Purification and characterization of a high-thermostable β-xylanase from newly isolated Thermomyces lanuginosus THKU-49

DOI Web Site Web Site 参考文献21件

書誌事項

タイトル別名
  • Purification and characterization of a high-thermostable <i>β</i>-xylanase from newly isolated <i>Thermomyces lanuginosus</i> THKU-49
  • Purification and characterization of a high thermostable v xylanase from newly isolated Thermomyces lanuginosus THKU 49

この論文をさがす

抄録

<p>Highly thermostable β-xylanase produced by newly isolated Thermomyces lanuginosus THKU-49 strain was purified in a four-step procedure involving ammonium sulfate precipitation and subsequent separation on a DEAE-Sepharose fast flow column, hydroxylapatite column, and Sephadex G-100 column, respectively. The enzyme purified to homogeneity had a specific activity of 552 U/mg protein and a molecular weight of 24.9 kDa. The optimal temperature of the purified xylanase was 70°C, and it was stable at temperatures up to 60°C at pH 6.0; the optimal pH was 5.0–7.0, and it was stable in the pH range 3.5–8.0 at 4°C. Xylanase activity was inhibited by Mn2+, Sn2+, and ethylenediaminetetraacetic acid. The xylanase showed a high activity towards soluble oat spelt xylan, but it exhibited low activity towards insoluble oat spelt xylan; no activity was found to carboxymethylcellulose, avicel, filter paper, locust bean gum, cassava starch, and p-nitrophenyl β-D-xylopyranoside. The apparent Km value of the xylanase on soluble oat spelt xylan and insoluble oat spelt xylan was 7.3 ± 0.236 and 60.2 ± 6.788 mg/ml, respectively. Thin-layer chromatography analysis showed that the xylanase hydrolyzed oat spelt xylan to yield mainly xylobiose and xylose as end products, but that it could not release xylose from the substrate xylobiose, suggesting that it is an endo-xylanase.</p>

収録刊行物

  • Mycoscience

    Mycoscience 51 (6), 405-410, 2010

    一般社団法人 日本菌学会

参考文献 (21)*注記

もっと見る

キーワード

詳細情報 詳細情報について

問題の指摘

ページトップへ