Activity and Stability of Nanoconfined Alpha-Amylase in Mesoporous Silica.

Mesoporous silica particles (MSPs) have been studied for their potential therapeutic uses in controlling obesity and diabetes. Previous studies have shown that the level of digestion of starch by α-amylase is considerably reduced in the presence of MSPs, and it has been shown to be caused by the adsorption of α-amylase by MSPs. In this study, we tested a hypothesis of enzymatic deactivation and measured the activity of α-amylase together with MSPs (SBA-15) using comparably small CNP-G3 (2-chloro-4-nitrophenyl alpha-d-maltotrioside) as a substrate. We showed that pore-incorporated α-amylase was active and displayed higher activity and stability compared to amylase in solution (the control). We attribute this to physical effects: the coadsorption of CNP-G3 on the MSPs and the relatively snug fit of the amylase in the pores. Biosorption in this article refers to the process of removal or adsorption of α-amylase from its solution phase into the same solution dispersed in, or adsorbed on, the MSPs. Large quantities of α-amylase were biosorbed (about 21% w/w) on the MSPs, and high values of the maximum reaction rate (

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© 2023 The Authors. Published by American Chemical Society.

Déclaration de conflit d'intérêts

The authors declare the following competing financial interest(s): Muhammad Naeem Iqbal has been an employee and Tore Bengtsson holds shares in Sigrid Therapeutics AB.