<b>IMMOBILIZATION OF TANNIN ACYL HYDROLASE FROM ASPERGILLUS NIGER</b>
Creators: name: Kumar Bompalli, Lenin
Publisher: name: figshare
Year: 2024
Subjects: classificationCode: 310604
subject: Industrial biotechnology diagnostics (incl. biosensors)
classificationCode: 310603
subject: Fermentation
classificationCode: 310602
subject: Bioprocessing, bioproduction and bioproducts
classificationCode: 310601
subject: Biocatalysis and enzyme technology
classificationCode: 310605
subject: Industrial microbiology (incl. biofeedstocks)
classificationCode: 410302
subject: Biological control
classificationCode: 410301
subject: Biodiscovery
classificationCode: 410305
subject: Environmental marine biotechnology

description: The immobilization of tannin acyl hydrolase (TAH) from <i>Aspergillus niger</i> involves the process of fixing or binding the enzyme onto a solid support or matrix, thereby enhancing its stability and reusability in various industrial and biotechnological applications. Here’s a detailed description of the process and its significance:<b>1. Tannin Acyl Hydrolase (TAH):</b>Tannin acyl hydrolase is an enzyme produced by <i>Aspergillus niger</i>, a filamentous fungus known for its ability to degrade and modify tannins. TAH specifically hydrolyzes the ester bonds present in tannins, breaking them down into simpler compounds.<b>2. Immobilization Process:</b><b>Selection of Support Matrix:</b> The first step in immobilization is choosing a suitable solid support or matrix. Common materials include agarose, silica gel, cellulose, chitosan, or various synthetic polymers. The choice depends on factors like enzyme stability, compatibility, and ease of handling.<b>Attachment of Enzyme:</b> The TAH enzyme is then attached or adsorbed onto the surface of the support material through physical adsorption, covalent bonding, entrapment, or encapsulation methods.<b>Cross-linking :</b> In some cases, cross-linking agents or techniques may be used to stabilize the enzyme and prevent leaching from the support matrix.<b>Characterization:</b> Post-immobilization, the activity, stability, and kinetic properties of the immobilized TAH are characterized to ensure its functionality and efficiency in practical applications.<b>3. Advantages of Immobilization:</b><b>Enhanced Stability:</b> Immobilization typically improves the enzyme’s stability against pH changes, temperature variations, and mechanical agitation, thereby extending its operational lifespan.<b>Reusability:</b> Immobilized enzymes can be reused multiple times, reducing operational costs and enzyme wastage.<b>Ease of Separation:</b> The immobilized TAH can be easily separated from the reaction mixture, simplifying downstream processing and product purification.<b>Controlled Reactivity:</b> Immobilization often provides better control over enzyme-substrate interactions and reaction kinetics, enhancing overall process efficiency.<b>4. Applications:</b><b>Food and Beverage Industry:</b> Immobilized TAH can be used in the processing of tea, coffee, and wine to reduce tannin content and improve flavor profiles.<b>Textile Industry:</b> Enzymatic treatment with immobilized TAH can aid in the modification and coloration of textiles by removing tannins.<b>Bioremediation:</b> Immobilized TAH can also be applied in environmental bioremediation efforts to degrade tannins present in industrial wastewaters.<b>5. Future Directions:</b>Research continues to explore novel immobilization techniques and support materials to further enhance the efficiency and application scope of immobilized TAH.Optimization of immobilization protocols to maximize enzyme loading and stability while minimizing costs remains a focus for scaling up industrial applications.In conclusion, the immobilization of tannin acyl hydrolase from <i>Aspergillus niger</i> represents a strategic approach to harnessing the enzymatic capabilities of this fungus for various industrial and environmental applications, offering enhanced stability, reusability, and process efficiency compared to free enzymes.