CELLOBIOHYDROLASE FROM TRICHODERMA-REESEI
CELLOBIOHYDROLASE FROM TRICHODERMA-REESEI
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DOI：
10.1042/bj2150677
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发表时间：
1983-01-01
影响因子：
4.1
通讯作者：
RAUNIO, V
中科院分区：
文献类型：
--
作者：
NUMMI, M;NIKUPAAVOLA, ML;RAUNIO, V
A 1，4-β-从T. reesei的生物特异性吸附和免疫亲和层析。聚丙烯酰胺凝胶电泳显示一条蛋白带，免疫电泳显示一条弧形，与酶活性相对应。MW为65，000。pI为4.2-3.6。纯化的酶含有约10%的己糖。该酶与先前描述的纤维二糖水解酶的不同之处在于在纤维素水解中更有效。
A 1,4-.beta.-D-glucan cellobiohydrolase was purified from the culture liquid of T. reesei by using biospecific sorption on amorphous cellulose and immunoaffinity chromatography. A single protein band in polyacrylamide-gel electrophoresis and 1 arc in immunoelectrophoresis corresponded to the enzyme activity. The MW was 65,000. The pI was 4.2-3.6. The purified enzyme contained about 10% hexose. The enzyme differs from previously described cellobiohydrolases in being more effective in the hydrolysis of cellulose.