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

研究成果: Article査読

42 被引用数 (Scopus)

抄録

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.

本文言語English
ページ(範囲)395-402
ページ数8
ジャーナルMarine Biotechnology
12
4
DOI
出版ステータスPublished - 2010

ASJC Scopus subject areas

  • Biotechnology
  • Aquatic Science

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