Purification and characterization of an alkaline cellulase from a newly isolated alkalophilic Bacillus sp. HSH-810.
An alkaline cellulase from Bacillus sp. HSH-810 was purified 8.7-fold with a 30% yield and a specific activity of 71 U mg(-1) protein. It was optimally active at pH 10 and 50 degrees C and was stable from pH 6 to 10 with more than 60% activity remaining after heating at 60 degrees C for 60 min. The molecular mass of cellulase was 80 kDa. It was inhibited by 50% by Fe3+ (1 mM) and Mn2+ (0.1 mM) but was relatively insensitive to Hg2+ and Pb2+ at 1 mM.
Kim
Ji-Yeon
JY
Genome Research Center, Inje University, Gimhae 621-749, Korea.
Hur
Sung-Ho
SH
Hong
Jeong-Hwa
JH
D001407:Bacillus / Q000201:enzymology*; D001709:Biotechnology / Q000379:methods*; D044602:Cellulases / Q000737:chemistry*; D004591:Electrophoresis, Polyacrylamide Gel; D006863:Hydrogen-Ion Concentration; D007477:Ions; D007501:Iron / Q000737:chemistry; D007854:Lead / Q000737:chemistry; D008345:Manganese / Q000737:chemistry; D008628:Mercury / Q000737:chemistry; D008670:Metals; D008970:Molecular Weight; D013045:Species Specificity; D013696:Temperature; D013997:Time Factors
D007477:Ions; D008670:Metals; D007854:Lead; D008345:Manganese; D007501:Iron; D044602:Cellulases; D008628:Mercury