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The properties of invertase, covalently immobilized at activated carbon

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Abstract

The covalent immobilization of yeast invertase with glutaraldehyde at activated carbon, modified preliminarily by urea and dimethyl formamide treatment, has been established. Some physicochemical properties of the immobilized and native enzyme in water and water-organic solutions have been studied. Hydrolytic, as well as transferase enzyme characteristics have changed after immobilization. The optimal conditions for hydrolytic and transferase activity of immobilized invertase are pH 6.0 and 7.0, respectively. The optimum temperature for the immobilized enzyme is 30°C. The conversion degree of isoamyl alcohol depends on the substrate and enzyme concentrations in medium, holdup time and organic phase quantity in the reaction medium.

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Authors and Affiliations

  1. National of University Uzbekistan, Tashkent, 100174, Uzbekistan

    D. T. Mirzarakhmetova, D. B. Dekhkonov & M. M. Rakhimov

  2. Tashkent Chemical-Techological Institute, Tashkent, 100011, Uzbekistan

    S. Kh. Abdurazakova

  3. Institute of Microbiology AcSci RUz, Tashkent, 100128, Uzbekistan

    Z. R. Akhmedova

Authors
  1. D. T. Mirzarakhmetova
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  2. D. B. Dekhkonov
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  3. M. M. Rakhimov
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  4. S. Kh. Abdurazakova
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  5. Z. R. Akhmedova
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Correspondence to D. T. Mirzarakhmetova.

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Original Russian Text © D.T. Mirzarakhmetova, D.B. Dekhkonov, M.M. Rakhimov, S.Kh. Abdurazakova, Z.R. Akhmedova, 2009, published in Prikladnaya Biokhimiya i Mikrobiologiya, 2009, Vol. 45, No. 3, pp. 287–291.

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Mirzarakhmetova, D.T., Dekhkonov, D.B., Rakhimov, M.M. et al. The properties of invertase, covalently immobilized at activated carbon. Appl Biochem Microbiol 45, 258–261 (2009). https://doi.org/10.1134/S000368380903003X

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  • DOI: https://doi.org/10.1134/S000368380903003X

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