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Original Articles

α-Amylase Inhibitors from Some Cassia Species and Their Interaction with α-Amylase Potential for Crop Protection

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Pages 64-69 | Received 18 Sep 2017, Accepted 21 Feb 2018, Published online: 13 Mar 2018

References

  • Gatehouse, A.M.R., Boulter, D. and Hilder, V.A. (1992). Potential of plant-derived genes in the genetic manipulation of crops for insect resistance. In Biotechnology in Agriculture, Plant Genetic Manipulation for Crop Protection. Vol. 7, pp. 155–181. CAB International, Wallingford, UK.
  • Franco, O.L., Rigden, D.J., Melo, F.R. and Grossi-de-Sá, M.F. (2002). Plant α-amylase inhibitors and their interaction with insect α-amylases. The FEBS Journal. 269(2): 397–412.
  • Tyagi, B., Trivedi, N. and Dubey, A. (2014). α-Amylase inhibitor: a compelling plant defense mechanism against insect/pests. Environment and Ecology. 32(3): 995–999.
  • Schuler, H.T., Poppy, M.G., Kerry, B.R. and Denholm, L. (1998) Insect-resistant transgenic plants. Trends in Biotechnology. 16: 168–174. doi: 10.1016/S0167-7799(97)01171-2
  • Ryan, C.A. (1973). Proteolytic Enzymes and Their Inhibitors in Plants. Annual Review of Plant Physiology. 24: 173–196. doi: 10.1146/annurev.pp.24.060173.001133
  • Ishimoto, M., Yamada, T. and Kaga, A. (1999). Insecticidal activity of an α-amylase inhibitor-like protein resembling a putative precursor of α-amylase inhibitor in the common bean, Phaseolus vulgaris L. Biochimica et Biophysica Acta (BBA)-Protein Structure and Molecular Enzymology. 1432(1): 104–112.
  • Marshall, J.J. and Lauda, C.M. (1975). Purification and properties of phaseolamin, an inhibitor of α-amylase, from the kidney bean, Phaseolus vulgaris. Journal of Biological Chemistry. 250(20): 8030–8037.
  • Oyedemi, S., Koekemoer, T., Bradley, G., van de Venter, M. and Afolayan, A. (2013). In vitro anti-hyperglycemia properties of the aqueous stem bark extract from Strychnos henningsii (Gilg). International Journal of Diabetes in Developing Countries. 33(2): 120–127.
  • Mirkov, T.E., Wahlstrom, J.M., Hagiwara, K., Finardi-Filho, F., Kjemtrup, S. and Chrispeels, M.J. (1994). Evolutionary relationships among proteins in the phytohemagglutinin-arcelin-α-amylase inhibitor family of the common bean and its relatives. Plant Molecular Biology. 26(4): 1103–1113. doi: 10.1007/BF00040692
  • Bradford, M.M. (1976). A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Analytical Biochemistry. 72(1-2): 248–254. doi: 10.1016/0003-2697(76)90527-3
  • Bernfeld, P. (1955). Methods in Enzymology, In: Colowick, S.P. and Kaplan, N.O. (eds), 1, Academic Press, New York, 149–158.
  • Laemmli, U.K. (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227: 680–685. doi: 10.1038/227680a0
  • Roy, I. and Gupta, M.N. (2000). Purification of a‘double-headed’ inhibitor of α-amylase/Proteinase K from wheat germ by expanded bed chromatography. Bioseparation. 9(4): 239–245. doi: 10.1023/A:1008120025526
  • Muralikrishna, G. and Nirmala, M. (2005). Cereal α-amylases-an overview. Carbohydrate Polymer. 60: 163–173. doi: 10.1016/j.carbpol.2004.12.002
  • Giri, A.P. and Kachole, M.S. (1998). Amylase inhibitors of pigeonpea (Cajanus cajan) seeds. Phytochemistry. 47(2): 197–202.
  • Kumari, B., Sharma, P. and Nath, A.K. (2012). α-Amylase inhibitor in local Himalyan collections of Colocasia: isolation, purification, characterization and selectivity towards α-amylases from various sources. Pesticide Biochemistry and Physiology. 103(1): 49–55. doi: 10.1016/j.pestbp.2012.03.003
  • Wisessing, A., Engkagul, A., Wongpiyasatid, A. and Choowongkomon, K. (2010). Bio-chemical characterization of the α-amylase inhibitor in mungbeans and its application in inhibiting the growth of callosobruchus maculatus. Journal of Agricultural and Food Chemistry. 58(4): 2131–2137. doi: 10.1021/jf903411x
  • Ishimoto, M. and Kitamura, K. (1991). Effect of absence of seed α-amylase inhibitor on the growth inhibitory activity to Azuki bean weevil (Callosobruchus chinensis) in common bean (Phaseolus vulgaris L.). Japanese Journal of Breeding. 41(2): 231–240. doi: 10.1270/jsbbs1951.41.231
