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CE analysis of single wood cells performing hydrolysis and preconcentration inopen micro channels
KTH, School of Chemical Science and Engineering (CHE), Chemistry, Analytical Chemistry.ORCID iD: 0000-0003-3548-217X
KTH, School of Chemical Science and Engineering (CHE), Chemistry, Analytical Chemistry.ORCID iD: 0000-0002-3444-9987
(English)Manuscript (preprint) (Other academic)
National Category
Analytical Chemistry
Identifiers
URN: urn:nbn:se:kth:diva-27609OAI: oai:DiVA.org:kth-27609DiVA: diva2:377528
Note
QC 20101214Available from: 2010-12-14 Created: 2010-12-14 Last updated: 2010-12-14Bibliographically approved
In thesis
1. Improved techniques for CE and MALDI-MS including microfluidic hyphenations foranalysis of biomolecules
Open this publication in new window or tab >>Improved techniques for CE and MALDI-MS including microfluidic hyphenations foranalysis of biomolecules
2011 (English)Doctoral thesis, comprehensive summary (Other academic)
Abstract [en]

In this thesis, improved techniques for biomolecule analysis using capillary electrophoresis (CE) and matrix-assisted laser desorption/ionization-mass spectrometry (MALDI-MS) and hyphenations between those have been presented.A pre-concentration method which is possible to apply in both techniques, has also been investigated.

In this work the off-line MS mode has been used either in the form of fractionation (Paper I) or by incorporating the MALDI target in the CE separation system (Paper II).In Paper I, a protocol for CE-MALDI analysis of cyanogen bromide digested bacteriorhodopsin (BR) peptides as model integral membrane protein peptides were established. Also, an improved protocol for partially automated manufacturing of a concentration MALDI-target plate is presented. The design of the targets was suitable for the fractions from the CE.

A novel technique for the integration of CE to MALDI-MS using a closed-open-closed system is presented in Paper II, where the open part is a micro canal functioning as a MALDI target window. A protein separation was obtained and detected with MALDI-MS analysis in the micro canal.

A method has been developed for detection of monosaccharides originating from hydrolysis of a single wood fiber performed in a micro channel, with an incorporated electromigration pre-concentration step preceding CE analysis in Paper III. The pre-concentration showed to be highly complex due to the fact that several parameters are included that affecting each other.

In Paper IV a protocol using enzymatic digestion, MALDI-TOF-MS and CE with laser induced fluorescence (LIF) detection for the investigation of the degree of substitution of fluorescein isothiocyanate (FITC) to bovine serum albumin (BSA), as a contact allergen model system for protein-hapten binding in the skin, is presented. The intention of a further CE-MALDI hyphenation has been considered during the work.

In Paper V 2,6-dihydroxyacetophenone (DHAP) was investigated, showing promising MALDI-MS matrix properties for hydrophobic proteins and peptides. 2,5-dihydroxybenzoic acid (DHB) was undoubtedly the better matrix for the hydrophilic proteins, but its performance for the larger and hydrophobic peptides was not optimal. Consequently, DHAP can be used as a compliment matrix for improved analysis of hydrophobic analytes.

Place, publisher, year, edition, pages
Stockholm: KTH, 2011. Xii, 85 p.
Series
Trita-CHE-Report, ISSN 1654-1081 ; 2011.1
Keyword
Capillary electrophoresis, Hydrophobic peptides/proteins, Matrix-Assisted Laser Desorption Ionization Mass Spectrometry, Prestructured target, Off-line interface, Silicon micro canal, Matrix, Peptide-fluorescein isothiocyanate adducts, Bovine serum albumin, DHAP, Hyphenations, Hydrophobicity, Single wood fiber analysis, Pre-concentration, Concentration platform
National Category
Analytical Chemistry
Identifiers
urn:nbn:se:kth:diva-27342 (URN)978-91-7415-808-3 (ISBN)
Public defence
2011-01-21, F3, Lindstedtsvägen 26, Stockholm, 10:00 (Swedish)
Opponent
Supervisors
Note
QC 20101214Available from: 2010-12-14 Created: 2010-12-10 Last updated: 2011-02-02Bibliographically approved

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Jacksén, JohanEmmer, Åsa

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