Flocculent activity of a recombinant protein from Moringa oleifera Lam. seeds

被引:0
|
作者
M. Broin
C. Santaella
S. Cuine
K. Kokou
G. Peltier
T. Joët
机构
[1] CEA/Cadarache,
[2] Direction des Sciences du Vivant,undefined
[3] Département d'Ecophysiologie Végétale et Microbiologie,undefined
[4] Laboratoire d'Ecophysiologie de la Photosynthèse,undefined
[5] UMR 163 CNRS CEA,undefined
[6] Univ-Méditerranée CEA 1000,undefined
[7] 13108 Saint-Paul-lez-Durance,undefined
[8] France,undefined
[9] CEA/Cadarache,undefined
[10] Direction des Sciences du Vivant,undefined
[11] Département d'Ecophysiologie Végétale et Microbiologie,undefined
[12] Laboratoire d'Ecologie Microbienne et de la Rhizosphère,undefined
[13] UMR 163 CNRS CEA,undefined
[14] Univ-Méditerranée,undefined
[15] 13108 Saint-Paul-lez-Durance,undefined
[16] France,undefined
[17] Laboratoire de Botanique et Ecologie Végétale,undefined
[18] Faculté des Sciences,undefined
[19] Université de Lomé,undefined
[20] BP1515,undefined
[21] Lomé,undefined
[22] Togo,undefined
[23] Present address: Saint George's Hospital Medical School,undefined
[24] Department of Infectious Diseases,undefined
[25] Cranmer Terrace,undefined
[26] London SW17 ORE,undefined
[27] UK,undefined
来源
关键词
Microscopy; Escherichia Coli; Clay; Purification; Montmorillonite;
D O I
暂无
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学科分类号
摘要
Seeds of the tropical tree Moringa oleifera contain small storage proteins able to flocculate particles in suspension in water. The cDNA encoding one of these flocculent proteins, MO2.1, was cloned and the recombinant protein was expressed in Escherichia coli. The flocculent activity of the purified recombinant MO2.1 was assayed on clays and bacteria using light and confocal microscopy and GFP-overexpressing bacteria. We show that MO2.1 is able to aggregate montmorillonite clay particles as well as gram-positive and gram-negative bacteria. We discuss the use of recombinant proteins to study flocculating properties and improve water purification processes.
引用
收藏
页码:114 / 119
页数:5
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