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Cited by 179

The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.

Structure, Function, and Stability of Enzymes Covalently Attached to Single-Walled Carbon Nanotubes

Asuri, Prashanth, Bale, Shyam Sundhar, Pangule, Ravindra C., Shah, Dhiral A., Kane, Ravi S., Dordick, Jonathan S.·2007·Langmuir

Abstract

We describe the structure, activity, and stability of enzymes covalently attached to single-walled carbon nanotubes (SWNTs). Conjugates of SWNTs with three functionally unrelated enzymes-horseradish peroxidase, subtilisin Carlsberg, and chicken egg white lysozyme-were found to be soluble in aqueous solutions. Furthermore, characterization of the secondary and tertiary structure of the immobilized proteins by circular dichroism and fluorescence spectroscopies, respectively, and determination of enzyme kinetics revealed that the enzymes retained a high fraction of their native structure and activity upon attachment to SWNTs. The SWNT-enzyme conjugates were also more stable in guanidine hydrochloride (GdnHCl) and at elevated temperatures relative to their solution counterparts. Thus, these protein conjugates represent novel preparations that possess the attributes of both soluble enzymes-high activity and low diffusional resistance-and immobilized enzymes-high stability-making them attractive choices for applications ranging from diagnostics and sensing to drug delivery.

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Metadata

Authors
Asuri, P., Bale, S. S., Pangule, R. C., Shah, D. A., Kane, R. S., & Dordick, J. S.
Venue
Langmuir
Published
2007-10-18
Volume
23
Issue
24
Pages
12318-12321
ISSN
  • 0743-7463 (ISSN-L)
  • 1520-5827
OpenAlex
W2019873707
Cited by
179
References
1
FWCI
4.79
Type
journal article
Language
en
Open access
closed

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