Nutt A, Sild V, Pettersson G, Johansson G
Department of Biochemistry, University of Uppsala, Sweden.
Eur J Biochem. 1998 Nov 15;258(1):200-6. doi: 10.1046/j.1432-1327.1998.2580200.x.
The chain-end preference and processivity of the cellulases 1,4-beta-D-glucan-cellobiohydrolase I (CBH I) and 1,4-beta-D-glucan-cellobiohydrolase II (CBH II) from Trichoderma reesei and 1,4-beta-D-glucan-cellobiohydrolase 50 (CBH 50) and 1,4-beta-D-glucan-cellobiohydrolase 58 (CBH 58) from Phanerochaete chrysosporium were studied by comparing experimental degradation data on reducing end-labelled bacterial microcrystalline cellulose with computer simulations of different models. Our results with T. reesei and P. chrysosporium cellulases show that there is a common pattern of hydrolysis for CBH-I-type enzymes and another clearly distinguishable pattern for CBH-II-type enzymes, especially in the initial part of the progress curve.
通过比较还原端标记的细菌微晶纤维素的实验降解数据与不同模型的计算机模拟结果，研究了里氏木霉的纤维素酶1,4-β-D-葡聚糖-纤维二糖水解酶I（CBH I）和1,4-β-D-葡聚糖-纤维二糖水解酶II（CBH II）以及黄孢原毛平革菌的1,4-β-D-葡聚糖-纤维二糖水解酶50（CBH 50）和1,4-β-D-葡聚糖-纤维二糖水解酶58（CBH 58）的链端偏好性和持续合成能力。我们对里氏木霉和黄孢原毛平革菌纤维素酶的研究结果表明，CBH-I型酶存在一种共同的水解模式，而CBH-II型酶则有另一种明显可区分的模式，尤其是在进程曲线的初始部分。
