Immobilization and activity of enzymes on stereocomplex platforms

Yuya Nagasaka; Hisao Matsuno; Kimio Kurita; Takeshi Serizawa

Immobilization and activity of enzymes on stereocomplex platforms

Yuya Nagasaka, Hisao Matsuno, Kimio Kurita, Takeshi Serizawa

Research output: Contribution to conference › Paper › peer-review

Abstract

Isotactic (it) and syndiotactic (st) poly(methyl methacrylate)s (PMMAs) form double-stranded helical stereocomplexes in organic solvents. We prepared PMMA stereocomplex films by a layer-by-layer assembly method on polystyrene microplate, and β-D-galactosidase (β-Gal) was immobilized on the PMMA stereocomplex film. Then, p-nitrophenyl-β-D-galactopyranoside (PNPG) solutions were added into the β-Gal immobilized wells. The enzymatic activity was determined by following the absorption at 405 nm by the ester cleavage of PNPG. The observation was also carried out on cast it-PMMA films. Effects of film surfaces on the enzyme reaction were investigated. As a result, it was found that the enzymatic activity of the immobilized β-Gal on PMMA stereocomplex films was higher than that on cast it-PMMA films.

Original language	English
Pages	2010
Number of pages	1
Publication status	Published - 2006
Externally published	Yes
Event	55th SPSJ Annual Meeting - Nagoya, Japan Duration: May 24 2006 → May 26 2006

Other

Other	55th SPSJ Annual Meeting
Country/Territory	Japan
City	Nagoya
Period	5/24/06 → 5/26/06

All Science Journal Classification (ASJC) codes

Engineering(all)

Cite this

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title = "Immobilization and activity of enzymes on stereocomplex platforms",

abstract = "Isotactic (it) and syndiotactic (st) poly(methyl methacrylate)s (PMMAs) form double-stranded helical stereocomplexes in organic solvents. We prepared PMMA stereocomplex films by a layer-by-layer assembly method on polystyrene microplate, and β-D-galactosidase (β-Gal) was immobilized on the PMMA stereocomplex film. Then, p-nitrophenyl-β-D-galactopyranoside (PNPG) solutions were added into the β-Gal immobilized wells. The enzymatic activity was determined by following the absorption at 405 nm by the ester cleavage of PNPG. The observation was also carried out on cast it-PMMA films. Effects of film surfaces on the enzyme reaction were investigated. As a result, it was found that the enzymatic activity of the immobilized β-Gal on PMMA stereocomplex films was higher than that on cast it-PMMA films.",

author = "Yuya Nagasaka and Hisao Matsuno and Kimio Kurita and Takeshi Serizawa",

year = "2006",

language = "English",

pages = "2010",

note = "55th SPSJ Annual Meeting ; Conference date: 24-05-2006 Through 26-05-2006",

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TY - CONF

T1 - Immobilization and activity of enzymes on stereocomplex platforms

AU - Nagasaka, Yuya

AU - Matsuno, Hisao

AU - Kurita, Kimio

AU - Serizawa, Takeshi

PY - 2006

Y1 - 2006

N2 - Isotactic (it) and syndiotactic (st) poly(methyl methacrylate)s (PMMAs) form double-stranded helical stereocomplexes in organic solvents. We prepared PMMA stereocomplex films by a layer-by-layer assembly method on polystyrene microplate, and β-D-galactosidase (β-Gal) was immobilized on the PMMA stereocomplex film. Then, p-nitrophenyl-β-D-galactopyranoside (PNPG) solutions were added into the β-Gal immobilized wells. The enzymatic activity was determined by following the absorption at 405 nm by the ester cleavage of PNPG. The observation was also carried out on cast it-PMMA films. Effects of film surfaces on the enzyme reaction were investigated. As a result, it was found that the enzymatic activity of the immobilized β-Gal on PMMA stereocomplex films was higher than that on cast it-PMMA films.

AB - Isotactic (it) and syndiotactic (st) poly(methyl methacrylate)s (PMMAs) form double-stranded helical stereocomplexes in organic solvents. We prepared PMMA stereocomplex films by a layer-by-layer assembly method on polystyrene microplate, and β-D-galactosidase (β-Gal) was immobilized on the PMMA stereocomplex film. Then, p-nitrophenyl-β-D-galactopyranoside (PNPG) solutions were added into the β-Gal immobilized wells. The enzymatic activity was determined by following the absorption at 405 nm by the ester cleavage of PNPG. The observation was also carried out on cast it-PMMA films. Effects of film surfaces on the enzyme reaction were investigated. As a result, it was found that the enzymatic activity of the immobilized β-Gal on PMMA stereocomplex films was higher than that on cast it-PMMA films.

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M3 - Paper

AN - SCOPUS:33749842693

SP - 2010

T2 - 55th SPSJ Annual Meeting

Y2 - 24 May 2006 through 26 May 2006

ER -

Immobilization and activity of enzymes on stereocomplex platforms

Abstract

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All Science Journal Classification (ASJC) codes

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