What question did this study set out to answer?

The aim is to identify and characterize collagenases derived from Pseudomonas chlororaphis GP72 for industrial use.

February 2, 2026BiologyOpen Access

Heterologous Expression and Characterization of Collagenases from Pseudomonas chlororaphis GP72

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Demonstrates the heterologous expression of collagenases in E. coli, revealing their enzyme properties and stability.

The aim is to identify and characterize collagenases derived from Pseudomonas chlororaphis GP72 for industrial use.
Identified five Pseudomonas-derived collagenases using sequence alignment.
Employed bioinformatics tools for structural and functional analysis.
Achieved heterologous expression of two collagenases in E. coli.
Characterized enzymatic properties including temperature, pH, and inhibitory effects of metal ions.
ColP1 and ColP2 were produced at yields of 148 mg/L and 322 mg/L, respectively.
Optimum temperature for activity was found to be 28 °C for both collagenases.
ColP1 showed highest activity at pH 8, while ColP2 peaked at pH 4.
Metal ions inhibited collagenase activity to varying extents.

Hu et al. (2026) studied this question.

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