Purification and characterization of a novel endo-beta-1,4-glucanase from the thermoacidophilic Aspergillus terreus.
An endo-beta-1,4-glucanase from a thermoacidophilic fungus, Aspergillus terreus M11, was purified 18-fold with 14% yield and a specific activity of 67 U mg(-1) protein. The optimal pH was 2 and the cellulase was stable from pH 2 to 5. The cellulase had a temperature optimum of 60 degrees C measured over 30 min and retained more than 60% of its activity after heating at 70 degrees C for 1 h. The molecular mass of the cellulase was about 25 kDa. Its activity was inhibited by 77% by Hg(2+) (2 mM) and by 59% by Cu(2+) (2 mM).
Gao
Jianmin
J
Department of Bioengineering, Zhengzhou University, 100 Kexue Road, Zhengzhou 450001, PR China.
Weng
Haibo
H
Xi
Yu
Y
Zhu
Daheng
D
Han
Shaoyin
S
D001230:Aspergillus / Q000201:enzymology*; D002480:Cellulase / Q000737:chemistry* / Q000302:isolation & purification*; D006863:Hydrogen-Ion Concentration; D013696:Temperature
D002480:Cellulase