Characterization of a Thermostable Esterase Activity from the Moderate Thermophile Bacillus licheniformis

概要

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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℃ and the half-life was 1 h at 64℃. Maximum activity was observed on pnitrophenyl caproate with little activity toward long-chain fatty acid esters. The enzyme had a K_M of 0.52 mM for pnitrophenyl caproate hydrolysis at pH 8 and 37℃. 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.
社団法人日本農芸化学会の論文
1999-11-23