Characterization of Clostridium paraputrificum Chitinase A from a Recombinant Escherichia coli

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概要

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• Clostridium paraputrificum chitinase A (ChiA) was purified from a recombinant Escherichia coli. ChiA was active toward chitin from crab shells, colloidal chitin, glycol chitin, and 4-methyl-umbelliferyl β-D-N, N'-diacetylchitobioside [4-MU-(GlcNAc)_2]. ChiA showed maximum activity at pH 6.0 and its optimum temperature was 45℃. ChiA was stable between pH6.0 and 9.0 and at temperatures up to 40℃. The K_m and V_<max> values of ChiA for 4-MU-(GleNAc)_2 were estimated to be 6.9 μM and 43 μmol/min/mg, respectively. Thin-layer chromatography indicated that ChiA hydrolyzes chitooligosaccharides to mainly chitobiose. ChiA was found to adsorb not only chitinous polymers but also cellulosic polymers.

• 社団法人日本生物工学会の論文
• 2001-11-25

著者

• Ohmiya K

  Graduate School Of Bioresources Mie Univ.

• Ohmiya Kunio

  Faculty Of Bioresources Mie University

• KIMURA Tetsuya

  Faculty of Bioresources, Mie University

• Kajino T

  Special Research Laboratory Ii Toyota Central R&d Laboratories Inc.

• Morimoto K

  Faculty Of Agriculture Kagawa University

• Karita Shuichi

  Faculty of Bioresources, Mie University

• MORIMOTO Kenji

  Faculty of Bioresources, Mie University

• SAKKA Kazuo

  Faculty of Bioresources, Mie University

• Morimoto Kenji

  Faculty Of Agriculture Kagawa University

• Morimoto Kenji

  Rare Sugar Research Center Faculty Of Agriculture Kagawa University

• Sakka Kazuo

  Faculty Of Bioresources Mie University

• Karita Shuichi

  Faculty Of Bioresources Mie University

• Kimura Tetsuya

  Graduate School Of Bioresources Mie University

• Kimura Tetsuya

  Faculty Of Bioresources Mie University

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