Failed to connect with MySQL: User dastyarekoob_sEcAdMiNDaTa already has more than 'max_user_connections' active connections Production of Recombinant Enzyme for Polluted Water Treatment Using Nanoplates

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Production of Recombinant Enzyme for Polluted Water Treatment Using Nanoplates

Production of Recombinant Enzyme for Polluted Water Treatment Using Nanoplates

Researchers at Shahrekord University have successfully expressed and purified the cold-adapted enzyme triacylglycerol lipase from the bacterium Psychrobacter sp. C18 and immobilized it on aminographene and cellulose nanoplates.

 January 20, 2025  Scientific


A biochemistry researcher at Shahrekord University explained the significance of the project: "Enzymes are well-known biocatalysts that, due to their diverse characteristics—such as reducing reaction steps and solvent requirements—accelerate reactions and lower costs."

Cold-adapted lipases offer significant potential in biotechnology due to their high catalytic activity at low temperatures and unique properties. However, their low thermal stability and tendency to aggregate present challenges.

The researcher emphasized the importance of long-term enzyme storage and reusability for cost-effective industrial applications. Lipases are widely used in industries such as pharmaceuticals, food, detergents, textiles, cosmetics, and biodiesel production. Stabilizing enzymes on solid supports is an effective strategy for maintaining their catalytic efficiency during extended use.

The researcher added: "Enzyme immobilization involves attaching the enzyme to a specific substrate while retaining its catalytic activity, allowing it to be reused across multiple cycles" . Selecting the right substrate and immobilization method is critical, as the interactions between the enzyme and substrate directly impact the enzyme's catalytic efficiency and stability under various pH and temperature conditions.

Hybrid organic-inorganic nanomaterials have shown promising results in enhancing the kinetic and thermodynamic parameters of immobilized enzymes compared to traditional macroscopic supports. This study marks the first time a cold-adapted lipase has been expressed, purified, and immobilized on hybrid graphene and cellulose nanoplates using advanced gene synthesis and recombinant DNA technology. The approach aims to facilitate commercialization and large-scale production in biotechnology applications.

The recombinant enzyme has potential applications in enzyme-based industries such as food flavoring, biodiesel production, and bioremediation of polluted water. These advancements can reduce production costs, foster technological development, and strengthen collaboration between academia and industry.

This research, titled "Subcloning, Expression, and Purification of Cold-Adapted Triacylglycerol Lipase from Psychrobacter sp. C18 and Immobilization on Aminographene and Cellulose Nanoplates," was conducted as part of a doctoral dissertation supported by the Iran National Science Foundation.

 

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