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학술연구/단체지원/교육 등 연구자 활동을 지속하도록 DBpia가 지원하고 있어요.
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연구자들이 자신의 연구와 전문성을 널리 알리고, 새로운 협력의 기회를 만들 수 있는 네트워킹 공간이에요.
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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.
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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