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

張勝祺(Shenq-Chyi Chang) ； 周慧琴(Hui-Chin Chou) ； 鄭閔魁(Min-Kuei Cheng) ； 魏玎玲(Ding-Ling Wei)

《Fungal Science》 20卷3&4期 (2005/12) Pp. 105-112

https://doi.org/10.7099/FS.200512.0105

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。

關鍵字

β-木糖苷酵素 ； 炭角菌株Xylaria regalis 76072314

並列摘要

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+).

並列關鍵字

β-xylosidase ； Xylaria regalis 76072314