Earlier UV-VIS study of α-amylase activity suggests that the protein is inactivated in the presence of caffeine and liberates a smaller amount of sugar from starch hydrolysis. The purpose of this FTIR study is to understand what happens at the molecular level when caffeine interacts with the protein. The broad peak at around 1636 cm<sup>-1 </sup>(C=O group) increases in intensity (absorbance) when caffeine is added to protein. Also, as the temperature of protein-caffeine solution is increased from 20 °C to 39, 67, 95 °C, there is a consistent increase in the absorbance values. Interestingly, the cooling of the solutions to 20 °C reduces the peak intensity to that of the 20 °C value except for that of 95 °C, in which case there is no change in intensity after cooling. These results together with those of pure protein solutions (without any caffeine) are explained by considering changes in the H-bonding pattern around the protein structure.

FTIR study of α-amylase -caffeine interaction at different temperatures

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