Acid Xylanase from Yeast<i>Cryptococcus</i>sp. S-2: Purification, Characterization, Cloning, and Sequencing
書誌事項
- タイトル別名
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- Acid Xylanase from Yeast Cryptococcus sp. S-2: Purification, Characterization, Cloning, and Sequencing.
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抄録
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.
収録刊行物
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- Bioscience, Biotechnology, and Biochemistry
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Bioscience, Biotechnology, and Biochemistry 60 (8), 1331-1338, 1996
公益社団法人 日本農芸化学会
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詳細情報
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- CRID
- 1390282681453220992
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- NII論文ID
- 110002678255
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- NII書誌ID
- AA10824164
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- COI
- 1:CAS:528:DyaK28Xltlektbc%3D
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- ISSN
- 13476947
- 09168451
- http://id.crossref.org/issn/09168451
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- PubMed
- 8987553
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- 本文言語コード
- en
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- データソース種別
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- JaLC
- Crossref
- PubMed
- CiNii Articles
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- 使用不可