TY - JOUR AU - Buddhapala Wongkaew, AU - Porntip Wongkaew, AU - Panupong Thanutong, AU - ChitsanuphongThanutong, PY - 2018/03/28 Y2 - 2024/03/29 TI - NANOSTRUCTURAL CHARACTERIZATION OF GLUTATHIONE- S-TRANSFERASE IMMOBILIZING CHITOSAN MODIFIED SCREEN PRINTED CARBON ELECTRODE BY ATOMIC FORCE MICROSCOPY JF - GEOMATE Journal JA - INTERNATIONAL JOURNAL OF GEOMATE VL - 14 IS - 43 SE - Articles DO - UR - https://geomatejournal.com/geomate/article/view/1687 SP - 132-139 AB - <p>Immobilization of a bio-recognition element to the surface of a functional working electrode is<br>fundamental for effective biosensor development. In this study, the enzyme glutathione-s-transferase (GST)<br>that constitutes a protein superfamily involving various distinct chemical transformations was introduces as a<br>versatile tool for the sensing of environmental toxicants. Functional electrode surface was made by self-<br>assembly of a great bioscaffold chitosan onto screen-printed carbon electrode surface concerning to its<br>excellent covalent bonding binding of biomolecules. To enhance the enzyme proximity, glutaraldehyde was<br>employed as an assisting bifunctional cross-linker. The self assembled chitosan layer and the GST<br>immobilizing nanostructural features were explored by morphological imaging and several quantitative<br>analyses such as surface grain size and distribution, power spectrum density (PSD) algorithm, fractal<br>dimension character and other important surface roughness parameters via atomic force microscopy (AFM).<br>Vertical aggregation of the successive layer was clearly verified in all quantitative approaches. Exceedingly,<br>a better understanding in the direction of aggregation along with the growth mechanism was obtained by PSD<br>analysis and the fractal dimension values gained around 2.27 for modified chitosan surface and 2.02 for GST<br>immobilized chitosan modified screen-printed carbon basement could thus imply for the diffusion limited<br>model in this growth mechanism.</p> ER -