Identification of Novel Esterase from Metagenomic Library of Yangtze River

  • Wu, Chao (Hefei National Laboratory for Physical Sciences at Microscale and School of Life Sciences, University of Science and Technology of China) ;
  • Sun, Baolin (Hefei National Laboratory for Physical Sciences at Microscale and School of Life Sciences, University of Science and Technology of China)
  • Published : 2009.02.28

Abstract

A metagenomic library of surface-water microbes from the Yangtze River in China was constructed, and a novel esterase, designated as EstY, was isolated and characterized. EstY had 423 amino acids with an estimated molecular mass of 44 kDa and pI of 7.28. It hydrolyzed various p-nitrophenyl esters(acetate, butyrate, caprate, caprylate, laurate, myristate, and palmitate) and its best substrate was p-nitrophenyl caprate(C8). The optimum pH for EstY activity was 9.0 and the optimum temperature was $50^{\circ}C$. Metal ions, such as $Mn^{2+},\;Co^{2+},\;Hg^{2+},\;Zn^{2+},\;and\;Fe^{3+}$, strongly inhibited the activity of EstY, whereas $Mg^{2+}$ was required for maximal activity. Activity remained in the presence of 10% alcohol, acetone, isopropanol, and dimethyl sulfoxide, respectively. An analysis of the amino acid sequence deduced from estY revealed that it had 7 closely related lipolytic enzymes. Moreover, a sequence analysis showed that EstY, like its 7 relatives, did not belong to any known lipolytic enzyme family.

Keywords

References

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