Volume 3, Issue 6, December 2015, Page: 337-341
Biochemical Nature of a Natural α-Amylase Inhibitor from Wild Amaranth (Amaranthus paniculatus) Seeds
Wang Lin, College of Bioscience and Biotechnology, Yangzhou University, Yangzhou, China
Ji Dejun, College of Animal Science and Technology, Yangzhou University, Yangzhou, China
Received: Oct. 31, 2014;       Accepted: Nov. 10, 2014;       Published: Dec. 5, 2015
DOI: 10.11648/j.jps.20150306.17      View  4338      Downloads  101
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.
Amaranth, α-Amylase, Proteinaceous Inhibitor, Inhibitory Activity
To cite this article
Wang Lin, Ji Dejun, Biochemical Nature of a Natural α-Amylase Inhibitor from Wild Amaranth (Amaranthus paniculatus) Seeds, Journal of Plant Sciences. Vol. 3, No. 6, 2015, pp. 337-341. doi: 10.11648/j.jps.20150306.17
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