Proteomic and characterization of alpha-amylase inhibitor from mungbean (Vigna radiate) | โปรตีโอมิกและคุณลักษณะของ alpha-amylase inhibitor จากถั่วเขียว
2008
Anussorn Wisessing(Kasetsart University. Bangkhen Campus, Bangkok (Thailand). Faculty of Science. Department of Biochemistry) | Arunee Engkagul(Kasetsart University. Bangkhen Campus, Bangkok (Thailand). Faculty of Science. Department of Biochemistry) | Arunee Wongpiyasatid(Kasetsart University. Bangkhen Campus, Bangkok (Thailand). Faculty of Science. Department of Applied Radiation and Isotopes) | Kiattawee Chuwongkomon(Kasetsart University. Bangkhen Campus, Bangkok (Thailand). Faculty of Science. Department of Biochemistry) E-mail:[email protected]
Callosobruchus maculatus causes damaging of storage mungbean seeds, leading to economical losses. For this reason the use of alpha-amylase inhibitors to interfere with the pest digestion process has been an interesting alternative as a biocontrolling agent. The studies of mutant mungbean by gramma radiation, M5-16, found that the alpha-amylase inhibitor from the mutant lines was more inhibitory effective to C. maculates alpha-amylase than its wild type, KPS1 (Engkagul et al., 2004). To investigate this mechanism, both proteomics and biochemical characterization were employed. The alpha-amylase inhibitor from the mungbean seed, M5-16, was purified in two step procedures involving ammonium sulfate precipitation and gel filtration chromatography using sephadex G-100. This alpha-amylase inhibitor exits as a monomer and has a molecular weight of 27 kDa. Moreover, It is very interesting that the alpha-amylase inhibitor from the mungbean seed can inhibit C. maculates alpha-amylase but can not inhibit human salivary alpha-amylase. 2D gel electrophoresis suggested that gamma-induced mutant line decrease expression of alpha-amylase inhibitor and other protein comparing with wild type.
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