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A new esterase EstD2 isolated from plant rhizosphere soil metagenome

Lee, Myung ; Hong, Kyung ; Malhotra, Shweta ; Park, Ji-Hye ; Hwang, Eul ; Choi, Hong ; Kim, Young ; Tao, Weixin ; Lee, Seon-Woo

Applied Microbiology and Biotechnology, 2010, Vol.88(5), pp.1125-1134 [Peer Reviewed Journal]

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  • Title:
    A new esterase EstD2 isolated from plant rhizosphere soil metagenome
  • Author: Lee, Myung ; Hong, Kyung ; Malhotra, Shweta ; Park, Ji-Hye ; Hwang, Eul ; Choi, Hong ; Kim, Young ; Tao, Weixin ; Lee, Seon-Woo
  • Subjects: Esterase ; Plant rhizosphere ; Soil metagenome
  • Is Part Of: Applied Microbiology and Biotechnology, 2010, Vol.88(5), pp.1125-1134
  • Description: Soil metagenome constitutes a reservoir for discovering novel enzymes from the unculturable microbial diversity. From three plant rhizosphere metagenomic libraries comprising a total of 142,900 members of recombinant plasmids, we obtained 14 recombinant fosmids that exhibited lipolytic activity. A selected recombinant plasmid, pFLP-2, which showed maximum lipolytic activity, was further analyzed. DNA sequence analysis of the subclone in pUC119, pELP-2, revealed an open reading frame of 1,191 bp encoding a 397-amino-acid protein. Purified EstD2 exhibited maximum enzymatic activity towards p -nitrophenyl butyrate, indicating that it is an esterase. Purified EstD2 showed optimal activity at 35 °C and at pH 8.0. The K m and K cat values were determined to be 79.4 μM and 120.5/s, respectively. The esterase exhibited an increase in enzymatic activity in the presence of 15% butanol and 15% methanol. Phylogenetic analysis revealed that the lipolytic protein EstD2 may be a member of a novel family of lipolytic enzymes. Several hypothetical protein homologs of EstD2 were found in the database. A hypothetical protein from Phenylobacterium zucineum HLK1, a close homolog of EstD2, displayed lipolytic activity when the corresponding gene was expressed in Escherichia coli . Our results suggest that the other hypothetical protein homologs of EstD2 might also be members of this novel family.
  • Language: English
  • Identifier: ISSN: 0175-7598 ; E-ISSN: 1432-0614 ; DOI: 10.1007/s00253-010-2729-6

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