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[Carboxylic proteinase from Trichoderma lignorum]

G N Rudenskaia, A L Osterman, V M Stepanov

Biokhimiia (Moscow, Russia)

|April 1, 1980

Summary

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Researchers isolated a fungal carboxylic proteinase from Trichoderma lignorum, achieving 400-fold purification. This enzyme, stable at acidic pH, shows characteristics similar to other fungal proteinases.

Area of Science:

Enzymology
Microbial Biochemistry

Background:

Trichoderma lignorum is a fungal species known for producing various enzymes.
Carboxylic proteinases are crucial enzymes with diverse industrial and biological applications.
Efficient isolation and characterization of novel proteinases are essential for exploring their potential.

Purpose of the Study:

To isolate and purify a carboxylic proteinase from a commercial Trichoderma lignorum enzyme preparation.
To characterize the biochemical properties of the isolated carboxylic proteinase.
To assess the enzyme's stability and inhibition profile.

Main Methods:

Enzyme purification using ammonium sulfate precipitation, gel-filtration (Acrylex P-10, Sephadex G-50), and affinity chromatography (gramicidin S, bacitracin-Sepharose).

Related Experiment Videos

Determination of molecular weight via gel-filtration.

Analysis of amino acid composition.

Assessment of enzyme stability across a pH range.

Inhibition studies using specific carboxylic proteinase inhibitors.

Main Results:

A carboxylic proteinase was successfully isolated from Trichoderma lignorum.
The purification process yielded a 400-fold increase in enzyme purity with a 7.2% yield.
The enzyme has a molecular weight of 33,000 Da and exhibits stability between pH 3.0 and 6.0.
Amino acid composition is comparable to other fungal carboxylic proteinases.
Complete inhibition was observed with N-diazoacetyl-N'-2,4-dinitrophenylethylenediamine and pepstatin.

Conclusions:

A novel carboxylic proteinase was purified from Trichoderma lignorum.
The characterized enzyme possesses properties suitable for applications requiring acidic stability.
The findings contribute to the understanding of fungal proteinases and their potential utility.