[Isolation of highly purified cyclodextrin glucanotransferase from Bacillus sp. 1070].
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.
Volkova
D A
DA
Center of Bioengineering, RAS, Moscow, 117312.
Lopatin
S A
SA
Gracheva
I M
IM
Varlamov
V P
VP
D001407:Bacillus / Q000201:enzymology*; D002846:Chromatography, Affinity; D002852:Chromatography, Ion Exchange; D004591:Electrophoresis, Polyacrylamide Gel; D005964:Glucosyltransferases / Q000302:isolation & purification*; D007525:Isoelectric Focusing
D005964:Glucosyltransferases; C019963:cyclomaltodextrin glucanotransferase