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

Yoshiko Okamura, Tomonori Kimura, Hiroko Yokouchi, Macarena Meneses-Osorio, Masaya Katoh, Tadashi Matsunaga, Haruko Takeyama

Research output: Contribution to journalArticle

39 Citations (Scopus)


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°C, and EstHE1 retained 60% of its enzymatic activity in the 30-50°C range. This esterase showed moderate thermostability, retaining 58% of its activity even after preincubation for 12 h at 40°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.

Original languageEnglish
Pages (from-to)395-402
Number of pages8
JournalMarine Biotechnology
Issue number4
Publication statusPublished - 2010 Jan 1



  • Esterase
  • GDSL family
  • Halotolerance
  • Marine sponge
  • Metagenome
  • Thermostability

ASJC Scopus subject areas

  • Biotechnology
  • Aquatic Science

Cite this