木霉4131菌株纤维素酶的分离纯化和部分性质研究

Studies on the Purification and Properties of Cellulase from Trichoderma Mutant Strain 4131

绿色木霉（ＴｒｉｃｈｏｄｅｒｍａＶｉｒｉｄｅ）突变菌株４１３１［１］产生的纤维素酶经过ｓｅｐｈａｄｅｘＧ－７５和ＤＥＡＥ－ｓｅｐｈａｄｅｘＡ－２５两种层析分离，分离得到具有内切β－葡聚糖酶（ＣＭＣａｓｅ）活性的纯组分，提纯后酶的比活力提高到原来的２６．２倍，回收率为３２．８％，分子量为５６９００，等电点为４．０，最适反应温度为５５℃，最适ｐＨ为４．５，金属离子Ｋ＋，Ｎａ＋，Ｃａ２＋，Ｍｇ２＋对其具有一定的激活作用，Ｈｇ２＋，Ａｇ＋，Ｆｅ３＋，Ｚｎ２＋等具有不同程度的抑制作用．

A cellulase was isolated and purified from Trichoderma Viride mutant strain 4131, by means of ammonium sulfate precipitation, followed by chromatography on sephadex G 75 and DEAE sephadex A 25. Analyses showed that the purified cellulase was CMCase. And it was demonstrated to be homogeneous on both SDS PAGE and IEF PAGE, with an isoelectric point of 4.0, molecular weight of 59600 daltons, optimum temperature of 55℃, optimum pH of 4.5. the specific activity of the cellulase increased to 26.2 fold of the source enzyme with an activity recovery of 32.8%. The cellulase can be inhibited by Mg 2+ ,Ag +,Fe 3+ ,Zn 2+ and activated by K +,Na +,Ca 2+ ,Mg 2+ .