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• W2080650341 abstract "The lipase from the Antarctic psychrophilic bacterium Psychrobacter immobilis B10 shows a very limited thermal stability when compared to the lipase from a mesophilic strain of Pseudomonas aeruginosa. The thermal dependence of its activity is shifted by at least 30 °C towards low temperatures and its activation energy is reduced by a factor of 2. The three-dimensional model of the P. immobilis lipase reveals several features typical of cold-adapted enzymes: a very low proportion of arginine residues as compared to lysines, a low content in proline residues, a small hydrophobic core, a very small number of salt bridges and of aromatic-aromatic interactions. All these properties should confer on the enzyme a more flexible structure, in accord with its low activation energy and its low thermal stability." @default.
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• W2080650341 date "1997-06-01" @default.
• W2080650341 modified "2023-09-27" @default.
• W2080650341 title "Molecular adaptation to cold of an Antarctic bacterial lipase" @default.
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• W2080650341 doi "https://doi.org/10.1016/s1381-1177(96)00041-0" @default.
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