Acid Xylanase from Yeast Cryptococcus sp. S-2: Purification, Characterization, Cloning, and Sequencing
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概要
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A xylan-degrading enzyme produced by yeast Cryptococcus sp. S-2 was isolated and purified, and characterized as an endoxylanase (1,4-β-D-xylan xylanohydrolase [EC 3.2.1.8]). We estimated the molecular weight and isoelectric point of purified xylanase (xyn-CS2) to be 22,000 and 7.4, respectively. This low-molecular-weight xylanase had an unusual pH optimum of 2.0, and showed 75% of maximal activity even at pH 1.0. An open reading frame of the cDNA specified 209 amino acids, including a putative signal peptide of 25 amino acids. The deduced amino acid sequence of xyn-CS2 shared significant similarities with the family-G xylanases of B. pumilus, C acetobutylicum, T reesei, and A. kawachii. Xyn-CS2 included two unique cysteine residues in a putative catalytic region, raising the possibility that these residues are at least partially responsible for its acidophilic nature.
- 社団法人日本農芸化学会の論文
- 1996-08-23
著者
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Iefuji Haruyuki
National Research Institute of Brewing
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Iimura Yuzuru
National Research Institute of Brewing
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Iefuji Haruyuki
National Res. Inst. Of Brewing
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CHINO Mariko
National Research Institute of Brewing
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KATO Miyoshi
National Research Institute of Brewing
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Chino M
Kansai Univ. Osaka Jpn
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