Effect of the activation strategy of nickel oxide‐multi‐walled carbon nanotubes on the immobilization of xylanase for synthesis of xylooligosaccharides

Magnetic nickel oxide multi-walled carbon nanotubes (MWCNT-NiO) were employed in the immobilization of xylanase from Thermomyces lanuginosus, after modification with (3-glycidoxypropyl)trimethoxysilane or 3-aminopropyltriethoxysilane (APTES). The APTES-derivatized MWCNT-NiO particles were activated with glutaraldehyde to immobilize T. lanuginosus xylanase via covalent attachment. The (3-glycidoxypropyl)trimethoxysilane-derivatized MWCNT-NiO particles were directly used for the covalent immobilization of T. lanuginosus xylanase, or the formed epoxy groups were converted to aldehyde groups. The free xylanase had maximum activity at pH 7.5, whereas the immobilized samples showed an optimum pH of 7.0. The optimum temperature was 60°C for the xylanase samples. The thermal stability of xylanase increased at 7 and/or 12 folds after immobilization. The results of xylooligosaccharide synthesis showed that the main formed xylooligosaccharides were xylobiose, xylotriose, and xylotetraose for the immobilized xylanase samples. Furthermore, an effect of the enzyme loading could be found, an increase in this parameter promoted that xylobiose and xylotriose amounts slightly increased, whereas xylotetraose amount slightly decreased. The immobilized xylanase samples retained at least 80% of their initial activity after five reuses at pH 7.0 and 60°C. The results show that the new xylanase preparations were easily separable, thermally stable, and reusable in the synthesis of xylooligosaccharides.

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Publication Details

Journal
Biotechnology and Applied Biochemistry
Published
2024-12-03
DOI
https://doi.org/10.1002/bab.2705
Citations
1
Primary Topic
Enzyme Catalysis and Immobilization
Type
article
Field-Weighted Citation Impact
0.23

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article

Effect of the activation strategy of nickel oxide‐multi‐walled carbon nanotubes on the immobilization of xylanase for synthesis of xylooligosaccharides

Roberto Fernández‐Lafuente, Deniz Yıldırım, Dilek Alagöz, Ali Toprak et al.
1 citations
Biotechnology and Applied Biochemistry
Enzyme Catalysis and Immobilization
0.23
article

Effect of the activation strategy of nickel oxide‐multi‐walled carbon nanotubes on the immobilization of xylanase for synthesis of xylooligosaccharides

Roberto Fernández‐Lafuente, Deniz Yıldırım, Dilek Alagöz, Ali Toprak, Nazlı Ece Varan
article en
1 citations

Abstract

Magnetic nickel oxide multi-walled carbon nanotubes (MWCNT-NiO) were employed in the immobilization of xylanase from Thermomyces lanuginosus, after modification with (3-glycidoxypropyl)trimethoxysilane or 3-aminopropyltriethoxysilane (APTES). The APTES-derivatized MWCNT-NiO particles were activated with glutaraldehyde to immobilize T. lanuginosus xylanase via covalent attachment. The (3-glycidoxypropyl)trimethoxysilane-derivatized MWCNT-NiO particles were directly used for the covalent immobilization of T. lanuginosus xylanase, or the formed epoxy groups were converted to aldehyde groups. The free xylanase had maximum activity at pH 7.5, whereas the immobilized samples showed an optimum pH of 7.0. The optimum temperature was 60°C for the xylanase samples. The thermal stability of xylanase increased at 7 and/or 12 folds after immobilization. The results of xylooligosaccharide synthesis showed that the main formed xylooligosaccharides were xylobiose, xylotriose, and xylotetraose for the immobilized xylanase samples. Furthermore, an effect of the enzyme loading could be found, an increase in this parameter promoted that xylobiose and xylotriose amounts slightly increased, whereas xylotetraose amount slightly decreased. The immobilized xylanase samples retained at least 80% of their initial activity after five reuses at pH 7.0 and 60°C. The results show that the new xylanase preparations were easily separable, thermally stable, and reusable in the synthesis of xylooligosaccharides.

Biotechnology and Applied BiochemistryVol. 72(4)
Nevşehir Hacı Bektaş Veli University (TR), Cukurova University (TR)
Agencia Estatal de Investigación
Clean water and sanitation
Openalex Percentile: Top 40%
Enzyme Catalysis and Immobilization
0.23
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