  • Ishimoto, M., Suzuki, K., Iwanaga, M., Kikuchi, F. and Kitamura, K. (1995). Variation of seed α-amylase inhibitors in the common bean. TAG Theoretical and Applied Genetics. 90(3): 425–429.
  • Baker, J.E., Woo, S.M., Throne, J.E. and Finney, P.L. (1991). Correlation of α-amylase inhibitor content in Eastern soft wheats with development parameters of the rice weevil (Coleoptera: Curculionidae). Environmental Entomology. 20(1): 53–60. doi: 10.1093/ee/20.1.53
  • Sanchez-Monge, R., Garcia-Casado, G., Malpica, J.M. and Salcedo, G. (1996). Inhibitory activities against heterologous α-amylases and in vitro allergenic reactivity of Einkorn wheats. Theoretical and Applied Genetics. 93(5-6): 745–750. doi: 10.1007/BF00224071
  • Prasadi, D.T., Umpathy, N.S. and Veeranna, R. (1996). Genotypic variation in cowpea (Vigna unguiculata) cultivars in relation to insect resistance. Journal of Plant Biochemistry and Bio-technology. 5(1): 47–49. doi: 10.1007/BF03262979
  • Jarrett, S.J., Marschke, R.J., Symons, M.H., Gibson, C.E., Henry, R.J. and Fox, G.P. (1997). Alpha-amylase/subtilisin inhibitor levels in Australian barleys. Journal of Cereal Science. 25(3): 261–266. doi: 10.1006/jcrs.1996.0084
  • Täufel, A., Böhm, H. and Flamme, W. (1997). Protein Inhibitors of Alpha-amylase in Mature and Germinating Grain of Rye (Secale cereale). Journal of Cereal Science. 25(3): 267–273. doi: 10.1006/jcrs.1996.0093
  • Oyedemi, S.O., Oyedemi, B.O., Ijeh, I.I., Ohanyerem, P.E., Coopoosamy, R.M. and Aiyegoro, O.A. (2017). Alpha-Amylase Inhibition and Antioxidative Capacity of Some Anti-diabetic Plants Used by the Traditional Healers in Southeastern Nigeria. The Scientific World Journal, 2017. pages 11, https://doi.org/10.1155/2017/3592491
  • Mulimani, V.H., Rudrappa, G. and Supriya, D. (1994). α-Amylase inhibitors in chick pea (Cicer arietinum L). Journal of the Science of Food and Agriculture. 64(4): 413–415. doi: 10.1002/jsfa.2740640404
  • Kneen, E. and Sandstedt, R.M. (1946). Distribution and general properties of an amylase inhibitor in cereals. Archives of Biochemistry and Biophysics. (9): 235–249.
  • Shainkin, R. and Birk, Y. (1970). α-amylase inhibitors from wheat isolation and characterization. Biochimica et Biophysica Acta (BBA)-Protein Structure. 221(3): 502–513. doi: 10.1016/0005-2795(70)90221-7
  • Rohn, S., Rawel, H.M. and Kroll, J. (2002). Inhibitory effects of plant phenols on the activity of selected enzymes. Journal of Agricultural and Food Chemistry. 50(12): 3566–3571. doi: 10.1021/jf011714b
  • Ho, M.F., Yin, X., Lajolo, F. and Whitaker, J.R. (1994). Naturally occurring α-amylase inhibitors: structure/function relationships. In Protein Structure-Function Relationships in Foods (pp. 89–119). Springer US.
  • Sanchez-Monge, R., Gomez, L., Garcia-Olmedo, F. and Salcedo, G. (1986). A tetrameric inhibitor of insect á-amylase from barley. FEBS Letters. 207(1): 105–109. doi: 10.1016/0014-5793(86)80021-7
  • Sasikiran, K., Rekha, M.R. and Padmaja, G. (2004). Purification and partial characterization of proteinase and α-amylase inhibitors from lesser yam (Dioscorea esculenta). International Journal of Food Properties, 7(2): 185–199. doi: 10.1081/JFP-120025395
  • Yang, M.Y., Zhang, X.Q., Ma, Y., Shen, J., Song, J.R. and Zhu, H.L. (2008). Purification and partial characterization of a glycoprotein á-amylase inhibitor from white kidney bean (Phaseolus vulgaris. L). Journal of Food Biochemistry. 32(1): 72–84. doi: 10.1111/j.1745-4514.2007.00147.x
  • Kokiladevi, E., Manickam, A. and Thayumanavan, B. (2005). Characterization of α-amylase inhibitor in Vigna sublobata. Botanical Bulletin of Academia Sinica. (46): 189–196
  • Kutty, A.V.M. and Pattabiraman, T.N. (1986). Isolation and characterization of an amylase inhibitor from sorghum seeds, specific for human enzymes. Journal of Agricultural and Food Chemistry. 34(3): 552–557. doi: 10.1021/jf00069a046

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