Cellulose nanocrystal/gold nanoparticle composite as a matrix for enzyme immobilization

Khaled A. Mahmoud; Keith B. Male; Sabahudin Hrapovic; John H.T. Luong

doi:10.1021/am900331d

Cellulose nanocrystal/gold nanoparticle composite as a matrix for enzyme immobilization

Khaled A. Mahmoud
, Keith B. Male
, Sabahudin Hrapovic
, John H.T. Luong

National Research Council of Canada

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

Abstract

A novel nanocomposite consisting of cellulose nanocrystals (CNCs) functionalized with gold nanoparticles (AuNPs) serving as an excellent support for enzyme immobilization with phenomenally high loading is presented in this work. As testing models, cyclodextrin glycosyl transferase (CGTase) and alcohol oxidase were conjugated on an activated CNC/AuNP matrix. This catalytic platform exhibits significant biocatalytic activity with excellent enzyme stability and without apparent loss of the original activity. The recovered specific activities were ∼70% and 95% for CGTase and alcohol oxidase, respectively. This novel and inexpensive material is anticipated to extend to other enzymes, enhancing the enzyme loading and activity as well as the stability in both operation and storage.

Original language	English
Pages (from-to)	1383-1386
Number of pages	4
Journal	ACS Applied Materials and Interfaces
Volume	1
Issue number	7
DOIs	https://doi.org/10.1021/am900331d
Publication status	Published - 29 Jul 2009
Externally published	Yes

Keywords

cellulose nanocrystals
CGTase
enzyme
gold nanoparticles
immobilization

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10.1021/am900331d

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title = "Cellulose nanocrystal/gold nanoparticle composite as a matrix for enzyme immobilization",

abstract = "A novel nanocomposite consisting of cellulose nanocrystals (CNCs) functionalized with gold nanoparticles (AuNPs) serving as an excellent support for enzyme immobilization with phenomenally high loading is presented in this work. As testing models, cyclodextrin glycosyl transferase (CGTase) and alcohol oxidase were conjugated on an activated CNC/AuNP matrix. This catalytic platform exhibits significant biocatalytic activity with excellent enzyme stability and without apparent loss of the original activity. The recovered specific activities were ∼70\% and 95\% for CGTase and alcohol oxidase, respectively. This novel and inexpensive material is anticipated to extend to other enzymes, enhancing the enzyme loading and activity as well as the stability in both operation and storage.",

keywords = "cellulose nanocrystals, CGTase, enzyme, gold nanoparticles, immobilization",

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year = "2009",

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doi = "10.1021/am900331d",

language = "English",

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journal = "ACS Applied Materials and Interfaces",

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T1 - Cellulose nanocrystal/gold nanoparticle composite as a matrix for enzyme immobilization

AU - Mahmoud, Khaled A.

AU - Male, Keith B.

AU - Hrapovic, Sabahudin

AU - Luong, John H.T.

PY - 2009/7/29

Y1 - 2009/7/29

N2 - A novel nanocomposite consisting of cellulose nanocrystals (CNCs) functionalized with gold nanoparticles (AuNPs) serving as an excellent support for enzyme immobilization with phenomenally high loading is presented in this work. As testing models, cyclodextrin glycosyl transferase (CGTase) and alcohol oxidase were conjugated on an activated CNC/AuNP matrix. This catalytic platform exhibits significant biocatalytic activity with excellent enzyme stability and without apparent loss of the original activity. The recovered specific activities were ∼70% and 95% for CGTase and alcohol oxidase, respectively. This novel and inexpensive material is anticipated to extend to other enzymes, enhancing the enzyme loading and activity as well as the stability in both operation and storage.

AB - A novel nanocomposite consisting of cellulose nanocrystals (CNCs) functionalized with gold nanoparticles (AuNPs) serving as an excellent support for enzyme immobilization with phenomenally high loading is presented in this work. As testing models, cyclodextrin glycosyl transferase (CGTase) and alcohol oxidase were conjugated on an activated CNC/AuNP matrix. This catalytic platform exhibits significant biocatalytic activity with excellent enzyme stability and without apparent loss of the original activity. The recovered specific activities were ∼70% and 95% for CGTase and alcohol oxidase, respectively. This novel and inexpensive material is anticipated to extend to other enzymes, enhancing the enzyme loading and activity as well as the stability in both operation and storage.

KW - cellulose nanocrystals

KW - CGTase

KW - enzyme

KW - gold nanoparticles

KW - immobilization

UR - https://www.scopus.com/pages/publications/77951647619

U2 - 10.1021/am900331d

DO - 10.1021/am900331d

M3 - Article

C2 - 20355939

AN - SCOPUS:77951647619

SN - 1944-8244

VL - 1

SP - 1383

EP - 1386

JO - ACS Applied Materials and Interfaces

JF - ACS Applied Materials and Interfaces

IS - 7

ER -

Cellulose nanocrystal/gold nanoparticle composite as a matrix for enzyme immobilization

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Keywords

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