Preparation of thermally stable enzyme with high dispersion stability

Hiroko Ishikawa; Michihiro Iijima; Keishi Nishio; Motoi Oishi; Yukio Nagasaki

Preparation of thermally stable enzyme with high dispersion stability

Hiroko Ishikawa, Michihiro Iijima, Keishi Nishio, Motoi Oishi, Yukio Nagasaki

Department of Materials Science and Technology

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

Abstract

The lipase coupled silica colloid was prepared in the presence of PEG/oligocation block copolymers. The both dispersion and thermal stability of the lipase-silica colloid modified with PEG/oligocation were improved significantly. Actually, the initial enzymatic activity was retained after 5-fold treatments at 58°C for 10 min., though the native free lipase loosed its activity almost completely after only the once thermal treatment. In addition, the lyophilized complex was resolubilized easily in aqueous media, retaining its activity. PEG tethered chains on the lipase-adsorbed silica colloid may play an important role for the stable complex. Such the stable complex is promising for biomedical materials.

Original language	English
Number of pages	1
Publication status	Published - 19 Oct 2006
Event	55th SPSJ Annual Meeting - Nagoya, Japan Duration: 24 May 2006 → 26 May 2006

Conference

Conference	55th SPSJ Annual Meeting
Country/Territory	Japan
City	Nagoya
Period	24/05/06 → 26/05/06

Keywords

Immobilized-enzyme
Lipase
PEGylated colloidal silica
Recycling
Thermal stabilization

Cite this

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title = "Preparation of thermally stable enzyme with high dispersion stability",

abstract = "The lipase coupled silica colloid was prepared in the presence of PEG/oligocation block copolymers. The both dispersion and thermal stability of the lipase-silica colloid modified with PEG/oligocation were improved significantly. Actually, the initial enzymatic activity was retained after 5-fold treatments at 58°C for 10 min., though the native free lipase loosed its activity almost completely after only the once thermal treatment. In addition, the lyophilized complex was resolubilized easily in aqueous media, retaining its activity. PEG tethered chains on the lipase-adsorbed silica colloid may play an important role for the stable complex. Such the stable complex is promising for biomedical materials.",

keywords = "Immobilized-enzyme, Lipase, PEGylated colloidal silica, Recycling, Thermal stabilization",

author = "Hiroko Ishikawa and Michihiro Iijima and Keishi Nishio and Motoi Oishi and Yukio Nagasaki",

year = "2006",

month = oct,

day = "19",

language = "English",

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

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TY - CONF

T1 - Preparation of thermally stable enzyme with high dispersion stability

AU - Ishikawa, Hiroko

AU - Iijima, Michihiro

AU - Nishio, Keishi

AU - Oishi, Motoi

AU - Nagasaki, Yukio

PY - 2006/10/19

Y1 - 2006/10/19

N2 - The lipase coupled silica colloid was prepared in the presence of PEG/oligocation block copolymers. The both dispersion and thermal stability of the lipase-silica colloid modified with PEG/oligocation were improved significantly. Actually, the initial enzymatic activity was retained after 5-fold treatments at 58°C for 10 min., though the native free lipase loosed its activity almost completely after only the once thermal treatment. In addition, the lyophilized complex was resolubilized easily in aqueous media, retaining its activity. PEG tethered chains on the lipase-adsorbed silica colloid may play an important role for the stable complex. Such the stable complex is promising for biomedical materials.

AB - The lipase coupled silica colloid was prepared in the presence of PEG/oligocation block copolymers. The both dispersion and thermal stability of the lipase-silica colloid modified with PEG/oligocation were improved significantly. Actually, the initial enzymatic activity was retained after 5-fold treatments at 58°C for 10 min., though the native free lipase loosed its activity almost completely after only the once thermal treatment. In addition, the lyophilized complex was resolubilized easily in aqueous media, retaining its activity. PEG tethered chains on the lipase-adsorbed silica colloid may play an important role for the stable complex. Such the stable complex is promising for biomedical materials.

KW - Immobilized-enzyme

KW - Lipase

KW - PEGylated colloidal silica

KW - Recycling

KW - Thermal stabilization

UR - http://www.scopus.com/inward/record.url?scp=33749865412&partnerID=8YFLogxK

M3 - Paper

AN - SCOPUS:33749865412

T2 - 55th SPSJ Annual Meeting

Y2 - 24 May 2006 through 26 May 2006

ER -

Preparation of thermally stable enzyme with high dispersion stability

Abstract

Conference

Keywords

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