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alpha,alpha-Trehalase of Trichoderma reesei.

P Vijayakumar, W Ross, E T Reese

Canadian Journal of Microbiology

|October 1, 1978

Summary

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Researchers purified the Trichoderma reesei trehalase enzyme using bentonite adsorption. This simple method significantly boosted enzyme activity and recovery, making it a promising technique for enzyme purification.

Area of Science:

Biochemistry
Enzyme Technology
Protein Purification

Background:

Trehalase enzymes are crucial in various biological processes.
Efficient purification of Trichoderma reesei trehalase is important for its applications.
Bentonite is a clay mineral with adsorbent properties.

Purpose of the Study:

To develop a simple and effective method for purifying Trichoderma reesei trehalase.
To characterize the purified alpha,alpha-trehalase.

Main Methods:

Adsorption and elution of trehalase from Trichoderma reesei on bentonite.
Determination of enzyme activity, optimum pH, isoelectric point (pI), and Michaelis constant (Km).

Main Results:

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A 70-80 fold increase in specific activity was achieved.

90% recovery of the trehalase enzyme was obtained.

The purified alpha,alpha-trehalase exhibited an optimum pH of 4.4, pI of 5.7, Km of 3.1 x 10(-3) M, and specific activity of 50 µmol/mg·min⁻¹.

Conclusions:

Simple bentonite adsorption and elution is a highly effective method for purifying Trichoderma reesei trehalase.
The characterized enzyme properties provide valuable data for potential biotechnological applications.