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Isolation and characterization of a GDSL esterase from the metagenome of a marine sponge-associated bacteria.

Authors
  • Okamura, Yoshiko
  • Kimura, Tomonori
  • Yokouchi, Hiroko
  • Meneses-Osorio, Macarena
  • Katoh, Masaya
  • Matsunaga, Tadashi
  • Takeyama, Haruko
Type
Published Article
Journal
Marine biotechnology (New York, N.Y.)
Publication Date
Aug 01, 2010
Volume
12
Issue
4
Pages
395–402
Identifiers
DOI: 10.1007/s10126-009-9226-x
PMID: 19789923
Source
Medline
License
Unknown

Abstract

Using a metagenome library constructed from a bacterial associated with a marine sponge Hyrtios erecta, we identified a novel esterase that belongs to the SGNH hydrolase superfamily of esterases. The substrate specificity of EstHE1 was determined using p-nitrophenyl (pNP) ester (C2: acetate, C4: butylate, C6: caproate, C12: laurate, C16: palmitate). EstHE1 exhibited activity against C2 (5.6 U/mg), C4 (5.1 U/mg), and C6 (2.8 U/mg) substrates. The optimal temperature for EstHE1 esterase activity of the pNP acetate substrate was 40 degrees C, and EstHE1 retained 60% of its enzymatic activity in the 30-50 degrees C range. This esterase showed moderate thermostability, retaining 58% of its activity even after preincubation for 12 h at 40 degrees C. EstHE1 also maintained activity in high concentrations of NaCl, indicating that this esterase is salt-tolerant. Thus, EstHE1 has the thermal stability and salt tolerance necessary for use as an industrial enzyme.

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