Purification and characterization of a thermostable chitinase from Bacillus licheniformis Mb-2

Aris Toharisman, Maggy Thenawidjaja Suhartono, Margarethe Spindler-Barth, Jae Kwan Hwang, Yu Ryang Pyun

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74 Citations (Scopus)


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 languageEnglish
Pages (from-to)733-738
Number of pages6
JournalWorld Journal of Microbiology and Biotechnology
Issue number5
Publication statusPublished - 2005 Jul

All Science Journal Classification (ASJC) codes

  • Biotechnology
  • Physiology
  • Applied Microbiology and Biotechnology


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