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DC Field | Value | Language |
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dc.contributor.author | Vidyasagar M | |
dc.contributor.author | Prakash S | |
dc.contributor.author | Litchfield C | |
dc.contributor.author | Sreeramulu K. | |
dc.date.accessioned | 2020-06-12T15:06:07Z | - |
dc.date.available | 2020-06-12T15:06:07Z | - |
dc.date.issued | 2006 | |
dc.identifier.citation | Archaea , Vol. 2 , 1 , p. 51 - 57 | en_US |
dc.identifier.uri | 10.1155/2006/430763 | |
dc.identifier.uri | http://gukir.inflibnet.ac.in:8080/jspui/handle/123456789/5068 | - |
dc.description.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. | en_US |
dc.publisher | Heron Publishing | |
dc.subject | Calcium chloride | |
dc.subject | Cetyltrimethylammonium bromide | |
dc.subject | Halophilic serine protease | |
dc.subject | Metal ions | |
dc.subject | Osmolytes | |
dc.subject | Protease inhibitors | |
dc.title | Purification and characterization of a thermostable, haloalkaliphilic extracellular serine protease from the extreme halophilic archaeon Halogeometricum borinquense strain TSS101 | en_US |
dc.type | Article | |
Appears in Collections: | 1. Journal Articles |
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