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Properties and Specific Functional Features of Wheat Grain α-Amylase/Subtilisin Inhibitor

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Abstract

A protein bifunctional inhibitor of endogenous α-amylase and subtilisin has been isolated from wheat grain and purified. The inhibitor specifically inactivates α-amylase isozymes with high isoelectric point values (group α-AMY1) and has almost no effect on the α-AMY2 isozymes with low isoelectric point values. This enzyme does not belong to glycoproteins and has a molecular weight of 21 kDa and an isoelectric point of 7.2. The protein displays a relatively high thermostability and pH optimum of 8.0; its inhibitory activity requires the presence of Ca2+ cations. The inhibition of excess α-amylase in wheat grain with a low falling number by the purified protein is studied.

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Authors and Affiliations

  1. Aitkhozhin Institute of Molecular Biology and Biochemistry, Almaty, 050012, Kazakhstan

    V. A. Kuzovlev, Zh. D. Beskempirova, O. V. Fursov & A. A. Khakimzhanov

  2. Almaty University of Technology, Almaty, 050012, Kazakhstan

    D. A. Shansharova

Authors
  1. V. A. Kuzovlev
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  2. Zh. D. Beskempirova
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  3. D. A. Shansharova
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  4. O. V. Fursov
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  5. A. A. Khakimzhanov
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Correspondence to A. A. Khakimzhanov.

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Original Russian Text © V.A. Kuzovlev, Zh.D. Beskempirova, D.A. Shansharova, O.V. Fursov, A.A. Khakimzhanov, 2018, published in Prikladnaya Biokhimiya i Mikrobiologiya, 2018, Vol. 54, No. 2, pp. 206–211.

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Kuzovlev, V.A., Beskempirova, Z.D., Shansharova, D.A. et al. Properties and Specific Functional Features of Wheat Grain α-Amylase/Subtilisin Inhibitor. Appl Biochem Microbiol 54, 215–219 (2018). https://doi.org/10.1134/S0003683818020059

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  • DOI: https://doi.org/10.1134/S0003683818020059

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