Journal of Plant Sciences
Volume 3, Issue 6, December 2015, Pages: 337-341
Received: Oct. 31, 2014;
Accepted: Nov. 10, 2014;
Published: Dec. 5, 2015
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Wang Lin, College of Bioscience and Biotechnology, Yangzhou University, Yangzhou, China
Ji Dejun, College of Animal Science and Technology, Yangzhou University, Yangzhou, China
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.
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.
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