Please use this identifier to cite or link to this item: http://gukir.inflibnet.ac.in:8080/jspui/handle/123456789/5068
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dc.contributor.authorVidyasagar M
dc.contributor.authorPrakash S
dc.contributor.authorLitchfield C
dc.contributor.authorSreeramulu K.
dc.date.accessioned2020-06-12T15:06:07Z-
dc.date.available2020-06-12T15:06:07Z-
dc.date.issued2006
dc.identifier.citationArchaea , Vol. 2 , 1 , p. 51 - 57en_US
dc.identifier.uri10.1155/2006/430763
dc.identifier.urihttp://gukir.inflibnet.ac.in:8080/jspui/handle/123456789/5068-
dc.description.abstractA 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.publisherHeron Publishing
dc.subjectCalcium chloride
dc.subjectCetyltrimethylammonium bromide
dc.subjectHalophilic serine protease
dc.subjectMetal ions
dc.subjectOsmolytes
dc.subjectProtease inhibitors
dc.titlePurification and characterization of a thermostable, haloalkaliphilic extracellular serine protease from the extreme halophilic archaeon Halogeometricum borinquense strain TSS101en_US
dc.typeArticle
Appears in Collections:1. Journal Articles

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