An intracellular halotolerant lipase was isolated from the moderately halophile, Thalassobacillus sp. SCULCB HNA-5. The enzyme was purified by chromatography using Q-Sepharose FF and POROS-XS columns. The molecular mass of the enzyme was estimated to be 60.8kDa by SDS-PAGE. The optimal temperature for activity was 50°C at pH 8.0. It was high active over broad temperature (25–65°C), pH (6.0–8.5), and NaCl concentration (0–4.5M) ranges, indicating its thermostable, alkali-stable, and halotolerant nature. The enzyme activity was markedly enhanced by Li+, but inhibited by Tween-80 and Cu2+. Moreover the lipase kept high activity in the organic solution such as DMSO, glycerol and methyl alcohol, implying that the enzyme was able to be used in organic synthesis.
Moderate halophile, Lipase, Thermostable, Halotolerant, Intracellular
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