Scholarlink

<p>The immobilization of catalase onto stable, reusable supports is crucial for efficient peroxide-based biocatalytic applications. In this study, catalase was immobilized for the first time onto epoxy-functionalized kaolinite particles prepared via surface silanization with (3-glycidyloxypropyl)trimethoxysilane. Structural and surface characterizations confirmed successful organosilane grafting while preserving the layered kaolinite framework. The modified support exhibited rapid enzyme uptake and a high immobilization capacity of approximately 300 mg g<sup>−1</sup>. Kinetic analysis showed a substantial decrease in <i>K</i><sub><i>m</i></sub> from 57.3 mM (free catalase) to 21.6 mM after immobilization, indicating enhanced substrate affinity. In contrast, <i>V</i><sub><i>max</i></sub> decreased due to diffusion limitations typical of heterogeneous systems. Despite this, catalytic efficiency increased nearly 1.8-fold. Moreover, immobilized catalase demonstrated significantly improved operational reusability and long-term storage stability compared to the free enzyme. These results highlight silanized kaolinite as a robust, low-cost, and efficient mineral-based support for catalase immobilization, with strong potential for environmental and industrial biocatalytic applications.</p>

错误：搜索内容不能为空，请输入英文关键词
错误：关键词超出字数限制，请精简
高级检索

Enhanced kinetic performance and stability of catalase immobilized on epoxy-functionalized kaolinite

  • 期刊论文

  • 出版模式：

    开放获取

  • 发表日期：

    2026年2月10日

查看全文
  • Kadir Erol,
  • Aysel Veyisoğlu,
  • Demet Tatar,
  • Buket Bulut Kocabaş,
  • İhsan Alacabey,
  • Ebru Gökmeşe

摘要

The immobilization of catalase onto stable, reusable supports is crucial for efficient peroxide-based biocatalytic applications. In this study, catalase was immobilized for the first time onto epoxy-functionalized kaolinite particles prepared via surface silanization with (3-glycidyloxypropyl)trimethoxysilane. Structural and surface characterizations confirmed successful organosilane grafting while preserving the layered kaolinite framework. The modified support exhibited rapid enzyme uptake and a high immobilization capacity of approximately 300 mg g−1. Kinetic analysis showed a substantial decrease in Km from 57.3 mM (free catalase) to 21.6 mM after immobilization, indicating enhanced substrate affinity. In contrast, Vmax decreased due to diffusion limitations typical of heterogeneous systems. Despite this, catalytic efficiency increased nearly 1.8-fold. Moreover, immobilized catalase demonstrated significantly improved operational reusability and long-term storage stability compared to the free enzyme. These results highlight silanized kaolinite as a robust, low-cost, and efficient mineral-based support for catalase immobilization, with strong potential for environmental and industrial biocatalytic applications.