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Title: | Purification and characterization of a thermostable, haloalkaliphilic extracellular serine protease from the extreme halophilic archaeon Halogeometricum borinquense strain TSS101 |
Authors: | Vidyasagar M Prakash S Litchfield C Sreeramulu K. |
Keywords: | Calcium chloride Cetyltrimethylammonium bromide Halophilic serine protease Metal ions Osmolytes Protease inhibitors |
Issue Date: | 2006 |
Publisher: | Heron Publishing |
Citation: | Archaea , Vol. 2 , 1 , p. 51 - 57 |
Abstract: | A novel haloalkaliphilic, thermostable serine protease was purified from the extreme halophilic archaeon, Halogeometricum borinquense strain TSS101. The protease was isolated from a stationary phase culture, purified 116-fold with 18% yield and characterized biochemically. The molecular mass of the purified enzyme was estimated to be 86 kDa. The enzyme showed the highest activity at 60°C and pH 10.0 in 20% NaCl. The enzyme had high activity over the pH range from 6.0 to 10.0. Enzymatic activity was strongly inhibited by 1 mM phenyl methylsulfonyl fluoride, but activity was increased 59% by 0.1% cetyltrimethylammonium bromide. The enzyme exhibited relatively high thermal stability, retaining 80% of its activity after 1 h at 90°C. Thermostability increased in the presence of Ca2+. The stability of the enzyme was maintained in 10% sucrose and in the absence of NaCl. © 2006 Heron Publishing. |
URI: | 10.1155/2006/430763 http://gukir.inflibnet.ac.in:8080/jspui/handle/123456789/5068 |
Appears in Collections: | 1. Journal Articles |
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