TY - JOUR
T1 - Purification and characterization of a thermostable chitinase from Bacillus licheniformis Mb-2
AU - Toharisman, Aris
AU - Suhartono, Maggy Thenawidjaja
AU - Spindler-Barth, Margarethe
AU - Hwang, Jae Kwan
AU - Pyun, Yu Ryang
PY - 2005/7
Y1 - 2005/7
N2 - A chitinase produced by Bacillus licheniformis MB-2 isolated from Tompaso geothermal springs, Indonesia, was purified and characterized. The extracellular enzyme was isolated by successive hydrophobic interaction, anion exchange, and gel filtration chromatographies. The purified enzyme was a monomer with an apparent molecular weight of 67 kDa. The optimal temperature and pH of the enzyme were 70°C and 6.0, respectively. It was stable below 60°C for 2 h and over a broad pH range of 4.0-11.0 for 4 h. The enzyme was resistant to denaturation by urea (1 M), Tween-20 (1%) and Triton-X (1%), but unstable toward organic solvents such as dimethyl sulphoxide, DMSO, (5%) and polyethylene glycol, PEG, (5%) for 30 min. The enzyme hydrolysed colloidal chitin, glycol chitin, chitosan, and glycol chitosan. The first 13 N-terminal amino acids of the enzyme were determined as SGKNYKIIGYYPS, which is identical to those in chitinases from B. licheniformis and B. circulans.
AB - A chitinase produced by Bacillus licheniformis MB-2 isolated from Tompaso geothermal springs, Indonesia, was purified and characterized. The extracellular enzyme was isolated by successive hydrophobic interaction, anion exchange, and gel filtration chromatographies. The purified enzyme was a monomer with an apparent molecular weight of 67 kDa. The optimal temperature and pH of the enzyme were 70°C and 6.0, respectively. It was stable below 60°C for 2 h and over a broad pH range of 4.0-11.0 for 4 h. The enzyme was resistant to denaturation by urea (1 M), Tween-20 (1%) and Triton-X (1%), but unstable toward organic solvents such as dimethyl sulphoxide, DMSO, (5%) and polyethylene glycol, PEG, (5%) for 30 min. The enzyme hydrolysed colloidal chitin, glycol chitin, chitosan, and glycol chitosan. The first 13 N-terminal amino acids of the enzyme were determined as SGKNYKIIGYYPS, which is identical to those in chitinases from B. licheniformis and B. circulans.
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U2 - 10.1007/s11274-004-4797-1
DO - 10.1007/s11274-004-4797-1
M3 - Article
AN - SCOPUS:23044471027
VL - 21
SP - 733
EP - 738
JO - Mircen Journal of Applied Microbiology and Biotechnology
JF - Mircen Journal of Applied Microbiology and Biotechnology
SN - 0265-0762
IS - 5
ER -