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題 名 | Purification and Characterization of β-xylosidase from an Isolated Xylaria regalis 76072314=臺灣分離之炭角菌株其β-木糖苷酵素之純化及其生化特性之探討 |
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作 者 | 張勝祺; 周慧琴; 鄭閔魁; 魏玎玲; | 書刊名 | 中華真菌學會會刊 |
卷 期 | 20:3/4 民94.12 |
頁 次 | 頁105-112 |
分類號 | 379.1 |
關鍵詞 | β-木糖苷酵素; 炭角菌株; β-xylosidase; Xylaria regalis 76072314; |
語 文 | 英文(English) |
中文摘要 | 從臺灣分離之炭角菌株(Xylaria regalis 76072314)產生之β-木糖苷酵素經由硫酸銨沉澱、疏水性管柱、離子交換樹脂管柱及分子篩膠體管柱之純化,得到最終產物活性提高23.0倍,回收率為24.2%。經由SDS-膠體電泳分析得知此酵素分子量為44.9 kDa;此外,本酵素最適反應溫度50℃,最適反應pH值5.5。測試金屬離子中只有Hg(上標 2+)及Fe(上標 2+)會抑制此酵素之活性,而EDTA或β-mercaptoothanol則不影響此酵素活性。 |
英文摘要 | An extracellular β-xylosidase was purified to homogeneity from the culture filtrate of Xylaria regalis 76072314. The β-xylosidase was purified 23.0 fold, giving a 24.2% yield. The crude enzyme was subjected to a series of the purification procedures, including, ammonium sulfate precipitation, hydrophobic interaction phenyl 650 M column, QAE Sephadex A-25 anion exchange column and Sephadex G-75 gel filtration column chromatography, respectively. The molecular mass of the purified β-xylosidase estimated by SDS-PAGE was 44.9 kDa. The optimal temperature of the enzyme activity was 50℃. The optimal pH of β-xylosidase activity was 5.5 and the enzyme appeared to be stable over the pH range from 5-9. The enzyme did not require any metal ion for activity and stability. Moreover, the β-xylosidase activity was inhibited by Hg(superscript 2+) and Fe(superscript 2+). |
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