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• W2048472811 endingPage "1870" @default.
• W2048472811 startingPage "1865" @default.
• W2048472811 abstract "A new esterase activity from Bacillus licheniformis was characterized from an Escherichia coli recombinant strain. The protein was a single polypeptide chain with a molecular mass of 81 kDa. The optimum pH for esterase activity was 8-8.5 and it was stable in the range 7-8.5. The optimum temperature for activity was 45 degrees C and the half-life was 1 h at 64 degrees C. Maximum activity was observed on p-nitrophenyl caproate with little activity toward long-chain fatty acid esters. The enzyme had a KM of 0.52 mM for p-nitrophenyl caproate hydrolysis at pH 8 and 37 degrees C. The enzyme activity was not affected by either metal ions or sulfydryl reagents. Surprisingly, the enzyme was only slightly inhibited by PMSF. These characteristics classified the new enzyme as a thermostable esterase that shared similarities with lipases. The esterase might be useful for biotechnological applications such as ester synthesis." @default.
• W2048472811 created "2016-06-24" @default.
• W2048472811 creator A5037003390 @default.
• W2048472811 creator A5055435218 @default.
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• W2048472811 date "1999-01-01" @default.
• W2048472811 modified "2023-10-10" @default.
• W2048472811 title "Characterization of a Thermostable Esterase Activity from the Moderate Thermophile Bacillus licheniformis" @default.
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• W2048472811 doi "https://doi.org/10.1271/bbb.63.1865" @default.
• W2048472811 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/10635551" @default.
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