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该文对光肩星天牛 (Anoplophoraglabripennis)幼虫纤维素酶的特性进行了研究 .内切 β 1,4 葡聚糖酶 (内切葡聚糖酶 ,Cx)和β 1,4 葡萄糖苷酶 (β 葡萄糖苷酶 )的最适作用温度均为 4 0℃ ,最适作用pH值分别为 4 4 5 6和 4 8,内切葡聚糖酶具有较广泛的pH值和温度作用范围 ,在 2 5 5 0℃之间能保持80 %以上活性 ,pH 3 2 7 2之间能保持 6 0 %以上的酶活性 .内切葡聚糖酶的热稳定性也稍强于 β 葡萄糖苷酶 ,但在 6 0℃温育 30min后 ,二者均丧失活性 .用含 0 1%CMC的聚丙烯酰胺凝胶电泳方法检测到光肩星天牛的内切葡聚糖酶具有两种同工酶 ,从非变性聚丙烯酰胺凝胶中回收该两条酶带 ,并在SDS 聚丙烯酰胺凝胶电泳中呈单一酶带 ,分子量分别为 2 6kD和 39kD .纯化的同工酶处于进一步研究中
In this paper, the characteristics of cellulase in larvae of Anoplophora glabripennis were studied. Endo-β 1,4-glucanase (Cx) and β 1,4 glucosidase (β-glucosidase ) Optimum temperature were 40 ℃, the optimum pH values were 4 4 5 6 and 4 8, endoglucanase has a wider range of pH and temperature range, at 2550 ℃ Can maintain more than 80% of the activity between the pH 3 2 7 2 to maintain more than 60% of the enzyme activity between endoglucanase thermal stability is also slightly stronger than β-glucosidase, but at 60 ℃ After incubation for 30 min, both of them lost their activity.The endoglucanases of S. aurantiacus with two isozymes were detected by polyacrylamide gel electrophoresis with 0 1% CMC, from non-denaturing polyacrylamide gel The two bands were recovered and presented as a single band in SDS polyacrylamide gel electrophoresis with molecular weights of 26 kD and 39 kD, respectively. The purified isozymes were further studied