Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Jakob Skjold-Jørgensen"'
Autor:
Jakob Skjold-Jørgensen, Allan Svendsen, Arne Stamm, Ida Berts, Thomas Vissing, Tommy Nylander
Publikováno v:
Chemistry and Physics of Lipids. 211:37-43
In spite of the importance of the triglyceride aqueous interface for processes like emulsification, surfactant interactions and lipase activity, relatively little is known about this interface compared to that between alkanes and water. Here, the con
Publikováno v:
European Journal of Lipid Science and Technology. 118:1644-1660
The attractiveness of lipases as industrial biocatalysts underlines the importance of understanding their molecular action in detail, helping future efforts to improve performance and applicability. Lipases represent a special class of carboxyl ester
Publikováno v:
Biochemistry. 55:146-156
Thermomyces lanuginosus lipase (TlL) and related lipases become activated in low-polarity environments that exist at the water-lipid interface where a structural change of the "lid" region occurs. In this work, we have investigated the activation of
Autor:
Jesper Vind, David L. Farrens, Vikram Kjoeller Bhatia, Allan Svendsen, Jakob Skjold-Jørgensen, Morten J. Bjerrum
Publikováno v:
Biochemistry. 54:4186-4196
Triacylglycerol hydrolases (EC 3.1.1.3) are thought to become activated when they encounter the water-lipid interface causing a "lid" region to move and expose the catalytic site. Here, we tested this idea by looking for lid movements in Thermomyces
Autor:
Allan Svendsen, Nathalie Willems, Mark S.P. Sansom, Jakob Skjold-Jørgensen, Mickaël Lelimousin
Lipases naturally function at the interface formed between amphiphilic molecules and the aqueous environment. Thermomyces lanuginosus lipase (TLL) is a well-characterised lipase, known to exhibit interfacial activation during which a lid region cover
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f9e56aa76982eee40053c495a4af7e76
https://ora.ox.ac.uk/objects/uuid:9907ccef-30a1-49b7-ac97-de86a094a7e1
https://ora.ox.ac.uk/objects/uuid:9907ccef-30a1-49b7-ac97-de86a094a7e1
Publikováno v:
Biochemistry. 53:4152-4160
It is shown by rational site-directed mutagenesis of the lid region in Thermomyces lanuginosus lipase that it is possible to generate lipase variants with attractive features, e.g., high lipase activity, fast activation at the lipid interface, abilit
Autor:
Morten J. Bjerrum, Keith S. Wilson, Elena Blagova, Allan Svendsen, Jesper Vind, Olga V. Moroz, Vikram Kjoeller Bhatia, Jakob Skjold-Jørgensen
Publikováno v:
Biochimica et biophysica acta. Proteins and proteomics. 1865(1)
Here, we present a lipase mutant containing a biochemical switch allowing a controlled opening and closing of the lid independent of the environment. The closed form of the TlL mutant shows low binding to hydrophobic surfaces compared to the binding