Event Title
Characterization of the Invertase-Sucrose Complex Using Surface-Enhanced Raman Scattering
Faculty Sponsor
Brian Gilbert
Location
Jereld R. Nicholson Library
Date
5-13-2011 3:00 PM
End Date
5-13-2011 4:30 PM
Subject Area
Chemistry (general)
Description
Understanding the relationship between protein structure and function is a hot topic of research. In this study we used the invertase-sucrose complex to analyze if SERS could be used to characterize changes in protein structure. Ideal conditions for SERS of the invertase were determined through multiple experiments varying pH and concentration. The optimal conditions were found to be pH 7 and 25 μg/mL invertase. Reference spectra were taken of invertase, sucrose, glucose, and fructose. The enzyme was mixed with sucrose and spectra were taken and compared to the reference spectra. Based on these preliminary results, the invertase-sucrose complex is detectable through SERS. One of the peaks seen in the complex that is not present in SERS of just invertase corresponds to B-sheet which indicates a conformational change. It could also indicate that invertase and the complex bind differently to the colloids.
Recommended Citation
Wolf, Amanda and Gilbert, Brian, "Characterization of the Invertase-Sucrose Complex Using Surface-Enhanced Raman Scattering" (2011). Science and Social Sciences. Event. Submission 1.
https://digitalcommons.linfield.edu/studsymp_sci/2011/all/1
Characterization of the Invertase-Sucrose Complex Using Surface-Enhanced Raman Scattering
Jereld R. Nicholson Library
Understanding the relationship between protein structure and function is a hot topic of research. In this study we used the invertase-sucrose complex to analyze if SERS could be used to characterize changes in protein structure. Ideal conditions for SERS of the invertase were determined through multiple experiments varying pH and concentration. The optimal conditions were found to be pH 7 and 25 μg/mL invertase. Reference spectra were taken of invertase, sucrose, glucose, and fructose. The enzyme was mixed with sucrose and spectra were taken and compared to the reference spectra. Based on these preliminary results, the invertase-sucrose complex is detectable through SERS. One of the peaks seen in the complex that is not present in SERS of just invertase corresponds to B-sheet which indicates a conformational change. It could also indicate that invertase and the complex bind differently to the colloids.
Comments
Presenter: Amanda Wolf