Temperature Controlled Activity of Lipase B from Candida Antarctica after Immobilization within p-NIPAM Microgel Particles

Abstract The immobilization of lipase B from Candida antarctica (CalB) within micronsized poly- N -Isopropylacrylamide (p-NIPAM) microgel particles with a crosslinker content of 5% is reported. The immobilization of the enzyme was reached by an exchange from polar to organic solvents. After determin...

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Bibliographic Details
Published in:Zeitschrift für Physikalische Chemie
Main Authors: Gawlitza, Kornelia, Wu, Changzhu, Georgieva, Radostina, Ansorge-Schumacher, Marion, von Klitzing, Regine
Format: Article in Journal/Newspaper
Language:English
Published: Walter de Gruyter GmbH 2012
Subjects:
Physical and Theoretical Chemistry
Antarc*
Antarctica
Online Access:http://dx.doi.org/10.1524/zpch.2012.0271
https://www.degruyter.com/document/doi/10.1524/zpch.2012.0271/xml
https://www.degruyter.com/document/doi/10.1524/zpch.2012.0271/pdf
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Summary:Abstract The immobilization of lipase B from Candida antarctica (CalB) within micronsized poly- N -Isopropylacrylamide (p-NIPAM) microgel particles with a crosslinker content of 5% is reported. The immobilization of the enzyme was reached by an exchange from polar to organic solvents. After determining the embedded amount of CalB within the polymer network, an enhanced specific activity in n -hexane was obtained. Due to the thermoresponsibility of the polymer particles, the activity reaction was done at 25 ºC and 50 ºC. The results presented show that the reversible collapse of the microgel leads to a decreased activity with increasing temperature. Hence, p-NIPAM microgels display a good opportunity to tailor the activity of CalB. An interesting side effect is that CalB presents a suitable probe to estimate the mesh size of the polymer network, since it penetrates in the unlabeled form but not after labeling with FITC.

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