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Temperature Controlled Activity of Lipase B from Candida Antarctica after Immobilization within p-NIPAM Microgel Particles
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Kornelia Gawlitza
Published/Copyright:
August 13, 2012
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.
Published Online: 2012-8-13
Published in Print: 2012-8-1
© by Oldenbourg Wissenschaftsverlag, München, Germany
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Keywords for this article
Lipase B;
p-NIPAM;
Immobilization;
Catalytic Activity;
Thermoresponsibility
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- Optimizing the Sensitivity of FT-Rheology to Quantify and Differentiate for the First Time the Nonlinear Mechanical Response of Dispersed Beer Foams of Light and Dark Beer
- Adsorption of Spherical Polyelectrolyte Brushes: from Interactions to Surface Patterning
- Complexation of charged colloids with polyelectrolyte stars
- Charging and Aggregation of Positively Charged Colloidal Latex Particles in Presence of Multivalent Polycarboxylate Anions
- Spherical Polyelectrolyte Brushes on Colloidal Poly(butadiene) Particles
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