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<p>This work describes the synthesis of a silver nanocoordination complex and capped silver nanoparticles (AgNPs). Several methods, such as field emission scanning electron microscopy (FESEM), dynamic light scattering (DLS), infrared spectroscopy (IR), powder X-ray diffraction (PXRD), and UV–Vis spectroscopy, were used to characterize the produced silver nanocoordination complex. With a maximum removal effectiveness of 96.9%, the complex demonstrated exceptional efficacy in eliminating the hazardous acid fuchsin dye. Furthermore, the <i>Aspergillus</i> sp. RL2Ct cutinase enzyme was immobilized using the coordination complex as a platform. As temperatures rose, it was found that the enzyme’s activity increased in both its free and immobilized forms. The free enzyme’s activity peaked at 30&#xa0;°C at 1853 U/mg protein, whereas the total activity of the 1344 U/mg protein at 40&#xa0;°C. The study also investigated the reusability of the AgNP-immobilized cutinase over 110th cycles of hydrolysis activity and found that it was very effective for its reuse about 110th cycle. Furthermore, it evaluated the storage stability of both free and immobilized enzymes, revealing that the immobilized enzymes exhibited greater stability over an extended period as compared to the free enzyme.</p>

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Synthesis of silver nanocoordination complex morpholine for the remediation of acid fuchsin dye and immobilization of Aspergillus sp. RL2Ct cutinase

  • 期刊论文

  • 发表日期：

    2025年3月18日

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  • Monika Bharti,
  • Saruchi,
  • Sonika Arti,
  • Sabah Ansar,
  • Vaneet Kumar

摘要

This work describes the synthesis of a silver nanocoordination complex and capped silver nanoparticles (AgNPs). Several methods, such as field emission scanning electron microscopy (FESEM), dynamic light scattering (DLS), infrared spectroscopy (IR), powder X-ray diffraction (PXRD), and UV–Vis spectroscopy, were used to characterize the produced silver nanocoordination complex. With a maximum removal effectiveness of 96.9%, the complex demonstrated exceptional efficacy in eliminating the hazardous acid fuchsin dye. Furthermore, the Aspergillus sp. RL2Ct cutinase enzyme was immobilized using the coordination complex as a platform. As temperatures rose, it was found that the enzyme’s activity increased in both its free and immobilized forms. The free enzyme’s activity peaked at 30 °C at 1853 U/mg protein, whereas the total activity of the 1344 U/mg protein at 40 °C. The study also investigated the reusability of the AgNP-immobilized cutinase over 110th cycles of hydrolysis activity and found that it was very effective for its reuse about 110th cycle. Furthermore, it evaluated the storage stability of both free and immobilized enzymes, revealing that the immobilized enzymes exhibited greater stability over an extended period as compared to the free enzyme.