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

Madan L. Verma; Rajneesh Chaudhary; Takuya Tsuzuki; Colin J. 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 L. Verma, Rajneesh Chaudhary, Takuya Tsuzuki, Colin J. Barrow, Munish Puri^*

^*Corresponding author for this work

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

191 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
Externally published	Yes

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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 (KM) 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 = "Verma, {Madan L.} and Rajneesh Chaudhary and Takuya Tsuzuki and Barrow, {Colin J.} and Munish Puri",

year = "2013",

month = may,

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

language = "English",

volume = "135",

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journal = "Bioresource Technology",

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T1 - Immobilization of β-glucosidase on a magnetic nanoparticle improves thermostability

T2 - Application in cellobiose hydrolysis

AU - Verma, Madan L.

AU - Chaudhary, Rajneesh

AU - Tsuzuki, Takuya

AU - Barrow, Colin J.

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 (KM) 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 (KM) 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

UR - http://www.scopus.com/inward/record.url?scp=84876474057&partnerID=8YFLogxK

U2 - 10.1016/j.biortech.2013.01.047

DO - 10.1016/j.biortech.2013.01.047

M3 - Article

SN - 0960-8524

VL - 135

SP - 2

EP - 6

JO - Bioresource Technology

JF - Bioresource Technology

ER -

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

Abstract

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