title: [Isolation of highly purified cyclodextrin glucanotransferase from Bacillus sp. 1070].
abstract: Two chromatographic processes for purification of cyclodextringlucanotransferase (CGTase) from Bacillus sp. 1070 was carried out. The enzyme has been purified into 9.5 times on Butyl-Toyopearl and followed immobilized metal ion chromatography on Cu(II)-Iminodiacetic (IDA)-agarose. By the application of second purification scheme (chromatography on Butyl-Toyopearl and DEAE-Sephacel) the specific activity of CGTase has folded into 13.5 times. The purity of enzyme was shown to be approximately 90% by SDS-electrophoreses data. It was shown that isolated enzyme has two isoelectric points estimated as 5.1 and 5.3.
authors.affiliation: Center of Bioengineering, RAS, Moscow, 117312.
authors.forename: D A
authors.initials: DA
authors.lastname: Volkova
authors.forename: S A
authors.initials: SA
authors.lastname: Lopatin
authors.forename: I M
authors.initials: IM
authors.lastname: Gracheva
authors.forename: V P
authors.initials: VP
authors.lastname: Varlamov
mesh_terms: D001407:Bacillus / Q000201:enzymology*; D002846:Chromatography, Affinity; D002852:Chromatography, Ion Exchange; D004591:Electrophoresis, Polyacrylamide Gel; D005964:Glucosyltransferases / Q000302:isolation & purification*; D007525:Isoelectric Focusing
chemical_list: D005964:Glucosyltransferases; C019963:cyclomaltodextrin glucanotransferase