Structure and enzymatic activity of laser immobilized ribonuclease A
| Autor: | Angela Popescu, G. Duta Cornescu, Alexandra Simon-Gruita, Nicoleta Constantin, C. Popescu, Daniela Maria Pojoga, Eniko Gyorgy, I. Iordache, Marilena Motoc |
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| Rok vydání: | 2014 |
| Předmět: |
Maple
biology Immobilized enzyme RNase P Chemistry Scanning electron microscope Mechanical Engineering Analytical chemistry engineering.material Laser law.invention Mechanics of Materials law biology.protein engineering Molecule General Materials Science Ribonuclease Fourier transform infrared spectroscopy Nuclear chemistry |
| Zdroj: | Journal of Materials Science. 49:4371-4378 |
| ISSN: | 1573-4803 0022-2461 |
| DOI: | 10.1007/s10853-014-8136-0 |
| Popis: | Ribonuclease A (RNase A) enzyme was immobilized on solid holders by matrix-assisted pulsed laser evaporation (MAPLE) technique. The experiments were performed inside a stainless steel irradiation chamber. A UV KrF* (λ = 248 nm, τFWHM ≅ 25 ns, ν = 10 Hz) excimer laser source was used for irradiations. Surface morphology, molecular structure, and enzymatic activity of laser transferred RNase A samples were investigated as a function of RNase A concentration in the frozen composite MAPLE targets. Surface morphology and thickness of the immobilized enzyme were investigated by atomic force microscopy, scanning electron microscopy, and surface profilometry. The molecular structure of the laser transferred RNase A was determined by Fourier transform infrared spectroscopy. The enzymatic activity of RNase A after immobilization was tested through ribonucleic acid removal from deoxyribonucleic acid (DNA) extract solutions isolated from plant and animal tissues. A molecular method based on polymerase chain reaction was used to investigate the functional properties of DNA extracts treated with laser immobilized RNase A. |
| Databáze: | OpenAIRE |
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