One-step isolation of a chitinase by affinity chromatography of the chitinolytic enzyme complex produced by Streptomyces kurssanovii.
One of the four chitinases with a molecular mass of 42 kDa existing in the chitinolytic enzyme complex produced by Streptomyces kurssanovii was separated in homogeneous form using one-step affinity chromatography on cross-linked and phosphorylated chitin-type sorbents. Three other chitinases were not selectively bound by the sorbents and were not obtained in homogeneous form. The affinity sorbents were shown to be stable over the time of separation and could be used repeatedly.
Ilyina
A V
AV
Center Bioengineering, Russian Academy of Sciences, Moscow.
Varlamov
V P
VP
Tikhonov
V E
VE
Yamskov
I A
IA
Davankov
V A
VA
D000327:Adsorption; D002688:Chitinases / Q000302:isolation & purification*; D002846:Chromatography, Affinity; D003432:Cross-Linking Reagents; D003470:Culture Media; D004591:Electrophoresis, Polyacrylamide Gel; D010766:Phosphorylation; D013302:Streptomyces / Q000201:enzymology*
D003432:Cross-Linking Reagents; D003470:Culture Media; D002688:Chitinases