liu.seSearch for publications in DiVA
Change search
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • harvard1
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • oxford
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf
Immobilization of lipase from Mucor miehei and Rhizopus oryzae into mesoporous silica - The effect of varied particle size and morphology
Chalmers University of Technology, Department of Chemical and Biological Engineering.
Linköping University, Department of Physics, Chemistry and Biology, Nanostructured Materials. Linköping University, The Institute of Technology.
Chalmers University of Technology, Department of Chemical and Biological Engineering.
Linköping University, Department of Physics, Chemistry and Biology, Nanostructured Materials. Linköping University, The Institute of Technology.ORCID iD: 0000-0002-2286-5588
Show others and affiliations
2012 (English)In: Colloids and Surfaces B: Biointerfaces, ISSN 0927-7765, E-ISSN 1873-4367, Vol. 100, 22-30 p.Article in journal (Refereed) Published
Abstract [en]

Immobilization of enzymes usually improves the recyclability and stability and can sometimes also improve the activity compared to enzymes free in solution. Mesoporous silica is a widely studied material as host for immobilized enzymes because of its large internal surface area and tunable pores. It has previously been shown that the pore size is critical both for the loading capacity and for the enzymatic activity; however, less focus has been given to the influence of the particle size. In this work the effect of particle size and particle morphology on the immobilization of lipase from Mucor miehei and Rhizopus oryzae have been investigated. Three kinds of mesoporous silica, all with 9 nm pores but with varying particle size (1000 nm, 300 nm and 40 nm) have been synthesized and were used as host for the lipases. The two lipases, which have the same molecular size but widely different isoelectric points, were immobilized into the silica particles at varied pH values within the interval 5 to 8. The 300 nm particles were proven to be the most suitable carrier with respect to specific activity for both enzymes. The lipase from Mucor miehei was more than four times as active when immobilized at pH 8 compared to free in solution whereas the difference was less pronounced for the Rhizopus oryzae lipase.

Place, publisher, year, edition, pages
Elsevier, 2012. Vol. 100, 22-30 p.
National Category
Other Materials Engineering
Identifiers
URN: urn:nbn:se:liu:diva-78683DOI: 10.1016/j.colsurfb.2012.04.042ISI: 000307683900004OAI: oai:DiVA.org:liu-78683DiVA: diva2:534743
Note

funding agencies|Nanolith Sverige AB||Swedish Research Council||

Available from: 2012-06-18 Created: 2012-06-18 Last updated: 2017-12-07

Open Access in DiVA

fulltext(753 kB)1182 downloads
File information
File name FULLTEXT01.pdfFile size 753 kBChecksum SHA-512
f9494c72e4bc915b8578b674249e76a94731c1721c8b8019a02a1ea10379dd0b9c90e942734da0c60a05170a1d432113a0f02909a78399050f79aa5ccdfc5fa8
Type fulltextMimetype application/pdf

Other links

Publisher's full text

Authority records BETA

Johannsson, EmmaOdén, Magnus

Search in DiVA

By author/editor
Johannsson, EmmaOdén, Magnus
By organisation
Nanostructured MaterialsThe Institute of Technology
In the same journal
Colloids and Surfaces B: Biointerfaces
Other Materials Engineering

Search outside of DiVA

GoogleGoogle Scholar
Total: 1182 downloads
The number of downloads is the sum of all downloads of full texts. It may include eg previous versions that are now no longer available

doi
urn-nbn

Altmetric score

doi
urn-nbn
Total: 157 hits
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • harvard1
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • oxford
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf