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Ministry points: Help
| Year | Points | List |
|---|---|---|
| Year 2024 | 5 | Journal not listed on ministry scored journal list 2024 |
| Year | Points | List |
|---|---|---|
| 2024 | 5 | Journal not listed on ministry scored journal list 2024 |
| 2023 | 5 | Not listed on the ministry scored journals list 2023 |
| 2022 | 5 | Not listed on the ministry scored journals list (2019-2022) |
| 2021 | 5 | Not listed on the ministry scored journals list (2019-2022) |
| 2020 | 5 | Not listed on the ministry scored journals list (2019-2022) |
| 2019 | 5 | Not listed on the ministry scored journals list (2019-2022) |
| 2012 | 15 | A |
| 2011 | 15 | A |
| 2010 | 13 | A |
Points CiteScore:
| Year | Points |
|---|---|
| Year 2022 | 0 |
| Year | Points |
|---|---|
| 2022 | 0 |
| 2021 | 0.9 |
| 2014 | 2 |
| 2013 | 1.7 |
| 2012 | 1.3 |
| 2011 | 0.9 |
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Papers published in journal
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total: 3
Catalog Journals
Year 2013
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Extracellular proteolytic activity of Deinococcus geothermalis
PublicationProduction of extracellular protease by extremophilic bacteria Deinococcus geothermalis cultivated in liquid media containing 0.1% (w/v) of peptone K, 0.1% yeast extract and 0.2% marine salt reached a maximum in 14 h of the cell growth at 45°C and pH 8.0. The enzyme was purified by a two-step procedure using fractionation by a graded ammonium sulphate precipitation technique and gel filtration on Sephadex G-100 column. Protease...
Year 2012
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Expression of Deinococcus geothermalis Trehalose Synthase Gene in Escherichia coli and Its Enzymatic Properties
PublicationA novel trehalose synthase gene from Deinococcus geothermalis (DSMZ 11300) containing 1,692 bp reading-frame encoding 564 amino acids was amplified using PCR. The gene was ligated into pET30Ek/LIC vector and expressed after isopropyl alfa-D-thiogalactopyranoside induction in Escherichia coli BL21(DE3)pLysS. The recombinant trehalose synthase (DgeoTreS) containing a His6 tag at the C-terminus was purified by metal affinity chromatography...
Year 2010
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Some applications of thermophiles and their enzymes for protein processing
PublicationPrzedstawiono charakterystykę, właściwości oraz możliwości zastosowań enzymów proteolitycznych wytwarzanych przez termofile. Zaletą tych biokatalizatorów jest między innymi duża odporność na działanie rozpuszczalników organicznych, detergentów i innych czynników denaturujących białka oraz mała wrażliwość na zmiany pH. Dokonano też przeglądu czynników powodujących dużą stabilność proteaz z termofili.
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