α-Glucosidase and β-glucosidase from psychrotrophic strain arthrobacter sp. C2-2
E. Benešová, M. Marková, B. Králováhttps://doi.org/10.17221/3380-CJFSCitation:Benešová E., Marková M., Králová B. (2005): α-Glucosidase and β-glucosidase from psychrotrophic strain arthrobacter sp. C2-2. Czech J. Food Sci., 23: 116-120.
In this work six psychophilic and psychrotrophic bacterial strains were screened for the presence of different glycosidase activities (α-galactosidase, α-glucosidase, β-glucosidase, α-mannosidase and β-glucuronidase). Nine enzymes were found and their elementary characteristics were measured (toptimum, pHoptimum, Km, Vlim).Two enzymes with the highest activities at low temperatures were chosen for the next study, i.e. α-glucosidase and β-glucosidase from the psychrotrophic strain Arthrobacter sp. C2-2. These enzymes were purified by ammonium sulphate precipitation, by chromatography with hydrophobic interaction, and by ion-exchange chromatography. Their molecular weights (α-glucosidase – 76 kDa, β-glucosidase – 93 kDa) were determined by gel chromatography. In addition to this, it was verified that both of these enzymes are able to catalyse the transglycosylation reaction with the saccharidic donor and acceptor.Keywords:
cold-active enzyme; glycosidase; transglycosylation