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[Separation and purification of cellulase using affinity membrane].

Xiang-zhu Shi¹, Chun-teng Guo, Jian-wu Zhou

¹Institute of Biotechnology, Fuzhou University, Fuzhou 350002, China. xshiibfu@yahoo.com

Se Pu = Chinese Journal of Chromatography

|January 25, 2003

Summary

A new, efficient method purifies cellulase from Aspergillus niger, yielding a highly active endoglucanase. This breakthrough simplifies enzyme isolation for broader cellulose resource utilization.

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Area of Science:

Biochemistry
Enzymology
Industrial Microbiology

Background:

Cellulase is crucial for utilizing abundant cellulose resources.
Efficient purification of cellulase is a significant challenge due to its complex enzyme system.
Current purification methods are often multi-step and enzyme-specific.

Purpose of the Study:

To develop a simple, rapid, and efficient method for purifying cellulase.
To isolate and characterize a novel cellulase from Aspergillus niger.
To enhance the wider application of cellulase through improved purification.

Main Methods:

A novel purification strategy using qualitative filter paper treated with 5 mol/L sodium hydroxide.
Anion-exchange chromatography with POROS 20HQ for further purification.

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Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) for molecular mass estimation.

Main Results:

A new endoglucanase was successfully purified from Aspergillus niger.
The purified enzyme demonstrated high activity (350 U.mg-1) towards carboxymethyl cellulose (CMC).
The enzyme exhibited optimal activity at pH 4.0 and 70°C, with notable pH and temperature stability.

Conclusions:

The developed method offers a simple, rapid, and efficient approach for cellulase purification.
The novel endoglucanase possesses desirable properties for industrial applications.
This purification technique can facilitate wider use of cellulase in cellulose bioconversion.