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Ethylene glycol and the thermostability of trypsin in a reverse micelle system

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Abstract

The influence of ethylene glycol (EG) on the kinetics of hydrolysis of N-α-benzoyl-L-arginine ethyl ether catalyzed by trypsin encapsulated in sodium bis-(2-ethylhexyl)sulfosuccinate (AOT)-based reverse micelles was studied at different temperatures. Ethylene glycol was shown to shift the range of the trypsin activity in the reverse micelles towards higher temperatures. Infrared spectroscopy showed a stabilizing effect of EG on the secondary structure of the protein in the system of reverse micelles. Electron spin resonance spectroscopy showed that the solubilized protein affected the interactions of EG with the polar head groups of AOT and altered the rigidity of the micellar matrix. The results indicate that EG increases the thermostability of the solubilized enzyme in microemulsion media by two mechanisms.

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Abbreviations

EG:

ethylene glycol

BAEE:

N-α-benzoyl-L-arginine ethyl ether

AOT:

sodium bis-(2-ethylhexyl)sulfosuccinate

ESR:

electron spin resonance

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Authors and Affiliations

  1. Kazan Institute of Biochemistry and Biophysics, Russian Academy of Sciences, 420111, Kazan, P. Box 30, Russia

    E. A. Stupishina, R. N. Khamidullin, N. N. Vylegzhanina, D. A. Faizullin & Yu. F. Zuev

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  1. E. A. Stupishina
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  2. R. N. Khamidullin
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  3. N. N. Vylegzhanina
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  4. D. A. Faizullin
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  5. Yu. F. Zuev
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Correspondence to Yu. F. Zuev.

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Original Russian Text © E. A. Stupishina, R. N. Khamidullin, N.N. Vylegzhanina, D. A. Faizullin, Yu. F. Zuev, 2006, published in Biokhimiya, 2006, Vol. 71, No. 5, pp. 660–665.

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Stupishina, E.A., Khamidullin, R.N., Vylegzhanina, N.N. et al. Ethylene glycol and the thermostability of trypsin in a reverse micelle system. Biochemistry (Moscow) 71, 533–537 (2006). https://doi.org/10.1134/S0006297906050105

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  • DOI: https://doi.org/10.1134/S0006297906050105

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