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

Madan Verma; Rajneesh Chaudhary; Takuya Tsuzuki; Colin Barrow; Munish Puri

doi:10.1016/j.biortech.2013.01.047

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

Madan Verma, Rajneesh Chaudhary, Takuya Tsuzuki, Colin Barrow, Munish Puri

Research output: Contribution to journal › Article › peer-review

189 Citations (Scopus)

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 4.3mM 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 16h.

Original language	English
Pages (from-to)	2-6
Number of pages	5
Journal	Bioresource Technology
Volume	135
DOIs	https://doi.org/10.1016/j.biortech.2013.01.047
Publication status	Published - May 2013

Keywords

Biofuel
Cellulase
Iron oxide
Lignocellulose
Nanobiotechnology

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

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

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 4.3mM 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 16h.",

keywords = "Biofuel, Cellulase, Iron oxide, Lignocellulose, Nanobiotechnology",

author = "Madan Verma and Rajneesh Chaudhary and Takuya Tsuzuki and Colin Barrow and Munish Puri",

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doi = "10.1016/j.biortech.2013.01.047",

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T2 - Application in cellobiose hydrolysis

AU - Verma, Madan

AU - Chaudhary, Rajneesh

AU - Tsuzuki, Takuya

AU - Barrow, Colin

AU - Puri, Munish

PY - 2013/5

Y1 - 2013/5

N2 - 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 4.3mM 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 16h.

AB - 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 4.3mM 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 16h.

KW - Biofuel

KW - Cellulase

KW - Iron oxide

KW - Lignocellulose

KW - Nanobiotechnology

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EP - 6

JO - Bioresource Technology

JF - Bioresource Technology

ER -

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

Abstract

Keywords

UN SDGs

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