Journal
JOURNAL OF THE SERBIAN CHEMICAL SOCIETY
Volume 88, Issue 5, Pages 495-504Publisher
SERBIAN CHEMICAL SOC
DOI: 10.2298/JSC221121009A
Keywords
MWCNT; MWCNT-COOH; nanobiocatalyst; enzyme immobilization; enzymes stability and reusability
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The immobilization of cross-linked tannase onto carboxyl-functionalized multi-walled carbon nanotubes (MWCNT-COOH) was achieved via physical adsorption. The successful adsorption event was confirmed through spectroscopic and morphological characterizations of the enzyme-nanotubes composite. The enzyme composite showed comparable or even superior catalytic activities and stabilities compared to free tannase under different conditions.
The immobilization of cross-linked tannase onto carboxyl-functionalized multi-walled carbon nanotubes (MWCNT-COOH) was achieved via physical adsorption. Glutaraldehyde was used to cross-link the enzyme molecules. Spectroscopic and morphological characterizations of the enzyme-nanotubes composite were carried out, which authenticated the successful adsorption event. Enzyme composite is proven equal to, or even superior than free tannase, in terms of catalytic activities and stabilities, when measured under different thermal, pH and recycling conditions. Whilst both free and immobilized tannase preparations exhibited optimum catalysis at pH 5.0 and 35 degrees C, tannase-nanotubes composite possesses better thermal stability. The immobilized preparation retained 75 % of its initial catalytic activity following ten consecutive uses. The study demonstrated a facile method to produce catalytically efficient nanobiocatalyst composite for biotechnological applications.
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