Enzymes That Hydrolyze Fungal Cell Wall Polysaccharides I. PURIFICATION AND PROPERTIES OF AN ENDO-α-d-(1 → 3)-GLUCANASE FROM TRICHODERMA VIRIDE
Enzymes That Hydrolyze Fungal Cell Wall Polysaccharides I. PURIFICATION AND PROPERTIES OF AN ENDO-α-d-(1 → 3)-GLUCANASE FROM TRICHODERMA VIRIDE
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水解真菌细胞壁多糖的酶 I. 绿色木霉 ENDO-α-d-(1 → 3)-葡聚糖酶的纯化及其性质
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发表时间：
1969
期刊：
影响因子：
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通讯作者：
S. Kirkwood
中科院分区：
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作者：
S. Hasegawa;J. H. Nordin;S. Kirkwood
从纤维素分解真菌绿色木霉（Trichoderma viride）的培养滤液中分离纯化出一种能水解多种α-（1 → 3）-葡聚糖的内切-α-d-（1 → 3）-葡聚糖酶，并对其专一性进行了研究。在所测试的化合物中，仅具有α-（1 → 3）-糖苷键的化合物受到攻击，并且酶促水解发生，同时保留参与裂解的异头碳原子的构型。研究了该酶的一些性质。最适pH为4.5，最适温度为50 ℃。标准测定条件下的Km和Vmax值为4.6 x 10-2 m葡萄糖当量和0.16 µ mol葡萄糖当量/min。通过Sephadex G-100柱色谱法估计的酶分子量约为47，000。Zn ~（++）和Fe ~（++）是酶的可逆抑制剂，而Ag ~（++）和Hg ~（++）则不可逆地抑制酶的活性。这种酶在结构碳水化合物化学中的应用进行了讨论。
Abstract An endo-α-d-(1 → 3)-glucanase capable of hydrolyzing various α-(1 → 3)-glucans has been isolated and purified from the culture filtrate of the cellulolytic fungus Trichoderma viride, and its specificity has been examined. Of the compounds tested only those with α-(1 → 3)-glucosidic linkages were attacked, and the enzymatic hydrolysis occurred with retention of configuration of the anomeric carbon atom involved in cleavage. Some properties of the enzyme have been investigated. Optimum pH and temperature for activity are 4.5 and 50°, respectively. The values of Km and Vmax under standard assay conditions are 4.6 x 10-2 m glucose equivalents and 0.16 µmole of glucose equivalent per min. The molecular weight of the enzyme estimated by column chromatography on Sephadex G-100 was found to be approximately 47,000. Zn++ and Fe++ were found to be reversible inhibitors of the enzyme while Ag+ and Hg+ abolished activity irreversibly. The use of this enzyme in structural carbohydrate chemistry is discussed.