Superior activities of enzymes physically immobilized on structurally regular poly(methyl methacrylate) surfaces

Hisao Matsuno, Yuya Nagasaka, Kimio Kurita, Takeshi Serizawa

Research output: Contribution to journalArticle

26 Citations (Scopus)

Abstract

Ultrathin poly(methyl methacrylate) (PMMA) stereocomplex films with macromolecularly doublestranded regular nanostructures were prepared by layer-by-layer (LbL) assembly of isotactic (it) and syndiotactic (st) PMMAs on solid substrates, and these films were used for enzyme immobilization supports. Hydrolysis of p-nitrophenyl-β-D-galactopyranoside (PNPG) by the immobilized β-galactosidase (β-Gal) on the complex film was 2- and 4-fold faster than those by the enzyme immobilized on singlecomponent it-PMMA and atactic (at) PMMA films, respectively. Quartz crystal microbalance (QCM) analysis revealed that greater amounts of β-Gal were immobilized on the complex film through physical adsorption than those on the single-component films. Michaelis constants (Km) of the enzyme were independent of film components; however, catalytic efficiencies (kcatKm) were increased by regulation of PMMA conformation at film surfaces. Attenuated total reflection infrared (ATR-IR) analysis revealed that structural denaturation of the enzyme after immobilization processes was well-suppressed on the complex film, although the enzyme on the bare gold or single-component PMMA films were denatured. We propose here that a slight difference of polymer surface structures strongly affects activities of immobilized enzymes, even though polymers have the same chemical component.

Original languageEnglish
Pages (from-to)2174-2179
Number of pages6
JournalChemistry of Materials
Volume19
Issue number9
DOIs
Publication statusPublished - May 1 2007
Externally publishedYes

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Immobilized Enzymes
Polymethyl Methacrylate
Polymethyl methacrylates
Enzymes
Polymers
Galactosidases
Enzyme immobilization
Denaturation
Quartz crystal microbalances
Galactose
Surface structure
Gold
Conformations
Hydrolysis
Nanostructures
Infrared radiation
Adsorption

All Science Journal Classification (ASJC) codes

  • Chemistry(all)
  • Chemical Engineering(all)
  • Materials Chemistry

Cite this

Superior activities of enzymes physically immobilized on structurally regular poly(methyl methacrylate) surfaces. / Matsuno, Hisao; Nagasaka, Yuya; Kurita, Kimio; Serizawa, Takeshi.

In: Chemistry of Materials, Vol. 19, No. 9, 01.05.2007, p. 2174-2179.

Research output: Contribution to journalArticle

Matsuno, Hisao ; Nagasaka, Yuya ; Kurita, Kimio ; Serizawa, Takeshi. / Superior activities of enzymes physically immobilized on structurally regular poly(methyl methacrylate) surfaces. In: Chemistry of Materials. 2007 ; Vol. 19, No. 9. pp. 2174-2179.
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