While most biochemical interactions of α-amylase occur in aqueous media, the studies using FTIR (Fourier-transform infrared) spectroscopy are often limited to non-aqueous media due to high water background.  In this study we successfully conduct water-based IR peak absorbance tests for α-amylase and find strong correlation and sensitivity for a new absorbance peak for the protein when its temperature is increased from 20<sup>o</sup>C to 90<sup>o</sup>C.  These results are explained by considering the rearrangement of some of the bonds around N, C, O and H atoms of the protein at high temperatures.

Investigating aqueous α-amylase restructuring under thermal stimuli

Where thousands of chemistry professionals meet to share ideas and advance scientific and technical knowledge. Spring 2023 abstracts, posters, and presentations will launch at the end of March.

ACS Spring 2023

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.