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Evaluation of the enzymatic activity of catalase in aqueous mediums of basic amino acids based deep eutectic solvents

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Abstract

We analyzed catalase's function, structure, and thermal stability in two basic amino acid-based deep eutectic solvents due to the importance of studying the enzymatic behavior in suitable non-aqueous media. We used various UV-visible spectroscopic methods, fluorescence, and circular dichroism (CD). Combining arginine with glycerol and lysine with glycerol was applied to form two distinct amino acid-based deep eutectic solvents.

Kinetic studies showed that forming an intricate hydrogen bond network between glycerol and amino acid components in arginine or lysine-based aqueous deep eutectic solvents of 45% and 40%, respectively, keeps the catalase activity near 50%. Our outcomes demonstrated that the intrinsic fluorescence of the catalase is quenched by increasing the concentration of these solvents via a static mechanism. Also, CD results have further represented remarkable changes in arginine-glycerol and lysine-glycerol solvents with a diminished α-helical content and an increase in β-pleated sheets content. Studies of the thermal stability of catalase in the presence of these solvents showed that with increasing concentration of these solvents, the thermal stability of enzyme (Tm and ΔG° values) decreases.

Finally, the above data suggested that arginine and lysine with chaotropic factors of guanidine and ammonium in their functional group, respectively, act as influential factors in the activity and structural stability of the enzyme.

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Acknowledgments

The Research Council of Kharazmi University has supported our research. We gratefully acknowledge their support.

Funding

Funding was provided by Kharazmi University, (Grant Number 1402).

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Authors and Affiliations

  1. Department of Cell & Molecular Sciences, Faculty of Biological Sciences, Kharazmi University, Tehran, Iran

    Elnaz Assar & Adeleh Divsalar

  2. Iran National Standard Organization Science and Technology Education Center, Tehran, Iran

    Tara Jafari

  3. Institute of Biochemistry and Biophysics, University of Tehran, Tehran, Iran

    Ali Akbar Saboury

  4. State Key Laboratory of Oncogenes and Related Genes, Institute for Personalized Medicine, School of Biomedical Engineering, Shanghai Jiao Tong University, Shanghai, 200030, China

    Behafarid Ghalandari & **anting Ding

Authors
  1. Elnaz Assar
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  2. Adeleh Divsalar
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  5. Behafarid Ghalandari
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  6. **anting Ding
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Correspondence to Adeleh Divsalar.

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Assar, E., Divsalar, A., Jafari, T. et al. Evaluation of the enzymatic activity of catalase in aqueous mediums of basic amino acids based deep eutectic solvents. J IRAN CHEM SOC 20, 2879–2888 (2023). https://doi.org/10.1007/s13738-023-02884-w

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  • DOI: https://doi.org/10.1007/s13738-023-02884-w

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