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Biosynthesis of Gold and Selenium Nanoparticles by Purified Protein from Acinetobacter sp. SW 30

Wadhwani, Sweety A., Shedbalkar, Utkarsha U., Singh, Richa, Chopade, Balu A.
Enzyme and Microbial Technology 2017
1-propanol, Acinetobacter, anion exchange chromatography, biosynthesis, gel chromatography, lignin peroxidase, microorganisms, molecular weight, nanogold, nanoparticles, pH, polyacrylamide gel electrophoresis, selenium, sodium, temperature, thiosulfates, zinc sulfate
Synthesis of nanoparticles is an enzymatic reduction process in microorganisms. In the present study, a protein, lignin peroxidase has been purified by DEAE-Cellulose anion exchange chromatography and Biogel P-150 gel filtration chromatography from the cell suspension of Acinetobacter sp. SW30 responsible for the synthesis of gold nanoparticles (AuNP) and selenium nanoparticles (SeNP). The purified fraction has a specific activity of 29.4U/mg/min with 959 fold purification. Native and SDS PAGE confirmed that purified lignin peroxidase is monomeric enzyme with 97.4KDa molecular weight. The enzyme synthesized spherical crystalline AuNP (10±2nm) and amorphous SeNP (100±10nm). It has maximum activity at pH 2 and temperature 40°C, with 1.0mMKm value, when n-propanol was used as a substrate. Activity was completely inhibited by sodium thiosulphate and zinc sulphate. This is the first report on association of lignin peroxidase in the synthesis of AuNP and SeNP from Acinetobacter sp. SW30.