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| DC Field | Value | Language |
|---|---|---|
| dc.contributor.author | Papamichael, E. M. | en |
| dc.contributor.author | Theodorou, L. G. | en |
| dc.contributor.author | Perisynakis, A. | en |
| dc.contributor.author | Drainas, C. | en |
| dc.date.accessioned | 2015-11-24T16:45:43Z | - |
| dc.date.available | 2015-11-24T16:45:43Z | - |
| dc.identifier.issn | 0959-3330 | - |
| dc.identifier.uri | https://olympias.lib.uoi.gr/jspui/handle/123456789/8973 | - |
| dc.rights | Default Licence | - |
| dc.subject | halo-alkaliphiles | en |
| dc.subject | purification | en |
| dc.subject | cysteine proteases | en |
| dc.subject | enzyme kinetics | en |
| dc.subject | polar organic solvents | en |
| dc.subject | cysteine proteinases | en |
| dc.subject | peptide-synthesis | en |
| dc.subject | papain | en |
| dc.subject | kinetics | en |
| dc.subject | mechanism | en |
| dc.subject | catalysis | en |
| dc.subject | insight | en |
| dc.title | Purification and characterization of a novel extracellular protease from a halo-alkaliphilic Bacillus sp 17N-1, active in polar organic solvents | en |
| heal.type | journalArticle | - |
| heal.type.en | Journal article | en |
| heal.type.el | Άρθρο Περιοδικού | el |
| heal.identifier.primary | Doi 10.1080/09593331003664136 | - |
| heal.identifier.secondary | <Go to ISI>://000278856500002 | - |
| heal.identifier.secondary | http://www.tandfonline.com/doi/pdf/10.1080/09593331003664136 | - |
| heal.language | en | - |
| heal.access | campus | - |
| heal.recordProvider | Πανεπιστήμιο Ιωαννίνων. Σχολή Θετικών Επιστημών. Τμήμα Χημείας | el |
| heal.publicationDate | 2010 | - |
| heal.abstract | A novel enzyme of molecular mass about 29 kDa was purified from the strain halo-alkaliphilic Bacillus sp. 17N-1 and designated protease-B-17N-1. This enzyme is likely to be a cysteine protease; it was found active in media containing EDTAK2 and dithiothreitol, it maintained considerable activity at temperatures 14 degrees C to 33 degrees C and pH 6.50 to 8.50 with optimum kcat/Km and/or kcat values at pH 7.00 and 25 degrees C. The activity of protease-B-17N-1 was strongly affected by the specific irreversible inhibitor of cysteine proteases E-64, while it remained unaffected by the 3,4-dichloro-isocoumarine, an irreversible inhibitor specific for serine proteases. Protease-B-17N-1 retained full activity at 25 degrees C after 30 min incubation at 8 degrees C or at 33 degrees C; moreover, it was found to be stable and active in the polar organic solvents DMSO and acetonitrile. The enzyme hydrolyzed the substrate Cbz-FR-pNA via Michaelis-Menten kinetics, while it showed insignificant activity for the substrate Suc-AAA-pNA. Valuable pKas, rate constants, activation energies and other important features were estimated from the profiles of parameters kcat/Km, kcat and Km, versus pH, temperature, and [NaCl]. In addition, interesting results were obtained from the effect of different metallic ions and polar organic solvents on the Michaelis-Menten parameters of protease-B-17N-1, showing that it performs catalysis via a (Cys)-S-/(His)-Im+H ion-pair, as well as its industrial and biotechnological potential, respectively. | en |
| heal.publisher | Taylor & Francis | en |
| heal.journalName | Environmental Technology | en |
| heal.journalType | peer reviewed | - |
| heal.fullTextAvailability | TRUE | - |
| Appears in Collections: | Άρθρα σε επιστημονικά περιοδικά ( Ανοικτά). ΧΗΜ | |
Files in This Item:
| File | Description | Size | Format | |
|---|---|---|---|---|
| Papamichael-2010-Purification and cha.pdf | 1.33 MB | Adobe PDF | View/Open Request a copy |
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