Purification and partial characterization of ¦Â-glucanase produced by Trichoderma viride TP09 isolated from sewage of beer-making

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• 作者：Huaxi Yi ; Shanbai Xiong ; Ming Du and Lanwei Zhang
• 关键词：Trichoderma viride ; β ; Glucanase ; Enzyme purification
• 刊名：European Food Research and Technology
• 出版年：2008
• 出版时间：July, 2008
• 年：2008
• 卷：227
• 期：3
• 页码：821-826
• 全文大小：369.0 KB

文摘

As an initial investigation to improve the insoluble yeast β-1, 3-glucan solubility, a novel β-glucanase from Trichoderma viride TP09 was purified in the culture supernatant and partially characterized. By 70 % saturation ammonium sulfate and chromatography on DEAE-Sepharose CL-6B column, β-glucanase was purified 28.7-fold, with recovery of 45.2 % of the initial activity. The molecular weight of this enzyme was estimated to be 54.6 KD by SDS-PAGE. The optimum pH and the optimum temperature for the enzyme were 5.0 and 50 ¡ãC, respectively. The enzyme showed high stability within the range of pH 3.0–5.0 and thermostability between 30 and 70 ¡ãC. The enzyme activity was inhibited by Fe3+, Mg2+, Mn2+, Cu2+, and stimulated by Zn2+, Ca2+, Fe2+. Substrate specificity studies revealed the enzyme to be a β-1, 3–1, 4-glucanase. The β-glucanase showed preference for β-1, 3 linkage and β-1, 4 linkage, but had no activity on α-1, 4 and α-1, 6 linkage. The above results indicated that the enzyme extracted from T. viride TP09 of the beer-making sewage could be used as a potential predominant tool to enhance solubility of the insoluble yeast β-1, 3-glucan. These findings may lead to an enhanced solubility and expedite the progress of application in immunotherapy.