Topic
Immobilized enzyme
About: Immobilized enzyme is a research topic. Over the lifetime, 15282 publications have been published within this topic receiving 401860 citations.
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TL;DR: The HP-MOFs were stable over a wide pH range and met the catalysis conditions of most enzymes and the as-prepared hierarchical micro/mesoporous MOFs with mesoporous defects showed a superior adsorption capacity towards enzymes.
Abstract: Metal–organic frameworks (MOFs) have drawn extensive research interest as candidates for enzyme immobilization owing to their tunable porosity, high surface area, and excellent chemical/thermal stability. Herein, we report a facile and universal strategy for enzyme immobilization using highly stable hierarchically porous metal–organic frameworks (HP-MOFs). The HP-MOFs were stable over a wide pH range (pH = 2–11 for HP-DUT-5) and met the catalysis conditions of most enzymes. The as-prepared hierarchical micro/mesoporous MOFs with mesoporous defects showed a superior adsorption capacity towards enzymes. The maximum adsorption capacity of HP-DUT-5 for glucose oxidase (GOx) and uricase was 208 mg g−1 and 225 mg g−1, respectively. Furthermore, we constructed two multi-enzyme biosensors for glucose and uric acid (UA) by immobilizing GOx and uricase with horseradish peroxidase (HRP) on HP-DUT-5, respectively. These sensors were efficiently applied in the colorimetric detection of glucose and UA and showed good sensitivity, selectivity, and recyclability.
101 citations
TL;DR: Synthesis of Thermal Phase Separation Reactive Polymers and their Applications in Immobilized Enzymes as discussed by the authors is a well-known technique for separating reactive polymers and reactive enzymes.
Abstract: Synthesis of Thermal Phase Separating Reactive Polymers and Their Applications in Immobilized Enzymes
101 citations
TL;DR: In this article, a soybean α-amylase from soybeans was immobilized on two different matrices, Chitosan beads and Amberlite MB-150.
Abstract: α-Amylase from soybeans was immobilized on two different matrices, Chitosan beads and Amberlite MB-150. Maximum immobilization of 62% and 70.4% was obtained with Chitosan and Amberlite MB-150, respectively. The optimum pH obtained was 8.0 and 7.0 for the α-amylase immobilized on Chitosan beads and Amberlite MB-150, respectively; free enzyme showed an optimum pH of 5.5. The optimum temperature for both free and Chitosan immobilized enzymes was 70 °C whereas it was 75 °C for enzyme immobilized on Amberlite MB-150. α-Amylase immobilized on Chitosan showed an apparent K m of 4 mg/mL, whereas Amberlite immobilized enzyme showed an apparent K m of 2.5 mg/mL. The immobilized enzyme showed a high operational stability by retaining 38% and 58% of initial activity after 10 uses for Chitosan and Amberlite, respectively. The easy accessibility of soybean α-amylase, the ease of its immobilization on low-cost matrices, increased stability upon immobilization make it a suitable product for future applications. Both the matrices used for enzyme immobilization are non-toxic, cheap, renewable, biodegradable and have importance in food, cosmetics, biomedical, or pharmaceuticals applications.
101 citations
TL;DR: A potential use of this procedure for enzyme immobilization by entrapment in copper alginate gel for the construction of bioreactors to be used in the detoxification of polluted waste waters is indicated.
101 citations
TL;DR: The flower shaped-hybrid nanomaterials called hybrid nanoflower (HNF) consisting of urease enzyme and copper ions (Cu(2+)) are synthesized and a mechanistic elucidation of enhancement in both activity and stability of the HNF is reported.
101 citations