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• W2117436760 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 degrees 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 degrees C. Thermostability increased in the presence of Ca2+. The stability of the enzyme was maintained in 10% sucrose and in the absence of NaCl." @default.
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• W2117436760 date "2006-01-01" @default.
• W2117436760 modified "2023-10-17" @default.
• W2117436760 title "Purification and characterization of a thermostable, haloalkaliphilic extracellular serine protease from the extreme halophilic archaeon<i>Halogeometricum borinquense</i>strain TSS101" @default.
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• W2117436760 doi "https://doi.org/10.1155/2006/430763" @default.
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