Abstract
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.
| Original language | English |
|---|---|
| Pages (from-to) | 733-738 |
| Number of pages | 6 |
| Journal | World Journal of Microbiology and Biotechnology |
| Volume | 21 |
| Issue number | 5 |
| DOIs | |
| Publication status | Published - 2005 Jul 1 |
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All Science Journal Classification (ASJC) codes
- Biotechnology
- Physiology
- Applied Microbiology and Biotechnology
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Purification and characterization of a thermostable chitinase from Bacillus licheniformis Mb-2. / Toharisman, Aris; Suhartono, Maggy Thenawidjaja; Spindler-Barth, Margarethe; Hwang, Jae-Kwan; Pyun, Yu Ryang.
In: World Journal of Microbiology and Biotechnology, Vol. 21, No. 5, 01.07.2005, p. 733-738.Research output: Contribution to journal › Article
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 - 2005/7/1
Y1 - 2005/7/1
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
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 -