Search
Abstract
Production 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 from D. geothermalis with a molecular mass of 24 kDa was active at 60°C and pH 9.0. The enzyme solution was stable for 1 h at 60°C and displayed about 60% of the initial activity after 1 h incubation at pH values 5.0 and 11. The phenylmethanesulfonyl fluoride (PMSF) at 1 mM concentration decreased proteolytic activity up to 27.4% of the initial value and it suggests that the enzyme is a serine protease. The activity was stimulated by Ca2+, Na+, Mg2+ and strongly inhibited by Hg2+, Cu2+, Zn2+ and Fe3+. Nonionic detergents like Triton X-100 and Tween 80 did not affect catalytic properties. It suggested that the enzyme produced by D. geothermalis could be used as a component of detergents.
Authors (3)
Cite as
Full text
full text is not available in portal
Keywords
Details
- Category:
- Articles
- Type:
- artykuły w czasopismach recenzowanych i innych wydawnictwach ciągłych
- Published in:
-
AFRICAN JOURNAL OF BIOTECHNOLOGY
no. 12,
pages 4020 - 4027,
ISSN: 1684-5315 - Language:
- English
- Publication year:
- 2013
- Bibliographic description:
- Pietrow-Tobiszewska O., Panek A., Synowiecki J.: Extracellular proteolytic activity of Deinococcus geothermalis// AFRICAN JOURNAL OF BIOTECHNOLOGY. -Vol. 12., nr. 25 (2013), s.4020-4027
- Verified by:
- Gdańsk University of Technology
seen 120 times
Recommended for you
Expression of Deinococcus geothermalis Trehalose Synthase Gene in Escherichia coli and Its Enzymatic Properties
- P. Filipkowski,
- A. Panek,
- A. Felczykowska
- + 2 authors