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http://nopr.niscpr.res.in/handle/123456789/23802| Title: | A study of extracellular alkaline protease from Bacillus subtilis NCIM 2713 |
| Authors: | Mane, R R Bapat, M M |
| Issue Date: | Jun-2001 |
| Publisher: | NISCAIR-CSIR, India |
| 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. |
| Page(s): | 578-583 |
| ISSN: | 0975-1009 (Online); 0019-5189 (Print) |
| 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 |
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