Journal of Plant Sciences

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Biochemical Nature of a Natural α-Amylase Inhibitor from Wild Amaranth (Amaranthus paniculatus) Seeds

Received: 31 October 2014    Accepted: 10 November 2014    Published: 05 December 2015
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Abstract

Endogenous á-amylase inhibitors exist widely in animals, plants and microorganisms. These inhibitors show remarkable structure variety with different modes of inhibition and specificity against different á-amylases. To explore the alpha-amylase inhibitors in wild amaranth, a novel proteinaceous inhibitor of á-amylase, named WAI-1, was purified and its structure and function were investigated in this study. WAI-1 was one of the smallest proteinaceous inhibitors with a molecular weight of 986.5 Da. The structural analysis exposed that WAI-1 was a cyclic nonapeptide of nine amino acids, with pyroglutamate as the N-terminal. The hydrolysis in hydrochloric acid solution opened the loop of the side chain of WAI-1 at the N-terminal, but did not affect its inhibitory activity. However, the hydrolysis by trypsin disconnected arginine at the c-terminal, causing almost a full loss of its inhibitory activity. WAI-1 had good heat stability and specific inhibitory activity against á-amylases of the insects. The integrity of the molecular loop structure of WAI-1 was critical for its stability and inhibitory activity.

DOI 10.11648/j.jps.20150306.17
Published in Journal of Plant Sciences (Volume 3, Issue 6, December 2015)
Page(s) 337-341
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This is an Open Access article, distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution and reproduction in any medium or format, provided the original work is properly cited.

Copyright

Copyright © The Author(s), 2024. Published by Science Publishing Group

Keywords

Amaranth, α-Amylase, Proteinaceous Inhibitor, Inhibitory Activity

References
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Author Information
  • College of Bioscience and Biotechnology, Yangzhou University, Yangzhou, China

  • College of Animal Science and Technology, Yangzhou University, Yangzhou, China

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    Wang Lin, Ji Dejun. (2015). Biochemical Nature of a Natural α-Amylase Inhibitor from Wild Amaranth (Amaranthus paniculatus) Seeds. Journal of Plant Sciences, 3(6), 337-341. https://doi.org/10.11648/j.jps.20150306.17

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    Wang Lin; Ji Dejun. Biochemical Nature of a Natural α-Amylase Inhibitor from Wild Amaranth (Amaranthus paniculatus) Seeds. J. Plant Sci. 2015, 3(6), 337-341. doi: 10.11648/j.jps.20150306.17

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    AMA Style

    Wang Lin, Ji Dejun. Biochemical Nature of a Natural α-Amylase Inhibitor from Wild Amaranth (Amaranthus paniculatus) Seeds. J Plant Sci. 2015;3(6):337-341. doi: 10.11648/j.jps.20150306.17

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  • @article{10.11648/j.jps.20150306.17,
      author = {Wang Lin and Ji Dejun},
      title = {Biochemical Nature of a Natural α-Amylase Inhibitor from Wild Amaranth (Amaranthus paniculatus) Seeds},
      journal = {Journal of Plant Sciences},
      volume = {3},
      number = {6},
      pages = {337-341},
      doi = {10.11648/j.jps.20150306.17},
      url = {https://doi.org/10.11648/j.jps.20150306.17},
      eprint = {https://download.sciencepg.com/pdf/10.11648.j.jps.20150306.17},
      abstract = {Endogenous á-amylase inhibitors exist widely in animals, plants and microorganisms. These inhibitors show remarkable structure variety with different modes of inhibition and specificity against different á-amylases. To explore the alpha-amylase inhibitors in wild amaranth, a novel proteinaceous inhibitor of á-amylase, named WAI-1, was purified and its structure and function were investigated in this study. WAI-1 was one of the smallest proteinaceous inhibitors with a molecular weight of 986.5 Da. The structural analysis exposed that WAI-1 was a cyclic nonapeptide of nine amino acids, with pyroglutamate as the N-terminal. The hydrolysis in hydrochloric acid solution opened the loop of the side chain of WAI-1 at the N-terminal, but did not affect its inhibitory activity. However, the hydrolysis by trypsin disconnected arginine at the c-terminal, causing almost a full loss of its inhibitory activity. WAI-1 had good heat stability and specific inhibitory activity against á-amylases of the insects. The integrity of the molecular loop structure of WAI-1 was critical for its stability and inhibitory activity.},
     year = {2015}
    }
    

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  • TY  - JOUR
    T1  - Biochemical Nature of a Natural α-Amylase Inhibitor from Wild Amaranth (Amaranthus paniculatus) Seeds
    AU  - Wang Lin
    AU  - Ji Dejun
    Y1  - 2015/12/05
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    N1  - https://doi.org/10.11648/j.jps.20150306.17
    DO  - 10.11648/j.jps.20150306.17
    T2  - Journal of Plant Sciences
    JF  - Journal of Plant Sciences
    JO  - Journal of Plant Sciences
    SP  - 337
    EP  - 341
    PB  - Science Publishing Group
    SN  - 2331-0731
    UR  - https://doi.org/10.11648/j.jps.20150306.17
    AB  - Endogenous á-amylase inhibitors exist widely in animals, plants and microorganisms. These inhibitors show remarkable structure variety with different modes of inhibition and specificity against different á-amylases. To explore the alpha-amylase inhibitors in wild amaranth, a novel proteinaceous inhibitor of á-amylase, named WAI-1, was purified and its structure and function were investigated in this study. WAI-1 was one of the smallest proteinaceous inhibitors with a molecular weight of 986.5 Da. The structural analysis exposed that WAI-1 was a cyclic nonapeptide of nine amino acids, with pyroglutamate as the N-terminal. The hydrolysis in hydrochloric acid solution opened the loop of the side chain of WAI-1 at the N-terminal, but did not affect its inhibitory activity. However, the hydrolysis by trypsin disconnected arginine at the c-terminal, causing almost a full loss of its inhibitory activity. WAI-1 had good heat stability and specific inhibitory activity against á-amylases of the insects. The integrity of the molecular loop structure of WAI-1 was critical for its stability and inhibitory activity.
    VL  - 3
    IS  - 6
    ER  - 

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