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<p>Tannase-immobilized titanium dioxide nanoparticles (TITNP) were prepared by amino-functionalization and glutaraldehyde crosslinking on the surface of titanium dioxide nanoparticles (TNP) in the anatase form. The TITNP exhibited characteristic properties in the FT-IR spectrum, zeta potential, and sedimentation behavior. The catalytic activity, thermal stability, and reusability of the immobilized tannases were assessed under various temperature and pH conditions using a tannase activity assay via capillary electrophoresis, which quantifies the gallic acid (GA) released during the tannase-catalyzed hydrolysis of tannic acid (TA). The tannases immobilized on TITNP showed maximum catalytic activity at 40&#xa0;°C and pH 5 within the tested range of temperature and pH. The immobilized tannases were thermally stable, retaining 43% of their activity after 60&#xa0;min of incubation at 70&#xa0;°C. Additionally, TITNP exhibited strong reusability, retaining 60% of its initial enzyme activity even after 20 cycles of reuse. Finally, TITNP altered the catechin composition in the green tea extraction (GTE) solution through the catalytic action of tannase, decreasing gallated catechins (EGCG and ECG) and correspondingly increasing non-gallated catechins (EGC, EC) and GA.</p>

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Preparation and characterization of tannase immobilized titanium dioxide nanoparticles

  • 期刊论文

  • 发表日期：

    2025年6月6日

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  • Dong Phuong Vu,
  • Hoon Yoo

摘要

Tannase-immobilized titanium dioxide nanoparticles (TITNP) were prepared by amino-functionalization and glutaraldehyde crosslinking on the surface of titanium dioxide nanoparticles (TNP) in the anatase form. The TITNP exhibited characteristic properties in the FT-IR spectrum, zeta potential, and sedimentation behavior. The catalytic activity, thermal stability, and reusability of the immobilized tannases were assessed under various temperature and pH conditions using a tannase activity assay via capillary electrophoresis, which quantifies the gallic acid (GA) released during the tannase-catalyzed hydrolysis of tannic acid (TA). The tannases immobilized on TITNP showed maximum catalytic activity at 40 °C and pH 5 within the tested range of temperature and pH. The immobilized tannases were thermally stable, retaining 43% of their activity after 60 min of incubation at 70 °C. Additionally, TITNP exhibited strong reusability, retaining 60% of its initial enzyme activity even after 20 cycles of reuse. Finally, TITNP altered the catechin composition in the green tea extraction (GTE) solution through the catalytic action of tannase, decreasing gallated catechins (EGCG and ECG) and correspondingly increasing non-gallated catechins (EGC, EC) and GA.