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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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Journal ArticleDOI
TL;DR: This review attempts to provide an updated compilation of studies reported in the literature pertaining to reactors containing lipases in immobilized forms, in a way that helps the reader direct a bibliographic search and develop an integrated perspective of the subject.

466 citations

Journal ArticleDOI
Haruo Takahashi1, Bo Li1, Toshiya Sasaki1, Chie Miyazaki1, Tsutomu Kajino1, Shinji Inagaki1 
TL;DR: In this paper, an enzyme, horseradish peroxidase (HRP), was adsorbed in the manner of the single immersion method on the silica mesoporous materials FSM-16, MCM-41, and SBA-15 with various pore diameters from 27 to 92 A, and their enzymatic activities in an organic solvent and thermal stabilities were studied.
Abstract: An enzyme, horseradish peroxidase (HRP), was adsorbed in the manner of the single immersion method on the silica mesoporous materials FSM-16, MCM-41, and SBA-15 with various pore diameters from 27 to 92 A, and their enzymatic activities in an organic solvent and the thermal stabilities were studied. FSM-16 and MCM-41 showed a larger amount of adsorption of HRP than SBA-15 or silica gel when the pore sizes were larger than the 50 A. The increased enzyme adsorption capacity may be due to the surface characteristics of FSM-16 and MCM-41, which would be consistent with the observed larger adsorption capacity of cationic pigment compared with anionic pigment for these materials. The immobilized HRP on FSM-16 and MCM-41 with pore diameter 50 A showed the highest enzymatic activity in an organic toluene and thermal stability in aqueous solution at the temperature of 70 °C. The immobilized enzymes on the other mesoporous materials including large or small pore sized FSM-16 showed lower enzymatic activity in an or...

466 citations

Journal ArticleDOI
11 Feb 1983-Science
TL;DR: Applications of immobilized enzymes and cells in the chemical, pharmaceutical, and food industries, in clinical and chemical analyses, and in medicine, as well as probable future trends in enzyme technology are discussed.
Abstract: Performance of enzymes and whole cells in commercial applications can often be dramatically improved by immobilization of the biocatalysts, for instance, by their covalent attachment to or adsorption on solid supports, entrapment in polymeric gels, encapsulation, and cross-linking. The effect of immobilization on enzymatic properties and stability of biocatalysts is considered. Applications of immobilized enzymes and cells in the chemical, pharmaceutical, and food industries, in clinical and chemical analyses, and in medicine, as well as probable future trends in enzyme technology are discussed.

442 citations

Journal ArticleDOI
01 Jan 2001-Analyst
TL;DR: The nanoparticle surface biochemical functionalization demonstrates the feasibility of using nanoparticles for biosensing and biomarking applications and shows that the silica nanoparticles are a good biocompatible solid support for enzyme immobilization.
Abstract: In this report, we demonstrate the biochemical modification of silica based nanoparticles. Both pure and dye-doped silica nanoparticles were prepared, and their surfaces were modified with enzymes and biocompatible chemical reagents that allow them to function as biosensors and biomarkers. The nanoparticles produced in this work are uniform in size with a 1.6% relative standard deviation. They have a pure silica surface and can thus be modified easily with many biomolecules for added biochemical functionality. Specifically, we have modified the nanoparticle surfaces with enzyme molecules (glutamate dehydrogenase (GDH) and lactate dehydrogenase (LDH)) and a biocompatible reagent for cell membrane staining. Experimental results show that the silica nanoparticles are a good biocompatible solid support for enzyme immobilization. The immobilized enzyme molecules on the nanoparticle surface have shown excellent enzymatic activity in their respective enzymatic reactions. The nanoparticle surface biochemical functionalization demonstrates the feasibility of using nanoparticles for biosensing and biomarking applications.

442 citations

Journal ArticleDOI
TL;DR: Recent work regarding the immobilization of enzymes in inorganic mesoporous materials as well as the modifications to those materials is summarized in this paper.
Abstract: The commercial application of biocatalysts depends on the development of effective methods of immobilization. The immobilization of enzymes greatly increases the stability of enzymes and eases the burden of enzyme cost and thus, is widely pursued for efficient, selective, and environmentally friendly catalysis. This brief perspective focuses on recent development in the area of enzyme immobilization in porous materials. Recent work regarding the immobilization of enzymes in inorganic mesoporous materials as well as the modifications to those materials is summarized in this paper. The configuration of supported enzyme as membranes and fibers may facilitate their application in areas that require a biocatalytic process. Enzymes immobilized in or on fibrous membranes provide high surface area for high throughput biocatalysis. These membrane bioreactors also allow for biotransformations to be carried out within a continuous flow process while maintaining enzyme stability under operating conditions as a result...

435 citations


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Performance
Metrics
No. of papers in the topic in previous years
YearPapers
2023219
2022417
2021480
2020548
2019553
2018543