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Enzymatic Performance of α-Amylase in the Presence of Organic Solvents: Activity, Stability, and Bioinformatic Studies. | LitMetric

AI Article Synopsis

  • Enzymatic reactions are affected by organic solvents, which can enhance enzyme stability and activity but also potentially cause inactivation.
  • A study on α-amylase (Taka-amylase) found it retains 20-25% activity in ethanol and ether, with ether offering better stability.
  • Molecular simulations showed that specific structural regions in Taka-amylase are vulnerable to destabilization by solvents, but the enzyme maintains stability and activity better in ether and ethanol due to their effects on its structure.

Article Abstract

Enzymatic reactions can be modulated by the incorporation of organic solvents, leading to alterations in enzyme stability, activity, and reaction rates. These solvents create a favorable microenvironment that enables hydrophobic reactions, facilities enzyme-substrate complex formation, and reduces undesirable water-dependent side reactions. However, it is crucial to understand the impact of organic solvents on enzymatic activity, as they can also induce enzyme inactivation. In this study, the enzymatic performance of 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.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC11041543PMC
http://dx.doi.org/10.1177/11779322241234767DOI Listing

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