Robust Immobilization and Activity Preservation of Enzymes in Porous Frameworks by Silica-Based “Inorganic Glue”

Abstract

The development of novel methods to enhance enzyme-carrier interactions in situ, at a feasible cost, and on a large scale is crucial for improving the stability and durability of current immobilized enzyme systems used in industrial settings. Here, a pioneering approach termed “silica-based inorganic glue” is proposed, which utilizes protein-catalyzed silicification to fix enzyme within porous matrix while preserving enzyme activity. This innovative strategy offers several key benefits, including conformational stabilization of enzymes, improved interactions between enzymes and the matrix, prevention of enzyme leakage, and mitigation of pore blocking. Moreover, the controllable and scalable nature of this method renders it a cost-effective solution for enhancing enzyme immobilization in industrial contexts. To demonstrate the effectiveness of the “silica-based inorganic glue” technology, it has applied to three different enzymes exhibiting varying surface characteristics, sizes, and functions and in diverse porous supports, including a metal-organic framework (MOF) and a commercial macroporous resin, which resulted in a significant improvement of the stability and longevity of the immobilized enzymes. Overall, this findings represent a significant advancement in enzyme immobilization techniques, signaling a paradigm shift in current industrial catalysis.