Back to Search
Start Over
Facile Mechanochemical Functionalization of Hydrophobic Substrates for Single-Walled Carbon Nanotube Based Optical Reporters of Hydrolase Activity.
- Source :
-
ACS applied materials & interfaces [ACS Appl Mater Interfaces] 2024 Nov 13; Vol. 16 (45), pp. 62547-62556. Date of Electronic Publication: 2024 Oct 30. - Publication Year :
- 2024
-
Abstract
- Single walled carbon nanotubes (SWCNT) have recently been demonstrated as modular, near-infrared (nIR) probes for reporting hydrolase activity; however, these have been limited to naturally amphipathic substrate targets used to noncovalently functionalize the hydrophobic nanoparticles. Many relevant substrate targets are hydrophobic (such as recalcitrant biomass) and pose a challenge for modular functionalization. In this work, a facile mechanochemistry approach was used to couple insoluble substrates, such as lignin, to SWCNT using l-lysine amino acid as a linker and tip sonication as the mechanochemical energy source. The proposed coupling mechanism is ion pairing between the lysine amines and lignin carboxylic acids, as evidenced by FTIR, NMR, SEM, and elemental analyses. The limits of detection for the lignin-lysine-SWCNT (LLS) probe were established using commercial enzymes and found to be 0.25 ppm (volume basis) of the formulated product. Real-world use of the LLS probes was shown by evaluating soil hydrolase activities of soil samples gathered from different corn root proximal locations and soil types. Additionally, the probes were used to determine the effect of storage temperature on the measured enzyme response. The modularity of this mechanochemical functionalization approach is demonstrated with other substrates such as zein and 9-anthracenecarboxylic acid, which further corroborate the mechanochemical mechanism.
Details
- Language :
- English
- ISSN :
- 1944-8252
- Volume :
- 16
- Issue :
- 45
- Database :
- MEDLINE
- Journal :
- ACS applied materials & interfaces
- Publication Type :
- Academic Journal
- Accession number :
- 39474933
- Full Text :
- https://doi.org/10.1021/acsami.4c13800