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Lignin Interacting with α-glucosidase and its Inhibitory Effect on the Enzymatic Activity

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Abstract

In this paper, we find firstly that lignin is an effective inhibitor against α-glucosidase, with minimized IC50 value of 0.076 μM which is much lower than that of acarbose (0.66 mM), a market diabetes healer, and it can competitively inhibit enzymatic activity with Ki value of 0.3 × 10−5 M. Meanwhile, lignin can interact with α-glucosidase to form 1:1 complex with the binding constant of 1.39 × 106 M−1 at 293 K. The binding of lignin to α-glucosidase is mainly driven by hydrophobic interaction and hydrogen bond, with binding distance of 3.54 nm. The formation of lignin-α-glucosidase complex results in the alteration of α-helix structure and aromatic amino sides and the increase of protein granule volume. Furthermore, the lignin binds to α-glucosidase in the form of the first order exponential decay function. This work would be significant for the exploration of lignin as food functional factor.

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Acknowledgments

This work is supported by the National Natural Science Foundation of China (Grant Nos. 31101354 and 21235003) and Shanghai Science and Technology Committee (11DZ2272100).

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Authors and Affiliations

  1. Shanghai Key Laboratory of Bio-Energy Crops, School of Life Sciences, Shanghai University, Shanghai, 200444, People’s Republic of China

    Yangyang Chen, Ying Liu, Juan Zhang & Genxi Li

  2. Department of Biochemistry and State Key Laboratory of Pharmaceutical Biotechnology, Nanjing University, Nanjing, 210093, People’s Republic of China

    Xiaoxi Li & Genxi Li

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  1. Yangyang Chen
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  2. Ying Liu
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  3. Xiaoxi Li
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  4. Juan Zhang
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Correspondence to Juan Zhang.

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Chen, Y., Liu, Y., Li, X. et al. Lignin Interacting with α-glucosidase and its Inhibitory Effect on the Enzymatic Activity. Food Biophysics 10, 264–272 (2015). https://doi.org/10.1007/s11483-014-9383-y

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