Kamenev D.G.,Institute of Biology and Soil science FEB RES |
Shkryl Y.N.,Institute of Biology and Soil science FEB RES |
Veremeichik G.N.,Institute of Biology and Soil science FEB RES |
Golotin V.A.,RAS Pacific Institute of Bioorganic Chemistry |
And 5 more authors.
Journal of Nanoscience and Nanotechnology | Year: 2015
The cDNA fragment encoding the catalytic domain of the new silicatein-like cathepsin enzyme LoCath was expressed in a strain Top10 of Escherichia coli, extracted and purified via nickel-affinity chromatography. Recombinant enzyme performed silica-polymerizing activity when mixed with water-soluble silica precursor-tetrakis-(2-hydroxyethyl)-orthosilicate. Scanning electron microscopy revealed hexagonal, octahedral and β-tridimit crystals. Energy dispersion fluorescence X-ray spectrometry analysis showed that all these crystals consist of pure silicon oxide. It is the first report about the ability of marine sponge's cathepsin to polymerize silicon, as well as about the structure and composition of the silicon oxide crystal formed by recombinant cathepsin. Further study of the catalytic activity of silicatein and cathepsin will help to understand the biosilification processes in vivo, and will create basis for biotechnological use of recombinant proteins for silicon polymerization. Copyright © 2015 American Scientific Publishers All rights reserved.