Enzyme switch by complementary polymer pair system (CPPS)
Author(s) -
Shunsuke Tomita,
Len Ito,
Hiroshi Yamaguchi,
Genichi Konishi,
Yukio Nagasaki,
Kentaro Shiraki
Publication year - 2010
Publication title -
soft matter
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.99
H-Index - 170
eISSN - 1744-6848
pISSN - 1744-683X
DOI - 10.1039/c000930j
Subject(s) - enzyme , allylamine , ribonuclease , lysozyme , chemistry , polymer , amylase , acrylic acid , rnase p , biochemistry , cellulase , enzyme assay , combinatorial chemistry , polyelectrolyte , organic chemistry , rna , copolymer , gene
Manipulation of enzyme activity at will presents various research and industrial applications. Herein we describe development of a technology for inactivation and reactivation of enzyme activities using a polyanionic poly(acrylic acid) (PAAc) and a polycationic poly(allylamine) (PAA). Enzyme activities of ribonuclease A (RNase A), lysozyme, cellulase, and α-amylase were lost through addition of PAAc or PAA because of their binding to the enzymes. The activity of these enzymes except for α-amylase was then fully restored from the complex by the addition of oppositely charged polymers. Such manipulation of enzyme activity using a complementary polymer pair system (CPPS) enables the expansion of biomedical and biotechnological applications of the enzymes, including realization of protein delivery and intelligent bioreactors
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