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.
| Published in | Journal of Plant Sciences (Volume 3, Issue 6) |
| DOI | 10.11648/j.jps.20150306.17 |
| Page(s) | 337-341 |
| Creative Commons |
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), 2015. Published by Science Publishing Group |
Amaranth, α-Amylase, Proteinaceous Inhibitor, Inhibitory Activity
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APA Style
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
ACS 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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Download@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://article.sciencepublishinggroup.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}
}
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 PY - 2015 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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