Research from Bar-Ilan University Reveals New Findings on Physical Chemistry and Chemical Physics (Trapping RNase A on MCM41 pores: effects on structure stability, product inhibition and overall enzymatic activity)
By a News Reporter-Staff News Editor at Life Science Weekly -- Investigators publish new report on Physical Chemistry and Chemical Physics. According to news reporting out of Ramat Gan, Israel, by NewsRx editors, research stated, "Catalytic activity of enzymes can be drastically modified by immobilization on surfaces of different materials. It is particularly effective when the dimensions of the biomolecules and adsorption sites on the material surfaces are commensurate."
Our news journalists obtained a quote from the research from Bar-Ilan University, "This can be utilized to hinder the biological activity of degradation enzymes and switch off undesired biological processes. Ribonucleases are particularly attractive targets for complete sequestration being efficient at disintegrating viable RNA molecules. Here we show that efficient quenching of ribonuclease A activity can be achieved by immobilization on the surface of MCM41 porous silica. Electron microscopy, isothermal titration calorimetry, differential scanning calorimetry and adsorption isotherm measurements of ribonuclease A on the MCM41 surface are used to demonstrate that the enzyme adsorbs on the external surface of the porous silica through electrostatic interactions that overcome the unfavorable entropy change as the protein gets trapped on the surface, and that immobilization shifts up its denaturation temperature by 20-25 °C."
According to the news editors, the research concluded: "Real-time kinetic measurements, using single injection titration calorimetry, demonstrate that enzymatic activity towards hydrolysis of cyclic nucleotides is lowered by nearly two orders of magnitude on MCM41 and that active inhibition by the formed product is much less effective on the surface than in solution."
For more information on this research see: Trapping RNase A on MCM41 pores: effects on structure stability, product inhibition and overall enzymatic activity. Physical Chemistry Chemical Physics, 2014;16(19):9031-8. (Royal Society of Chemistry - www.rsc.org/; Physical Chemistry Chemical Physics - pubs.rsc.org/en/journals/journalissues/cp)
Our news journalists report that additional information may be obtained by contacting I. Matlahov, Dept. of Chemistry, Bar Ilan University, Ramat Gan 52900, Israel. Additional authors for this research include Y. Geiger and G. Goobes (see also Physical Chemistry and Chemical Physics).
Keywords for this news article include: Asia, Israel, Ramat Gan, Physical Chemistry and Chemical Physics.
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