Please use this identifier to cite or link to this item:
http://nopr.niscpr.res.in/handle/123456789/23802Full metadata record
| DC Field | Value | Language |
|---|---|---|
| dc.contributor.author | Mane, R R | - |
| dc.contributor.author | Bapat, M M | - |
| dc.date.accessioned | 2013-11-19T08:51:36Z | - |
| dc.date.available | 2013-11-19T08:51:36Z | - |
| dc.date.issued | 2001-06 | - |
| dc.identifier.issn | 0975-1009 (Online); 0019-5189 (Print) | - |
| dc.identifier.uri | http://hdl.handle.net/123456789/23802 | - |
| dc.description | 578-583 | en_US |
| dc.description.abstract | An alkaline protease was isolated from culture filtrate of B. subtilis NCIM 2713 by ammonium sulphate precipitation and was purified by gel filtration. With casein as a substrate, the proteolytic activity of the purified protease was found to be optimal at pH 8.0 and temperature 70° C. The purified protease had molecular weight 20 kDa. lsoelectric point 5.2 and km 2.5 mg ml-1. The enzyme was stable over the pH range 6.5 - 9.0 at 37° C for 3 hr. During chromatographic separation this protease was found to be susceptible to autolytic degradation in the absence of Ca2+ , Ca2+ was not only required for the enzyme activity but also for the stability of the enzyme above 50° C. About 62 % activity was retained after 60 min at pH 8.0 and 55°C. DFP and PMSF completely inhibited the activity of this enzyme, while in the presence of EDTA only 33 % activity remained. However, it was not affected either by su101ydryl reagent, or by divalent metal cations, except SDS and Hg2+ . The results indicated that this is a serine protease. | en_US |
| dc.language.iso | en_US | en_US |
| dc.publisher | NISCAIR-CSIR, India | en_US |
| dc.rights |  CC Attribution-Noncommercial-No Derivative Works 2.5 India | en_US |
| dc.source | IJEB Vol.39(06) [June 2001] | en_US |
| dc.title | A study of extracellular alkaline protease from Bacillus subtilis NCIM 2713 | en_US |
| dc.type | Article | en_US |
| Appears in Collections: | IJEB Vol.39(06) [June 2001] | |
Files in This Item:
| File | Description | Size | Format | |
|---|---|---|---|---|
| IJEB 39(6) 578-583.pdf | 1.2 MB | Adobe PDF | View/Open |
Items in NOPR are protected by copyright, with all rights reserved, unless otherwise indicated.