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Journal of the Korean Chemical Society (JKCS)

ISSN 1017-2548(Print)
ISSN 2234-8530(Online)
Volume 40, Number 1
JKCSEZ 40(1)
February 20, 1996 

 
Title
Purification and Some Properties of Chitinase from Serratia marcescens JM

Serratia marcescens JM에 의한 Chitinase의 정제와 특성
Author
Sang-Hwan Lee, Euy-Kyung Yu

이상환, 유의경
Keywords
Abstract
요 약. Chitinase를 생성하는 세균인 Serratia marcescens JM을 해안 갯벌 시료로부터 분리하여, ammonium sulfate precipitation, affinity adsorption, hydroxylapatite와 Sephadex G-200 column chromatography를 통하여 정제하였다. 정제된 Chitinase는 7.1% 회수율과 42.2 의 정제도를 나타내었으며, 전기 영동시 단일 밴드를 얻을 수 있었고, SDS-PAGE에 의해 측정된 분자량은 59,000으로 나타났다. 정제된 chitinase의 Km과 Vmax는 5.17mg/mL와 39.8 unit/mL로 나타났다. Chitinase의 최적활성 pH와 온도는 7과 50℃ 이하에서는 안정하였다. Cu2+, Ca2+ 및 Mg2+ 는 효소활성을 증가시켰으나, Hg2+와 I2는 효소활성을 억제시켰다. 또한. cysteine은 효소활성을 증가시키나 EDTA, MIA, PCMB 및 SDS는 효소활성을 약간 증가시켰으나 Na+이온은 1mM이상 농도에서 활성이 억제 되었다. 본 논문에서 정제된 chitinase는 여러가지 특이점이 있는 Serratia 효소 였다.

A chitinase-producing bacterium, Serratia marcescens JM, was isolated from a seashore muds. A chitinase was purified by ammonium sulfate precipitation, affinity adsorption, hydroxylapatite and sephadex G-200 column chromatography. The chitinase obtained from Serratia marcescens JM was purified 42.2 folds with the overall yield of 7.1%. The purified chitinase showed a single band on sodium dodecyl sulfate polyacrylamide gel electrophoresis. The molecular weight of the enzyme was 59,000 and the apparent kinetic parameters Km and Vmax for the purified chitinase were 5.17 mg/mL and 39.8 unit/mL, respectively. The optimum pH and temperature of the purified chitinase were 7.0 and 50℃, respectively and the purified enzyme was stable on pH 7.0 up to 50℃. The enzyme were activated by Cu2+, Ca2+ and Mg2+ and inhibited by Hg2+ respectively. In addition, Cysteine increased the chitinase activity and EDTA, MIA, PCMB and SDS inhibited enzyme activities. Major cations, Mg2+, Ca2+, K+ and Na+ present in seawater slightly stimulated the chitinase activity.

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72 - 80
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