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里氏木霉纤维素酶系的分离及其酶学性质(PDF)

《南京林业大学学报(自然科学版)》[ISSN:1000-2006/CN:32-1161/S]

Issue:
2007年06期
Page:
48-52
Column:
研究论文
publishdate:
2007-06-20

Article Info:/Info

Title:
Purification and Characterization of Cellulase from Trichoderma reesei
Article ID:
1000-2006(2007)06-0048-05
Author(s):
JIANG Hua YU Zhao-hai
College of Chemical Engineering Nanjing Forestry University, Nanjing 210037, China
Keywords:
Cellulase Endoglucanase Cellobiohydrolase β-glucosidase Purification
Classification number :
Q814.1
DOI:
10.3969/j.jssn.1000-2006.2007.06.011
Document Code:
A
Abstract:
The purification steps, e.g. a two-step ultrafiltration, cationic (CM-Sepharose FF) and anionic (DEAE-Sepharose FF) chromatography and size exclusion (Sephadex G-100) chromatography and the six homogeneous cellulase etc, were used to purify three endoglucanases (EG Ⅰ, EG Ⅱ and EG Ⅲ), two cellobiohydrolases (CBH Ⅰ and CBH Ⅱ) and a (β-glucosidase (GB) according to SDS—PAGE analysis from the culture broth of Trichoderma reesei. The specific activities of EG Ⅰ, EG Ⅱ and EG Ⅲ with carboxymethyl celluloses were estimated to be 176.35, 153.96, 64.22IU/mg, respectively. For CBH I and CBH Ⅱ, their specific activities with microcelluloses were 16.86, 4.82IU/mg, respectively. The GB with salicin was 31.00IU/mg. Their Km were 6.70, 8.46, 13.22, 1.37, 3.46, 2.20mg/mL, respectively. The greater Km of the purified enzyme component of the same class is, the smaller their turnover is. Their molecular weights of EG Ⅰ, EG Ⅱ, EG Ⅲ, CBH I, CBH Ⅱ and GB were 50, 46, 25, 65, 58, 75kDa, respectively.

References

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Last Update: 2013-05-20