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Cellulase immobilized on poly-L-glutamic acid.

T Takeuchi¹, K Makino

¹Department of Polymer Science and Engineering, Faculty of Textile Science, Kyoto Institute of Technology, Matsugasaki, Kyoto, Japan.

Biotechnology and Bioengineering

|February 1, 1987

Summary

Immobilized cellulase (IC) on poly-L-glutamic acid offers pH-controlled solubility and recovery. This enhanced enzyme stability and activity facilitates cellulose solvolysis for producing valuable low-molecular-weight compounds.

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Area of Science:

Biotechnology
Enzyme Immobilization
Biocatalysis

Background:

Cellulase is a key enzyme for cellulose degradation.
Enzyme immobilization enhances stability and reusability.
Developing efficient methods for cellulose hydrolysis is crucial.

Purpose of the Study:

To immobilize cellulase (Cellulosin AC-8) onto poly-L-glutamic acid.
To characterize the properties of the immobilized cellulase (IC).
To investigate the application of IC in cellulose solvolysis.

Main Methods:

Cellulase was immobilized on poly-L-glutamic acid.
Solubility, optimal pH, and temperature were determined.
Stability and activity of immobilized cellulase were assessed.

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Solvolysis of treated cellulose using IC was performed.

Main Results:

Immobilized cellulase (IC) exhibited pH-dependent solubility and recovery.
Optimal activity was observed at pH 5.5 and 55°C.
Immobilization improved IC stability against pH and temperature fluctuations.
IC efficiently produced low-molecular-weight compounds from treated cellulose.

Conclusions:

Poly-L-glutamic acid is a suitable support for cellulase immobilization.
Immobilized cellulase offers advantages in handling and reusability.
This method shows potential for efficient cellulose bioconversion.