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- 저자 : ( Zihni Demirba ) (검색결과 2 건)
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Biryol Seda,Demirbağ Zihni,Erdoğan Pervin,DEMIR, ISMAIL 한국응용곤충학회 2022 Journal of Asia-Pacific Entomology Vol.25 No.1
Long-term and intensive use of synthetic insecticides to control the green peach aphid, Myzus persicae (Homo ptera: Aphididae) in agricultural production in the world has resulted in pest resistance and environmental pollution. The aim of the study was to develop an environmentally-friendly and effective mycoinsecticide from a local fungal isolate against M. persicae. According to the results of the screening experiments using 15 isolates (6 × Metarhizium, 5 × Beauveria, 2 × Isaria, 2 × Lecanicillium) at 1 × 10 7 conidia ml − 1 concentrations and the dose–response experiments at 1 × 10 5 –1 × 10 9 conidia ml − 1 concentrations against M. persicae nymphs, Beauveria bassiana (KTU-24) was identified as the most promising isolate. The strain KTU-24 is also had tolerance to ecological conditions such as temperature, and UV-B. KTU-24 with advantageous and superior properties was used to develop a test mycoinsecticide. Mass production of spores by KTU-24 was conducted out by liquid-state fermentation using liquid medium. Spores harvested from the sporulated biomass were used to develop an oilbased mycoinsecticide, and the product was designated as AFIDISIDAL-OD Bbas-TR61. The product had lethal effect on M. persicae nymphs at a concentration of 1 × 10 8 conidia ml − 1 in leaf-disc (82.5%) and pot (84.33%) experiments in a climate chamber. The oil-based mycoinsecticide developed in this study could be profitable when used in aphid-IPM prgrams by reducing crop loss and synthetic pesticides use.
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A Novel cry2Ab Gene from the Indigenous Isolate Bacillus thuringiensis subsp. kurstaki
( Sevim Ali ),( Emine Eryuzlu1 ),( Zihni Demirba ),( Smail Demir ) 한국미생물 · 생명공학회 2012 Journal of microbiology and biotechnology Vol.22 No.1
A novel cry2Ab gene was cloned and sequenced from the indigenous isolate of Bacillus thuringiensis subsp. kurstaki. This gene was designated as cry2Ab25 and its sequence revealed an open reading frame of 1,902 bp encoding a 633 aa protein with calculated molecular mass of 70 kDa and pI value of 8.98. The amino acid sequence of the Cry2Ab25 protein was compared with previously known Cry2Ab toxins, and the phylogenetic relationships among them were determined. The deduced amino acid sequence of the Cry2Ab25 protein showed 99% homology to the known Cry2Ab proteins, except for Cry2Ab10 and Cry2Ab12 with 97% homology, and a variation in one amino acid residue in comparison with all known Cry2Ab proteins. The cry2Ab25 gene was expressed in Escherichia coli BL21(DE3) cells. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) revealed that the Cry2Ab25 protein is about 70 kDa. The toxin expressed in BL21(DE3) exhibited high toxicity against Malacosoma neustria and Rhagoletis cerasi with 73% and 75% mortality after 5 days of treatment, respectively.
ScienceON
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