Immobilization of lipase B within micron-sized poly-N-isopropylacrylamide hydrogel particles by solvent exchange

Kornelia Gawlitza; Changzhu Wu; Radostina Georgieva; Dayang Wang; Marion B. Ansorge-Schumacher; Regine Von Klitzing

doi:10.1039/c2cp40624a

Immobilization of lipase B within micron-sized poly-N-isopropylacrylamide hydrogel particles by solvent exchange

Kornelia Gawlitza, Changzhu Wu, Radostina Georgieva, Dayang Wang, Marion B. Ansorge-Schumacher, Regine Von Klitzing^*

^*Corresponding author for this work

Research output: Contribution to journal › Journal article › Research › peer-review

Abstract

The aim of the present work is the use of a water soluble enzyme in an organic solvent, still with a pronounced catalytic activity. Therefore, lipase B from Candida antarctica (CalB) is immobilized within micron-sized thermosensitive p-NIPAM hydrogel particles using a solvent exchange from polar to organic solvents. The absorbed amount of CalB is investigated at different immobilization temperatures. Confocal laser scanning microscopy (CLSM) shows that CalB is homogeneously distributed within the polymer network. An enhanced specific activity of CalB in n-hexane is achieved after immobilization within the p-NIPAM microgels. In order to get information on the supply of the substrate depending on the temperature, the activity is determined at different reaction temperatures. Additionally, the system is stable in the organic solvent, namely n-hexane, and shows a good reusability. This journal is

Original language	English
Journal	Physical Chemistry Chemical Physics
Volume	14
Issue number	27
Pages (from-to)	9594-9600
ISSN	1463-9076
DOIs	https://doi.org/10.1039/c2cp40624a
Publication status	Published - 21. Jul 2012
Externally published	Yes

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10.1039/c2cp40624a

Cite this

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title = "Immobilization of lipase B within micron-sized poly-N-isopropylacrylamide hydrogel particles by solvent exchange",

abstract = "The aim of the present work is the use of a water soluble enzyme in an organic solvent, still with a pronounced catalytic activity. Therefore, lipase B from Candida antarctica (CalB) is immobilized within micron-sized thermosensitive p-NIPAM hydrogel particles using a solvent exchange from polar to organic solvents. The absorbed amount of CalB is investigated at different immobilization temperatures. Confocal laser scanning microscopy (CLSM) shows that CalB is homogeneously distributed within the polymer network. An enhanced specific activity of CalB in n-hexane is achieved after immobilization within the p-NIPAM microgels. In order to get information on the supply of the substrate depending on the temperature, the activity is determined at different reaction temperatures. Additionally, the system is stable in the organic solvent, namely n-hexane, and shows a good reusability. This journal is",

author = "Kornelia Gawlitza and Changzhu Wu and Radostina Georgieva and Dayang Wang and Ansorge-Schumacher, {Marion B.} and Klitzing, {Regine Von}",

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doi = "10.1039/c2cp40624a",

language = "English",

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T1 - Immobilization of lipase B within micron-sized poly-N-isopropylacrylamide hydrogel particles by solvent exchange

AU - Gawlitza, Kornelia

AU - Wu, Changzhu

AU - Georgieva, Radostina

AU - Wang, Dayang

AU - Ansorge-Schumacher, Marion B.

AU - Klitzing, Regine Von

PY - 2012/7/21

Y1 - 2012/7/21

N2 - The aim of the present work is the use of a water soluble enzyme in an organic solvent, still with a pronounced catalytic activity. Therefore, lipase B from Candida antarctica (CalB) is immobilized within micron-sized thermosensitive p-NIPAM hydrogel particles using a solvent exchange from polar to organic solvents. The absorbed amount of CalB is investigated at different immobilization temperatures. Confocal laser scanning microscopy (CLSM) shows that CalB is homogeneously distributed within the polymer network. An enhanced specific activity of CalB in n-hexane is achieved after immobilization within the p-NIPAM microgels. In order to get information on the supply of the substrate depending on the temperature, the activity is determined at different reaction temperatures. Additionally, the system is stable in the organic solvent, namely n-hexane, and shows a good reusability. This journal is

AB - The aim of the present work is the use of a water soluble enzyme in an organic solvent, still with a pronounced catalytic activity. Therefore, lipase B from Candida antarctica (CalB) is immobilized within micron-sized thermosensitive p-NIPAM hydrogel particles using a solvent exchange from polar to organic solvents. The absorbed amount of CalB is investigated at different immobilization temperatures. Confocal laser scanning microscopy (CLSM) shows that CalB is homogeneously distributed within the polymer network. An enhanced specific activity of CalB in n-hexane is achieved after immobilization within the p-NIPAM microgels. In order to get information on the supply of the substrate depending on the temperature, the activity is determined at different reaction temperatures. Additionally, the system is stable in the organic solvent, namely n-hexane, and shows a good reusability. This journal is

U2 - 10.1039/c2cp40624a

DO - 10.1039/c2cp40624a

M3 - Journal article

C2 - 22684227

SN - 1463-9076

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SP - 9594

EP - 9600

JO - Physical Chemistry Chemical Physics

JF - Physical Chemistry Chemical Physics

IS - 27

ER -

Immobilization of lipase B within micron-sized poly-N-isopropylacrylamide hydrogel particles by solvent exchange

Abstract

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