Bt蛋白在矿物表面吸附的光谱研究
Studies on secondary structures of the toxin of Bacillus thuringiensis subsp. kurstaki adsorbed onto minerals by spectral methods
本文利用荧光光谱,圆二色光谱 (CD)和红外光谱 (IR) 技术研究了Bt蛋白在与矿物吸附-解吸过程中结构变化。结果表明,在282 nm 激发光的作用下Bt蛋白有色氨酸的荧光峰 (338 nm),吸附在高岭石和蒙脱石表面的蛋白解吸后荧光峰红移了5 – 9.5 nm,而吸附在针铁矿和二氧化硅表面的蛋白解吸后荧光峰位移不明显。Bt蛋白在供试矿物表面的吸附解吸过程导致其α-螺旋含量下降,β-折叠含量则增加了4.5-17.2%,且在一定程度上增加了蛋白的有序结构。红外光谱结果表明Bt蛋白与矿物可能形成表面键合作用,且矿物吸附态蛋白的二级结构变化不明显。
he persistence of the insecticidal protein of Bacillus thuringiensis (Bt) may constitute a hazard to the soil ecosystem, however, studies on secondary structures of the Bt toxin adsorbed onto soil minerals are limited. The secondary structures of the toxin, in Na2HPO4-NaH2PO4 buffer (pH 7.0) or adsorbed onto montmorillonite, kaolinite, goethite and silicon dioxide, were carried out by fluorescence spectroscopy, circular dichroism (CD) spectroscopy and infrared spectroscopy (IR). The maximum emission (λem) of the Bt toxin was at 338 nm by the excitation at 282 nm. Theλem of the toxin desorbed from kaolinite and montmorillonite was red shifted 5 and 9.5 nm, respectively, and that of the toxin desorbed from goethite and silicon dioxide was not obviously shifted. The α-helix content of the toxin was reduced while the β-sheet fraction was increased 4.5-17.2% among the toxin adsorption-desorption with minerals, and the ordered structure (α-helix + β-sheet) of the toxin was increased in a certain extent. IR spectroscopy indicated that the conformational of the adsorbed Bt toxin onto minerals were not obviously changed.
胡红青、陈守文、黄丽、付庆灵、邓雅丽
环境科学理论生物科学研究方法、生物科学研究技术环境生物学
Bt蛋白二级结构矿物荧光光谱圆二色光谱红外光谱
Bacillus thuringiensisCDFluorescence spectroscopyToxinIRMineralsSecondary structure
胡红青,陈守文,黄丽,付庆灵,邓雅丽.Bt蛋白在矿物表面吸附的光谱研究[EB/OL].(2007-08-29)[2025-08-06].http://www.paper.edu.cn/releasepaper/content/200708-432.点此复制
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