Optimal production and characterization of alkaline protease from newly isolated halotolerant Jeotgalicoccus sp. Issue 2 (April 2015)
- Record Type:
- Journal Article
- Title:
- Optimal production and characterization of alkaline protease from newly isolated halotolerant Jeotgalicoccus sp. Issue 2 (April 2015)
- Main Title:
- Optimal production and characterization of alkaline protease from newly isolated halotolerant Jeotgalicoccus sp
- Authors:
- Mokashe, Narendra
Chaudhari, Ambalal
Patil, Ulhas - Abstract:
- <abstract abstract-type="author" id="ab0005"> <title id="sect0005">Abstract</title> <sec> <p id="sp0040">A halotolerant strain UG was newly isolated from saline soil, produces an extracellular alkaline protease. The strain was identified as <italic>Jeotgalicoccus</italic> sp. on the basis of phylogenetic and phenotypic characteristics. The maximum protease yield (256.4±4.3 U/ml) was attained using optimized medium consists; peptone, K<sub>2</sub>HPO<sub>4</sub>, MgSO<sub>4</sub>·7H<sub>2</sub>O, CaCl<sub>2</sub> and NaCl; pH 10 at 37 °C within 40 h. The protease secretion was calcium ion dependent and enhanced by CaCl<sub>2</sub> supplementation in the production medium.</p> <p id="sp0045">A protease produced by <italic>Jeotgalicoccus</italic> sp. was most active at 48 °C and pH 10. The protease was purified by three step purification pattern which resulted in ~39 fold protease purification with a yield of 38%. The molecular weight of purified protease was estimated to be 51 kDa by SDS-PAGE. The protease was inhibited by EDTA, indicating that enzyme belongs to metalloprotease class. Protease showed better activity over a wide range of NaCl (0–1.5 M) and reasonable activity in presence of Ca<sup>2+</sup>, Mg<sup>2+</sup>, K<sup>+</sup>, Mn<sup>2+</sup>, Cd<sup>2+</sup> and Sn<sup>2+</sup>. Furthermore, the protease was active in the presence of H<sub>2</sub>O<sub>2</sub> and sodium perborate. Also, protease showed the substantial activity in the presence of rhamnolipid and<abstract abstract-type="author" id="ab0005"> <title id="sect0005">Abstract</title> <sec> <p id="sp0040">A halotolerant strain UG was newly isolated from saline soil, produces an extracellular alkaline protease. The strain was identified as <italic>Jeotgalicoccus</italic> sp. on the basis of phylogenetic and phenotypic characteristics. The maximum protease yield (256.4±4.3 U/ml) was attained using optimized medium consists; peptone, K<sub>2</sub>HPO<sub>4</sub>, MgSO<sub>4</sub>·7H<sub>2</sub>O, CaCl<sub>2</sub> and NaCl; pH 10 at 37 °C within 40 h. The protease secretion was calcium ion dependent and enhanced by CaCl<sub>2</sub> supplementation in the production medium.</p> <p id="sp0045">A protease produced by <italic>Jeotgalicoccus</italic> sp. was most active at 48 °C and pH 10. The protease was purified by three step purification pattern which resulted in ~39 fold protease purification with a yield of 38%. The molecular weight of purified protease was estimated to be 51 kDa by SDS-PAGE. The protease was inhibited by EDTA, indicating that enzyme belongs to metalloprotease class. Protease showed better activity over a wide range of NaCl (0–1.5 M) and reasonable activity in presence of Ca<sup>2+</sup>, Mg<sup>2+</sup>, K<sup>+</sup>, Mn<sup>2+</sup>, Cd<sup>2+</sup> and Sn<sup>2+</sup>. Furthermore, the protease was active in the presence of H<sub>2</sub>O<sub>2</sub> and sodium perborate. Also, protease showed the substantial activity in the presence of rhamnolipid and cyclodextrin. The protease from <italic>Jeotgalicoccus</italic> sp. was suggested as a better bio-additive agent for detergent industry.</p> </sec> </abstract> … (more)
- Is Part Of:
- Biocatalysis and agricultural biotechnology. Volume 4:Issue 2(2015)
- Journal:
- Biocatalysis and agricultural biotechnology
- Issue:
- Volume 4:Issue 2(2015)
- Issue Display:
- Volume 4, Issue 2 (2015)
- Year:
- 2015
- Volume:
- 4
- Issue:
- 2
- Issue Sort Value:
- 2015-0004-0002-0000
- Page Start:
- 235
- Page End:
- 243
- Publication Date:
- 2015-04
- Subjects:
- Agricultural biotechnology -- Periodicals
Enzymes -- Biotechnology -- Periodicals
660.6 - Journal URLs:
- http://rave.ohiolink.edu/ejournals/issn/18788181/ ↗
http://www.sciencedirect.com/science/journal/18788181 ↗
http://www.elsevier.com/journals ↗ - DOI:
- 10.1016/j.bcab.2015.01.003 ↗
- Languages:
- English
- ISSNs:
- 1878-8181
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 3657.xml