Patrick Adlercreutz

Learn More
Lipase-catalyzed ethanolysis of triolein was studied as a model for biodiesel production. Four lipases were immobilized on porous polypropylene, and ethanol-ysis reactions were carried out in methyl t-butyl ether. The reaction products were analyzed using gas chromatography. Three of the four lipases studied were efficient in the conversion of triolein to(More)
Unveiling the determinants for transferase and hydrolase activity in glycoside hydrolases would allow using their vast diversity for creating novel transglycosylases, thereby unlocking an extensive toolbox for carbohydrate chemists. Three different amino acid substitutions at position 220 of a GH1 β-glucosidase from Thermotoga neapolitana caused an increase(More)
BACKGROUND At present, the conversion of oils to biodiesel is predominantly carried out using chemical catalysts. However, the corresponding lipase-catalysed process has important advantages, which include mild reaction conditions and the possibility of using cheap, low quality feedstocks with a high free fatty acid content. Further increases in the(More)
The possibility of improving the physical quality of extruded fish feed using transglutaminase (TGase) treatment at different stages of the production process was investigated. The addition of TGase to the raw material mix and processing under high and medium moisture conditions significantly increased (p > 0.05) the durability, hardness and elasticity of(More)
Lipases and glycoside hydrolases have large similarities concerning reaction mechanisms. Acyl-enzyme intermediates are formed during lipase-catalyzed reactions and in an analogous way, retaining glycoside hydrolases form glycosyl-enzyme intermediates during catalysis. In both cases, the covalent enzyme intermediates can react with water or other(More)
In this work, we present the first XOS degrading glycoside hydrolase from Weissella, WXyn43, a two-domain enzyme from GH43. The gene was amplified from genomic DNA of the XOS utilizing Weissella strain 92, classified under the species-pair Weissella cibaria/W.confusa, and expressed in Escherichia coli. The enzyme is lacking a putative signal peptide and is,(More)
  • 1