English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
  Immobilization of water-soluble HRP within Poly-N-isopropylacrylamide microgel particles for use in organic media

Gawlitza, K., Georgieva, R., Tavraz, N., Keller, J., & von Klitzing, R. (2013). Immobilization of water-soluble HRP within Poly-N-isopropylacrylamide microgel particles for use in organic media. Langmuir, 29(51), 16002-16009. doi:10.1021/la403598s.

Item is

Files

show Files
hide Files
:
1921762.pdf (Publisher version), 2MB
 
File Permalink:
-
Name:
1921762.pdf
Description:
-
OA-Status:
Visibility:
Restricted (Max Planck Institute of Colloids and Interfaces, MTKG; )
MIME-Type / Checksum:
application/pdf
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
License:
-

Locators

show

Creators

show
hide
 Creators:
Gawlitza, Kornelia, Author
Georgieva, Radostina, Author
Tavraz, Neslihan, Author
Keller, Janos1, Author           
von Klitzing, Regine, Author
Affiliations:
1Gerald Brezesinski, Grenzflächen, Max Planck Institute of Colloids and Interfaces, Max Planck Society, ou_1863310              

Content

show
hide
Free keywords: -
 Abstract: In the present work, the immobilization of enzymes within poly-N-isopropylacrylamide (wp-NIPAM) microgels using the method of solvent exchange is applied to the enzyme horseradish peroxidase (HRP). When the solvent is changed from water to isopropanol, H RP is embedded within the polymer structure. After the determination of the immobilized amount of enzyme, an enhanced specific activity of the biocatalyst in isopropanol can be observed. Karl Fischer titration is used to determine the amount of water within the microgel particles before and after solvent exchange, leading to the conclusion that an "aqueous cage" remains within the polymer structure. This represents the driving force for the immobilization due to the high affinity of HRP for water. Beside, confocal laser scanning microscopy (CLSM) images show that HRP is located within the microgel network after immobilization. This gives the best conditions for HRP to be protected against chemical and mechanical stress. We were able to transfer a water-soluble enzyme to an organic phase by reaching a high catalytic activity. Hence, the method of solvent exchange displays a general method for immobilizing enzymes within p-NIPAM microgels for use in organic solvents. With this strategy, enzymes that are not soluble in organic solvents such as HRP can be used in such polar organic solvents.

Details

show
hide
Language(s):
 Dates: 2013
 Publication Status: Issued
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: -
 Identifiers: ISI: 000329137000032
DOI: 10.1021/la403598s
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: Langmuir
  Abbreviation : Langmuir
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: Columbus, OH : American Chemical Society
Pages: - Volume / Issue: 29 (51) Sequence Number: - Start / End Page: 16002 - 16009 Identifier: ISSN: 0743-7463