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• W2092531639 abstract "Thermostable alkaline proteases from two haloalkaliphilic bacteria, Oceanobacillus iheyensis O.M.A(1)8 (EU680961) and Haloalkaliphilic bacterium O.M.E(1)2 (EU680960) were studied for enzymatic properties and amino acid sequences in comparative manner. The bacteria were isolated from salt enriched soil located in Okha, Coastal Gujarat, India. The unique aspect of the study was that alkaline protease from Haloalkaliphilic bacterium O.M.A(1)8 optimally catalyzed the reaction over a wide range of temperature, 50-90°C, with a half-life of 36 h at 90°C. The molecular weights of O.M.A(1)8 and O.M.E(1)2 were 35 kDa and 25 kDa, respectively. The enzyme secretion was over the broader range of pH 8-11, with an optimum at 11. The alkaline proteases from the two haloalkaliphilic strains isolated from the same site reflected quite different characteristics features. To the best of our knowledge, we have not come across with any such report on the thermal stability of alkaline proteases from haloalkaliphiles. Amino acid sequences for both enzymes were deduced from the nucleotide sequences of their corresponding genes followed by the analysis of physico-chemical properties of the enzymes." @default.
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• W2092531639 date "2011-07-01" @default.
• W2092531639 modified "2023-09-23" @default.
• W2092531639 title "Comparative analysis of enzymatic stability and amino acid sequences of thermostable alkaline proteases from two haloalkaliphilic bacteria isolated from Coastal region of Gujarat, India" @default.
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• W2092531639 doi "https://doi.org/10.1016/j.ijbiomac.2011.04.001" @default.
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