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KMID : 0613820030130010090
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Journal of Life Science
2003 Volume.13 No. 1 p.90 ~ p.98
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Growth Inhibition of Sclerotium Cepivorum Causing Allium White Rot by Serratia plymuthica Producing Chitinase
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Kim Jin-Ho
Choi Yong-Hwa
Kang Sang-Jae
Kim Young-Hoon
Joo Gil-Jae
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Abstract
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An allium rhizobacterium Serratia plymuthica AL-1 was previously selected as a biocontrol agent of allium white rot. The chitinase from S. plymuthica AL-1 produced in medium containing colloidal chitin was purified by ammonium sulfate precipitation (40～70%), affinity adsorption, column chromatography on DEAE-sephadex A-50 and sephadex G-200 gel filtration. The enzyme was purified 10.8-fold with a yield of 7.3% from the starting culture broth. The
purified chtinase gave a single band on sodium dodecyl sulfate polyacrylamide gel electrophoresis, it’s molecular weight was estimated to be 55 kDa. The optimum pH and temperature of the purified enzyme were pH 5.5 and 55℃, respectively and it is stable up to 50℃ and maintains around 90% of its activity for 60min. The enzyme were activated by Ca²+, Mn²+ and Mg²+ and inhibited by Cu²+, SDS, p-CMB, MIA, respectively. The purified chitinase showed broad spectrum of antifungal activities against plant pathogenic fungi Sclerotium cepivorum, Alternaria alternata, Colletotrichum
gloeosporioides, Phoma sp., Sclerotinia sclerotiorum, Stemphylium solani, Fusarium oxysporium f. sp. niveum but rarely inhibited Phytophthora capsici and Pythium ultimum. The purified chitinase from S. plymuthica AL-1 caused swelling, lysis, decoloration and degradation of the hyphal tips of S. sclerotiorum causing allium white rot. It suggest that S. plymuthica AL-1 chitinase play an important part in the bifunctional chitinase / lysozyme activity.
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KEYWORD
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Allium, Sclerotium cepivorum, Serratia plymuthica, antagonistic bacterium, white rot, chitinase, purification
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