Endre søk
RefereraExporteraLink to record
Permanent link

Direct link
Referera
Referensformat
  • apa
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Annet format
Fler format
Språk
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Annet språk
Fler språk
Utmatningsformat
  • html
  • text
  • asciidoc
  • rtf
Rational engineering of CALB for selective monoacylation of diols
KTH, Skolan för bioteknologi (BIO), Biokemi.
KTH, Skolan för bioteknologi (BIO), Biokemi.
(engelsk)Manuskript (preprint) (Annet vitenskapelig)
Identifikatorer
URN: urn:nbn:se:kth:diva-13820OAI: oai:DiVA.org:kth-13820DiVA, id: diva2:327474
Merknad
QC20100629Tilgjengelig fra: 2010-06-29 Laget: 2010-06-29 Sist oppdatert: 2010-06-29bibliografisk kontrollert
Inngår i avhandling
1. Serine Hydrolase Selectivity: Kinetics and applications in organic and analytical chemistry
Åpne denne publikasjonen i ny fane eller vindu >>Serine Hydrolase Selectivity: Kinetics and applications in organic and analytical chemistry
2010 (engelsk)Doktoravhandling, med artikler (Annet vitenskapelig)
Abstract [en]

The substrate selectivities for different serine hydrolases were utilized in various applications, presented in papers I-VI. The articles are discussed in the thesis in view of the kinetics of the enzyme catalysis involved.

In paper I the enantioselectivities towards a range of secondary alcohols were reversed for Candida antarctica lipase B by site directed mutagenesis. The thermodynamic components of the enantioselectivity were determined for the mutated variant of the lipase.

In papers II-III Candida antarctica lipase B was engineered for selective monoacylation using two different approaches. A variant of the lipase created for substrate assisted catalysis (paper II) and three different variants with mutations which decreased the volume of the active site (paper III) were evaluated. Enzyme kinetics for the different variants were measured and translated into activation energies for comparison of the approaches.

In papers IV and V three different enzymes were used for rapid analysis of enantiomeric excess and conversion of O-acylated cyanohydrins synthesized by a defined protocol. Horse liver alcohol dehydrogenase, Candida antarctica lipase B and pig liver esterase were sequentially added to a solution containing the O-acylated cyanohydrin. Each enzyme caused a drop in absorbance from oxidation of NADH to NAD+. The product yield and enantiomeric excess was calculated from the relative differences in absorbance.

In paper VI a method for C-terminal peptide sequencing was developed based on conventional Carboxypeptidase Y digestion combined with matrix assisted laser desorption/ionization mass spectrometry. An alternative nucleophile was used to obtain a stable peptide ladder and improve sequence coverage.

sted, utgiver, år, opplag, sider
Stockholm: KTH, 2010. s. viii, 62
Serie
Trita-BIO-Report, ISSN 1654-2312 ; 2010:12
Emneord
Candida antarctica lipase B, monoacylation of diols, kinetic resolution, thermodynamics in enzyme catalysis, enzyme engineering
HSV kategori
Identifikatorer
urn:nbn:se:kth:diva-12831 (URN)978-91-7415-663-8 (ISBN)
Disputas
2010-06-04, FD5, AlbaNova University Center, Roslagstullsbacken 21, Stockholm, 15:42 (engelsk)
Opponent
Veileder
Merknad
QC20100629Tilgjengelig fra: 2010-05-24 Laget: 2010-05-12 Sist oppdatert: 2010-06-29bibliografisk kontrollert

Open Access i DiVA

Fulltekst mangler i DiVA

Søk i DiVA

Av forfatter/redaktør
Hamberg, AndersHult, Karl
Av organisasjonen

Søk utenfor DiVA

GoogleGoogle Scholar

urn-nbn

Altmetric

urn-nbn
Totalt: 96 treff
RefereraExporteraLink to record
Permanent link

Direct link
Referera
Referensformat
  • apa
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Annet format
Fler format
Språk
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Annet språk
Fler språk
Utmatningsformat
  • html
  • text
  • asciidoc
  • rtf