galactosidase / Q000378:metabolism
D011108:Polymers; D011092:Polyethylene Glycols; D000516:alpha-Amylases; D001616:beta-Galactosidase