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.
Jun-Ichi Sumitani; Yoshimasa Tsujimoto; Takashi Kawaguchi; Mtoo Arai.Cloning and Secretive Expression of the Gene Encoding the Proteinaceous α-Amylase Inhibitor Paim from Streptomyces Corchorusii[J]. Journal of Bioscience and Bioengineering, 2000, 90(2): 214—216.
Svensson B, Fukuda K, Nielsen PK, Bønsager BC.Proteinaceous alpha-amylase inhibitors [J]. Biochimica et Biophysica Acta, 2004, 1696(2):145-156.
Wang Lin. Progress in Research on Inhibitors of Insect Amylase[J].Chinese Agricultural Science Bulletin, 2006, 22(8): 397－400.
KATAOKA K, DIMAGNO E P. Effect of prolonged intraluminal alpha-amylase inhibition on eating, weight, and the small intestine of rats [J]. Nutrition. 1999, 15(2):123-129.
Vértesy L, Oeding V, Bender R, Zepf K, Nesemann G. Tendamistat (HOE 467), a tight-binding alpha-amylase inhibitor from Streptomyces tendae 4158. Isolation, biochemical properties [J], Eur J Biochem. 1984, 141(3):505-512.
Melo F R, Sales M P, Silva L S, Franco O L, Bloch C Jr, Ary M B.α-amylase inhibitors from cowpea seeds. Prot. Pept. Lett., 1999, 6: 387-392.
Giri AP, Kachole MS. Amylase inhibitors of pigeonpea (Cajanus cajan) seeds [J]. Phytochemistry. 1998, 47(2): 197-202.
Bloch C Jr, Richardson M. A new family of small (5 kDa) protein inhibitors of insect alpha-amylases from seeds or sorghum (Sorghum bicolar (L) Moench) have sequence homologies with wheat gamma-purothionins[J].FEBS Lett. 1991, 279(1):101-104.
Weselake RJ, Macgregor AW, Hill RD, Duckworth HW.Purification and characteristics of an endogenous α-amylase inhibitor from barley kernels[J].Plant Physiol. 1983, 73(4):1008-1012.
Iulek J, Franco OL, Silva M, Slivinski CT, Bloch C Jr, Rigden DJ, Grossi de Sá MF. Purification, biochemical characterisation and partial primary structure of a new alpha-amylase inhibitor from Secale cereale (rye) [J].Int J Biochem Cell Biol. 2000, 32(11-12):1195-1204.
Yamagata H, Kunimatsu K, Kamasaka H, Kuramoto T, Iwasaki T. Rice bifunctional α-amylase/subtilisin inhibitor: characterization, localization, and changes in developing and germinating seeds [J]. Biosci Biotechnol Biochem. 1998, 62(5):978-985.
Nakaguchi T, Arakawa T, Philo JS, Wen J, Ishimoto M, Yamaguchi H.Structural characterization of an α-amylase inhibitor from a wild common bean (Phaseolus vulgaris): insight into the common structural features of leguminous α-amylase inhibitors[J]. J Biochem. 1997, 121(2):350-354.
Le Berre-Anton V, Bompard-Gilles C, Payan F, Rougé P.Characterization and functional properties of the alpha-amylase inhibitor (α-AI) from kidney bean (Phaseolus vulgaris) seeds[J]. Biochim Biophys Acta. 1997, 1343(1):31-40.
Chagolla-Lopez A, Blanco-Labra A, Patthy A, Sánchez R, Pongor S.A novel alpha-amylase inhibitor from amaranth (Amaranthus hypocondriacus) seeds[J]. J Biol Chem. 1994, 269(38):23675-23680.
Yamada T, Hattori K, Ishimoto M.Purification and characterization of two alpha-amylase inhibitors from seeds of tepary bean (Phaseolus acutifolius A. Gray) [J]. Phytochemistry. 2001, 58(1):59-66.
Schimoler-O'Rourke R, Richardson M, Selitrennikoff CP. Zeamatin inhibits trypsin and α-amylase activities[J].Appl Environ Microbiol. 2001, 67(5):2365-2366.
Lalit Saxena, Bharti K. Iyer, Laxmi Ananthanarayan. Three phase partitioning as a novel method for purification of ragi (Eleusinecoracana) bifunctional amylase/protease inhibitor[J]. Process Biochemistry, 2007, 42(3): 491-495.
Wang L, Zhou TY, Wang XC, Liang SP. Purification and Characterization of a Novel α-Amylase Inhibitor from Wild Amaranth (Amaranthus paniculatus) Weeds [J]. Chinese Journal of Biochemistry and Molecular Biology,2004, 20(4): 434-439.
Peter Bernfeld. Amylases, α- and β-[J]. Methods in Enzymology, 1955(1): 149-158
Adediwura Fred-Jaiyesimi, Abo Kio, Wilkins Richard. α-Amylase inhibitory effect of 3β-olean-12-en-3-yl (9Z)-hexadec-9-enoate isolated from Spondias mombin leaf, [J]. Food Chemistry, 2009, 116(1):285-288.
Liang SP, Zhang DY, Pan X, Chen Q, Zhou PA. Properties and amino acid sequence of huwentoxin-I, a neurotoxin purified from the venom of the Chinese bird spider Selenocosmia huwena[J].Toxicon. 1993, 31(8):969-78.
Zhang PF, Chen P, Hu WJ, Liang SP. Huwentoxin-V, a novel insecticidal peptide toxin from the spider Selenocosmia huwena, and a natural mutant of the toxin: indicates the key amino acid residues related to the biological activity [J]. Toxicon. 2003, 42(1):15-20.
Ping Chen,Song Nie, Wei Mi, Xian-Chun Wang, Song-Ping Liang. De novo sequencing of tryptic peptides sulfonated by 4-sulfophenyl isothiocyanate for unambiguous protein identification using post-source decay matrix-assisted laser desorption/ionization mass spectrometry. Rapid Communications in Mass Spectrometry [J]. 2004, 18(2): 191–198.
Hashimoto T, Ohki K, Sakura N. . Hydrolytic cleavage of pyroglutamyl-peptide bond. I. The susceptibility of pyroglutamyl-peptide bond to dilute hydrochloric acid [J]. Chem Pharm Bull (Tokyo).1995, 43(12):2068-2074.