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A chitinase was purified from the culture supernatant of Paenibacillus illinoisensis KJA-424 by protein precipitation, DEAE-Sephadex anion-exchange chromatography, and Sephadex G-150 gel filtration. The molecular weight of the purified chitinase was 54 kDa on SDS-PAGE and activity staining. Optimal pH and temperature were pH 5.0 and 60$^{circ}$C, the presence of 10 ruM Ag$^{+}$ and Hg$^{2+}$ inhibited the activity by $92.1/%$ and $97.7/%$, and the K$_{m}$ and V$_{max}$ values were 1.12 mg chitin mrl and 1.48$\mu$mol GlcNAc min$^{-1}$, respectively. The enzyme hydrolyzed tetramer to dimer, pentamer to dimer and trimer, and hexamer to dimer, trimer and tetramer, indicating an endo-splitting mechanism. The chitinase had no hydrolytic activity toward dimer and trimer. The chitinase inhibited the mycelial growth of Rhizoctonia solani, suggesting an antifungal property.

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이 논문을 인용한 문헌 (4)

  1. 2006. "" Journal of microbiology and biotechnology, 16(10): 1650~1655 
  2. 2007. "" Journal of microbiology and biotechnology, 17(3): 474~480 
  3. 2007. "" Journal of microbiology and biotechnology, 17(5): 753~760 
  4. 2008. "" Journal of microbiology and biotechnology, 18(2): 189~193 


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