What is it about?
Tannin acyl hydrolase, commonly referred to as tannase (E.C. 3.1.1.20), an inducible extra-cellular enzyme produced by a number of animals, plants and microbes. In this investigation, tannase production under solid-state fermentation by using Aspergillus niger and the waste residue of cashew husk was used as substrate for obtaining the desired fermented product. After termination of fermentation gallic acid was isolated from the tannase, and it was used in the production of an antibacterial drug Trimethoprim by using chemical and bioconversions. Microbial tannase is more stable than tannase from other sources like plants or animals. Tannase from fungal sources are reported to be active in a wide range of pH and temperature. Aspergillus niger was used in this study for the immobilization of tannase enzyme. Tannase production was reached maximum within 24 to 36 h against crude tannin extract obtained from Anacardium occidentale by using Aspergillus niger. Tannase assay was calculated. Activation energy of the immobilized enzyme was lower than that of the free enzyme. Optimum pH and temperature was evaluated for the free and immobilized enzyme.
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Why is it important?
The investigation focuses on utilizing Aspergillus niger for tannase production via solid-state fermentation using cashew husk waste. Tannase, an extracellular enzyme, efficiently hydrolyzes tannins found in natural sources like Anacardium occidentale. The enzyme's stability and broad pH and temperature tolerance, characteristic of fungal sources, make it ideal for industrial applications. Gallic acid, a product of tannase action on tannins, is then utilized for synthesizing trimethoprim, an antibacterial drug. Immobilization of the enzyme enhances its efficiency and stability, demonstrated by lower activation energy compared to the free form. Optimal conditions for pH and temperature are crucial for maximizing enzyme activity during both production and application phases. This research underscores the biotechnological potential of fungal tannase in sustainable enzymatic processes for pharmaceutical and other industrial uses.
Perspectives
The study on fungal tannase underscores its potential in sustainable bioprocessing, offering environmentally friendly alternatives to traditional chemical methods. Utilizing waste materials like cashew husk for enzyme production highlights opportunities for cost-effective and eco-friendly industrial practices. The ability of tannase to convert tannins into gallic acid, and subsequently into trimethoprim, showcases a novel pathway for pharmaceutical synthesis. Immobilization of tannase enhances its stability and catalytic efficiency, promising improved industrial application and cost-effectiveness. Optimization of pH and temperature conditions for enzyme activity could further enhance productivity and application scope in various industries. Cross-disciplinary collaboration between microbiology, enzymology, and pharmaceutical sciences drives innovation in biotechnological applications. Global implications include potential advancements in sustainable manufacturing practices and pharmaceutical production. Future research could focus on scaling up production, exploring new enzyme sources, and optimizing bioprocessing technologies. Commercial viability and regulatory considerations are critical for translating laboratory findings into industrial applications. Overall, the perspectives from this study suggest promising avenues for enhancing sustainability, efficiency, and innovation in biotechnological and pharmaceutical industries.
Dr. Lenin Kumar Bompalli
Dr. B. R. Ambedkar University, Etcherla.
Read the Original
This page is a summary of: , International Journal of Pharmaceutical Sciences and Research, April 2013, International Journal of Pharmaceutical Sciences and Research,
DOI: 10.13040/ijpsr.0975-8232.4(4).1485-87.
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