[논문]Purification and Characterization of Chitinase from Paenibacillus illinoisensis KJA-424

JUNG WOO JIN; KUK JU HEE; KIM KIL YONG; KIM TAE HWAN; PARK RO DONG

Purification and Characterization of Chitinase from Paenibacillus illinoisensis KJA-424 원문보기

Journal of microbiology and biotechnology, v.15 no.2, 2005년, pp.274 - 280

JUNG WOO JIN (Glucosamine Saccharide Materials-National Research Laboratory (GSM-NRL), Division of Applied Bioscience and Biotechnology Institute of Agricultural Science and Technology, Chonnam National University) , KUK JU HEE (Glucosamine Saccharide Materials-National Research Laboratory (GSM-NRL), Division of Applied Bioscience and Biotechnology Institute of Agricultural Science and Technology, Chonnam National University) , KIM KIL YONG (Glucosamine Saccharide Materials-National Research Laboratory (GSM-NRL), Division of Applied Bioscience and Biotechnology Institute of Agricultural Science and Technology, Chonnam National University) , KIM TAE HWAN (Department of Animal Science, College of Agriculture and Life Science, Chonnam National University) , PARK RO DONG (Glucosamine Saccharide Materials-National Research Laboratory (GSM-NRL), Division of Applied Bioscience and Biotechnology Institute of Agricultural Science and Technology, Chonnam National University)

Abstract ▼ AI-Helper

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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