Change search
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • 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
A colorimetric assay to rapidly determine the activities of lytic polysaccharide monooxygenases
KTH, School of Engineering Sciences in Chemistry, Biotechnology and Health (CBH), Chemistry, Glycoscience. KTH, School of Engineering Sciences in Chemistry, Biotechnology and Health (CBH), Centres, Wallenberg Wood Science Center.
KTH, School of Engineering Sciences in Chemistry, Biotechnology and Health (CBH), Chemistry, Glycoscience.ORCID iD: 0000-0001-5007-2705
KTH, School of Engineering Sciences in Chemistry, Biotechnology and Health (CBH), Protein Science, Affinity Proteomics. KTH, Centres, Science for Life Laboratory, SciLifeLab.
Show others and affiliations
2018 (English)In: Biotechnology for Biofuels, ISSN 1754-6834, E-ISSN 1754-6834, Vol. 11, no 215Article in journal (Refereed) Published
Abstract [en]

Lytic polysaccharide monooxygenase (LPMOs) are enzymes that catalyze the breakdown of polysaccharides in biomass and have excellent potential for biorefinery applications. However, their activities are relatively low, and methods to measure these activities are costly, tedious or often reflect only an apparent activity to the polysaccharide substrates. Here, we describe a new method we have developed that is simple to use to determine the activities of type-1 (C1-oxidizing) LPMOs. The method is based on quantifying the ionic binding of cations to carboxyl groups formed by the action of type-1 LPMOs on polysaccharides. It allows comparisons to be made of activities under different conditions.

Place, publisher, year, edition, pages
BMC, CAMPUS, 4 CRINAN ST, LONDON N1 9XW, ENGLAND , 2018. Vol. 11, no 215
Keywords [en]
Lytic polysaccharide monooxygenase, Enzyme assay, Biomass deconstruction
National Category
Bioenergy Biocatalysis and Enzyme Technology
Identifiers
URN: urn:nbn:se:kth:diva-232857DOI: 10.1186/s13068-018-1211-zISI: 000440537000001PubMedID: 30083228Scopus ID: 2-s2.0-85051124411OAI: oai:DiVA.org:kth-232857DiVA, id: diva2:1236758
Funder
Knut and Alice Wallenberg FoundationScience for Life Laboratory - a national resource center for high-throughput molecular bioscience
Note

QC 20180814

Available from: 2018-08-05 Created: 2018-08-05 Last updated: 2018-08-14Bibliographically approved

Open Access in DiVA

fulltext(3003 kB)57 downloads
File information
File name FULLTEXT01.pdfFile size 3003 kBChecksum SHA-512
77781509fe6ea05a96f2d7c200ea06430729926f2916e8aa8cc1cf917be19b04ed3f0fee54232097173112f83ce29b63489eb6d73f1413a11fb52ce1ae056972
Type fulltextMimetype application/pdf

Other links

Publisher's full textPubMedScopus

Authority records BETA

Li, JingHsieh, Yves S. Y.

Search in DiVA

By author/editor
Wang, DamaoLi, JingWong, Ann C. Y.Hsieh, Yves S. Y.
By organisation
GlycoscienceWallenberg Wood Science CenterAffinity ProteomicsScience for Life Laboratory, SciLifeLab
In the same journal
Biotechnology for Biofuels
BioenergyBiocatalysis and Enzyme Technology

Search outside of DiVA

GoogleGoogle Scholar
Total: 57 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
pubmed
urn-nbn

Altmetric score

doi
pubmed
urn-nbn
Total: 1770 hits
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • 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