AustralieFrV1, Main, Exploration, bibRecord, 004E90

Immobilization of β-glucosidase on a magnetic nanoparticle improves thermostability: Application in cellobiose hydrolysis

Identifieur interne : 004E90 ( Main/Exploration ); précédent : 004E89; suivant : 004E91

Immobilization of β-glucosidase on a magnetic nanoparticle improves thermostability: Application in cellobiose hydrolysis

Auteurs : Madan L. Verma [Australie] ; Rajneesh Chaudhary [Australie] ; Takuya Tsuzuki [Australie] ; Colin J. Barrow [Australie] ; Munish Puri [Australie]

Source :

Bioresource technology [ 0960-8524 ] ; 2013.

RBID : Pascal:13-0218019

Descripteurs français

Pascal (Inist)
- Immobilisation, Nanomatériau magnétique, Nanoparticule, Stabilité thermique, Hydrolyse, Lignocellulose, Biocarburant, Nanobiotechnologie, β-Glucosidase, Cellobiose, Oxyde de fer, Cellulolytic enzyme, Cellulase.

English descriptors

KwdEn :
- Biofuel, Cellobiose, Cellulase, Cellulolytic enzyme, Hydrolysis, Immobilization, Iron oxide, Lignocellulosics, Magnetic nanomaterial, Nanobiotechnology, Nanoparticle, Thermal stability, β-Glucosidase.

Abstract

The objective of the present work was to develop a thermostable β-glucosidase through immobilization on a nanoscale carrier for potential application in biofuel production. β-Glucosidase (BGL) from Aspergillus niger was immobilized to functionalized magnetic nanoparticles by covalent binding. Immobilized nanoparticles showed 93% immobilization binding. Immobilized and free BGL were characterized using Transmission electron microscopy (TEM) and Fourier transform infrared spectroscopy (FTIR) techniques. Free and immobilized enzyme exhibited different pH-optima at pH 4.0 and 6.0, respectively, but had the same temperature optima at 60 °C. Michaelis constant (K_M) was 3.5 and 4.3 mM for free and immobilized BGL. Thermal stability of the immobilized enzyme was enhanced at 70 °C. The immobilized nanoparticle-enzyme conjugate retained more than 50% enzyme activity up to the 16th cycle. Maximum glucose synthesis from cellobiose hydrolysis by immobilized BGL was achieved at 16 h.

Affiliations:

Australie

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Le document en format XML

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<front><div type="abstract" xml:lang="en">The objective of the present work was to develop a thermostable β-glucosidase through immobilization on a nanoscale carrier for potential application in biofuel production. β-Glucosidase (BGL) from Aspergillus niger was immobilized to functionalized magnetic nanoparticles by covalent binding. Immobilized nanoparticles showed 93% immobilization binding. Immobilized and free BGL were characterized using Transmission electron microscopy (TEM) and Fourier transform infrared spectroscopy (FTIR) techniques. Free and immobilized enzyme exhibited different pH-optima at pH 4.0 and 6.0, respectively, but had the same temperature optima at 60 °C. Michaelis constant (K<sub>M</sub>
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Immobilization of β-glucosidase on a magnetic nanoparticle improves thermostability: Application in cellobiose hydrolysis

Immobilization of β-glucosidase on a magnetic nanoparticle improves thermostability: Application in cellobiose hydrolysis

Source :

Descripteurs français

English descriptors

Abstract

Links toward previous steps (curation, corpus...)

Le document en format XML

Pour manipuler ce document sous Unix (Dilib)

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