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

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

Research output: Contribution to journalArticle

113 Citations (Scopus)

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 languageEnglish
Pages (from-to)1383-1386
Number of pages4
JournalACS Applied Materials and Interfaces
Volume1
Issue number7
DOIs
Publication statusPublished - 29 Jul 2009
Externally publishedYes

Fingerprint

alcohol oxidase
Enzyme immobilization
Cellulose
Gold
Nanocrystals
Enzymes
Cyclodextrins
Transferases
Nanoparticles
Composite materials
Alcohols
Catalyst activity
Nanocomposites
Testing
Oxidoreductases

Keywords

  • cellulose nanocrystals
  • CGTase
  • enzyme
  • gold nanoparticles
  • immobilization

ASJC Scopus subject areas

  • Materials Science(all)

Cite this

Cellulose nanocrystal/gold nanoparticle composite as a matrix for enzyme immobilization. / Mahmoud, Khaled; Male, Keith B.; Hrapovic, Sabahudin; Luong, John H T.

In: ACS Applied Materials and Interfaces, Vol. 1, No. 7, 29.07.2009, p. 1383-1386.

Research output: Contribution to journalArticle

Mahmoud, Khaled ; Male, Keith B. ; Hrapovic, Sabahudin ; Luong, John H T. / Cellulose nanocrystal/gold nanoparticle composite as a matrix for enzyme immobilization. In: ACS Applied Materials and Interfaces. 2009 ; Vol. 1, No. 7. pp. 1383-1386.
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