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 immobilized xylanase has been immobilized in hydrogel beads prepared by complexation between chitosan and xanthan and shows a predominantly fibrilar microstructure within which there are regions having globular shapes where the enzymes are lodged.
Abstract: endo-1,4-β-Xylanase (E.C. 3.2.1.8) has been immobilized in hydrogel beads prepared by complexation between chitosan and xanthan. The enzyme immobilization efficiency is between 88 and 98% within a wide range of concentrations of xylanase. The optimum xylanase activity requires a pH between 5.0 and 5.5. The immobilized enzymes show 60-70% higher activity than free enzymes. The K m of the immobilized xylanase increases with the concentration of the enzyme in the beads. The latter show, by electron microscopy, a predominantly fibrilar microstructure within which there are regions having globular shapes where the enzymes are lodged.
87 citations
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TL;DR: In this paper, a bifunctional support containing epoxide and thiol-reactive groups for protein immobilization was presented, where the epoxides of the support can form irreversible bonds with nucleophile surface groups of the already immobilized protein in a rapid way.
87 citations
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TL;DR: The enzyme immobilization method was optimized for biosensor applications and the following optimal values were determined: pH 4.0 for the synthesis medium, 1.23 M monomer concentration and 3.2% (w/w) cross-linking content.
87 citations
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TL;DR: The improvement of hydrolysis by DFU assisted-enzymolysis was achieved by enhancing the solid solubility, changing the molecular structure of protein and increased the surface area of immobilized enzyme.
87 citations
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TL;DR: A polyamidoamine (PAMAM) dendrimer was grafted onto magnetic multi-walled carbon nanotubes (m-MWCNTs) to combine magnetic properties with a large surface functionalized with amino groups as mentioned in this paper.
87 citations