 ผลงานตีพิมพ์ในวารสารวิชาการOptimization of one-step real-time reverse transcription-polymerase chain reaction assays for norovirus detection and molecular epidemiology of noroviruses in thailandผู้แต่ง: Neesanant, P.,  Dr.Theerapol Sirinarumitr, Associate Professor , Dr.Sirirak Chantakru, Assistant Professor, Dr.Ukadej Boonyaprakob, Assistant Professor , Chuwongkomon, K., Bodhidatta, L., Sethabutr, O., Abente, E.J., Supawat, K., Mason, C.J., วารสาร:  
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 หัวเรื่อง:ไม่มีชื่อไทย (ชื่ออังกฤษ : Proteomic and Characterization of ?-amylase Inhibitor from Mungbean (Vigna radiate)) ผู้เขียน:อนุสสรณ์ วิเศษสิงห์, ดร.อรุณี อิงคากุล, ผู้ช่วยศาสตราจารย์, นางอรุณี วงศ์ปิยะสถิตย์, ศาสตราจารย์, Kiattawee Chuwongkomon สื่อสิ่งพิมพ์:pdf AbstractCallosobruchus maculatus, the insect pest, causes damaging to stored mungbean seeds leading to economical losses. For this reason the use of ?-amylase inhibitors to interfere the pest digestion process has been an interesting alternative as a biocontrolling agent. The studies of gamma irradiated mungbean mutant, M5-16, demonstrated that ?-amylase inhibitor from the mutant line was more inhibitory effective on C. maculatus ?-amylase than its wild type, KPS1. To investigate this mechanism, both proteomics and biochemical characterization were employed. The ?-amylase inhibitor from mungbean seed, M5-16, was purified in a two-step procedure involving ammonium sulfate precipitation and gel filtration chromatography using a sephadex G-100 column. This ?-amylase inhibitor existed as a monomer and had a molecular weight of 27 kDa. Moreover, It was very interesting that ?-amylase inhibitor from the mungbean seed inhibited C. maculatus ?-amylase but did not inhibit human salivary ?-amylase. 2D gel electrophoresis suggested that the gamma-induced mutant line has decreased expression of ?-amylase inhibitor and other proteins comparing with its wild type. |
หัวเรื่อง:ไม่มีชื่อไทย (ชื่ออังกฤษ : Purification and Characterization of C. maculatus ?-amylase) ผู้เขียน:อนุสสรณ์ วิเศษสิงห์, ดร.อรุณี อิงคากุล, ผู้ช่วยศาสตราจารย์, นางอรุณี วงศ์ปิยะสถิตย์, ศาสตราจารย์, Kiattawee Chuwongkomon สื่อสิ่งพิมพ์:pdf AbstractCallosobruchus maculatus causes damaging of storage mungbean seeds. Understanding control mechanism of a-amylase activity is essential for developing method for the insect control. In this study, C. maculatus a-amylase was purified and characterized. Purification was carried out using self-coupled ?-cyclodextrin sepharose 6B affinity column. It was found that C. maculatus ?-amylase had one isoform with a molecular weight of 50 kDa. The purified enzyme with specific activity of 182.78 U mg protein-1, showing optimum pH at around 5-6 and optimum temperature at 50-60 ?C. |
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