Purificaiton and Properties of Chitinase from Streptomyces cinereoruber
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概要
- 論文の詳細を見る
A chitinase(EC 3.2.1.14)was purified from the culture filtrate of Streptomyces cinereoruber, selected as a microorganism which produces enzymes lysing Aspergillus niger cell wall, by fractional precipitation with ammonium sulfate and column chromatographies on DEAE-cellulose, Sephadex G-100 and CM-Sephadex C-50. The final preparation was homogenous in polycrylamide gel disc electrophoresis. The molecular weight of the enzyme was about 19,000 daltons and its isoelectric point was pH 8.6. The optimum pH and temperature for chitinase activity were 4.5 and at 50℃, respectively. The enzyme was stable in the pH range from 4.0 to 10.0. The activity was inhibited by Ag^+, Hg^+, Hg^<2+> and p-chloromercuribenzoate. Paper chromatographic analysis demonstrated that the hydrolytic products of colloidal chitin and chitotriose with tye enzyme were N-acetylglucosamine and chitobiose. The lysis of A. niger cell wall with the enzyme is discussed.
- 公益社団法人日本生物工学会の論文
- 1991-04-25
著者
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Tagawa Kiyoshi
Department Of Bioresource Science Faculty Of Agriculture Kagawa University
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Okazaki Katsuichiro
Department Of Applied Biological Science Faculty Of Agriculture Kagawa University
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