Biosynthesis of selenoproteins by Saccharomyces cerevisiae and characterization of its antioxidant activities
| Autor: | Liyong Jiao, Shuhong Ye, Fengjun Shen, Fei Wang, Zhichao Xu |
|---|---|
| Rok vydání: | 2020 |
| Předmět: |
Antioxidant
Chemical Phenomena DPPH medicine.medical_treatment chemistry.chemical_element 02 engineering and technology Saccharomyces cerevisiae Biochemistry Saccharomyces Antioxidants 03 medical and health sciences chemistry.chemical_compound Selenium Structural Biology medicine Selenoproteins Molecular Biology 030304 developmental biology Gel electrophoresis chemistry.chemical_classification 0303 health sciences integumentary system biology Spectrum Analysis General Medicine Free Radical Scavengers 021001 nanoscience & nanotechnology biology.organism_classification Yeast Molecular Weight chemistry Protein Biosynthesis Fermentation Selenoprotein 0210 nano-technology |
| Zdroj: | International journal of biological macromolecules. 164 |
| ISSN: | 1879-0003 |
| Popis: | The study investigated biosynthesis of selenoproteins by Saccharomyces. cerevisiae using inorganic selenium. Selenium supplement via two stages was carried out during fermentation and the physicochemical characteristics of selenoproteins and its antioxidant activities were examined through in vitro assessment procedures. After fermentation, dry cells weight (7.47 g/L) and selenium content (3079.60 μg/kg) in the yeast were achieved when fermentation time points at the 6th hour and the 9th hour were chosen to supplement 30% and 70% of 30 μg/mL Na2SeO3 respectively. A maximal yield of selenium content in selenoproteins reached 1013.07 μg/g under optimized culture conditions and was 133-fold higher than the control. One new band with molecular weight of 26.76 KDa appeared in conjugated selenoproteins of sodium dodecyl sulphate-polyacrylamide gel electrophoresis. Surface structure of selenoproteins and the control was different by Scanning electron microscopy images. Infrared spectrometry analysis demonstrated that groups of H Se, Se O and C-Se-O involved in selenoproteins were important pieces of evidence showing presence of Se embedded in the protein molecule. Selenoproteins showed strong antioxidant activities on DPPH·, OH and ·O2−, which was much higher than the control proteins. Therefore, the study provided an efficient selenium-enriched culture method of inorganic selenite to organic selenium and basis for selenoproteins applications. |
| Databáze: | OpenAIRE |
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