Enzymatic Performance of < em > Aspergillus oryzae < /em > α-Amylase in the Presence of Organic Solvents: Activity, Stability, and Bioinformatic Studies

In this study, the enzymatic performance of Aspergillus oryzae α-amylase (Taka-amylase) in various organic solvents both experimentally and computationally was investigated. The results demonstrated that ethanol and ether sustain Taka-amylase activity up to 20% to 25% of the organic solvents, with ether providing twice the stability of ethanol. Molecular dynamics simulations further revealed that Taka-amylase has a more stable structure in ether and ethanol relative to other organic solvents. In addition, the analysis showed that the loop located near the active site in the AB-domain is a vulnerable site for enzyme destabilization when exposed to organic solvents. The ability of Taka-amylase to preserve the secondary loop structure in ether and ethanol contributed to the enzyme's activity. In addition, the solvent accessibility surface area of Taka-amylase is distributed throughout all enzyme structures, thereby contributing to the instability of Taka-amylase in the presence of most organic solvents.PMID:38660393 | PMC:PMC11041543 | DOI:10.1177/11779322241234767
Source: Bioinformatics and Biology Insights - Category: Bioinformatics Authors: Source Type: research