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A novel β-glucosidase with lipolytic activity from a soil metagenome

Moonlighting proteins have two different functions within a single polypeptide chain. Exploring moonlighting enzymes from the environment using the metagenomic approach is interesting. In the present study, a novel β-glucosidase gene, designated as bgl1D , with lipolytic activity (renamed Lip1C) was... Full description

Journal Title: Folia Microbiologica 2011, Vol.56(6), pp.563-570
Main Author: Jiang, Cheng-Jian
Other Authors: Chen, Gao , Huang, Jie , Huang, Qin , Jin, Ke , Shen, Pei-Hong , Li, Jun-Fang , Wu, Bo
Format: Electronic Article Electronic Article
Language: English
Subjects:
ID: ISSN: 0015-5632 ; E-ISSN: 1874-9356 ; DOI: 10.1007/s12223-011-0083-4
Link: http://dx.doi.org/10.1007/s12223-011-0083-4
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recordid: springer_jour10.1007/s12223-011-0083-4
title: A novel β-glucosidase with lipolytic activity from a soil metagenome
format: Article
creator:
  • Jiang, Cheng-Jian
  • Chen, Gao
  • Huang, Jie
  • Huang, Qin
  • Jin, Ke
  • Shen, Pei-Hong
  • Li, Jun-Fang
  • Wu, Bo
subjects:
  • Lipase -- Analysis
  • Esters -- Analysis
  • Aluminum Compounds -- Analysis
  • Genetically Modified Organisms -- Analysis
  • Genes -- Analysis
  • Cladistic Analysis -- Analysis
  • Enzymology -- Analysis
  • Soil Microbiology -- Analysis
ispartof: Folia Microbiologica, 2011, Vol.56(6), pp.563-570
description: Moonlighting proteins have two different functions within a single polypeptide chain. Exploring moonlighting enzymes from the environment using the metagenomic approach is interesting. In the present study, a novel β-glucosidase gene, designated as bgl1D , with lipolytic activity (renamed Lip1C) was cloned through function-based screening of a metagenomic library from uncultured soil microorganisms. The deduced amino acid sequence comparison and phylogenetic analysis also indicated that Lip1C and other putative lipases are closely related. Biochemical characterization demonstrated that the maximum activity of the recombinant Lip1C protein occurs at pH 8.0 and 30°C using 4-nitrophenyl butyrate as substrate. The putative lipase had an apparent K m value of 0.88 mmol/L, a k cat value of 212/min, and a k cat / K m value of 241 L/mmol/min. Lip1C exhibited habitat-specific characteristics with 5 mmol/L AlCl 3 , CuCl 2 , and LiCl. The characterization of the biochemical properties of Lip1C enhances our understanding of this novel moonlighting enzyme isolated from a soil metagenome.
language: eng
source:
identifier: ISSN: 0015-5632 ; E-ISSN: 1874-9356 ; DOI: 10.1007/s12223-011-0083-4
fulltext: fulltext
issn:
  • 1874-9356
  • 18749356
  • 0015-5632
  • 00155632
url: Link


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titleA novel β-glucosidase with lipolytic activity from a soil metagenome
creatorJiang, Cheng-Jian ; Chen, Gao ; Huang, Jie ; Huang, Qin ; Jin, Ke ; Shen, Pei-Hong ; Li, Jun-Fang ; Wu, Bo
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descriptionMoonlighting proteins have two different functions within a single polypeptide chain. Exploring moonlighting enzymes from the environment using the metagenomic approach is interesting. In the present study, a novel β-glucosidase gene, designated as bgl1D , with lipolytic activity (renamed Lip1C) was cloned through function-based screening of a metagenomic library from uncultured soil microorganisms. The deduced amino acid sequence comparison and phylogenetic analysis also indicated that Lip1C and other putative lipases are closely related. Biochemical characterization demonstrated that the maximum activity of the recombinant Lip1C protein occurs at pH 8.0 and 30°C using 4-nitrophenyl butyrate as substrate. The putative lipase had an apparent K m value of 0.88 mmol/L, a k cat value of 212/min, and a k cat / K m value of 241 L/mmol/min. Lip1C exhibited habitat-specific characteristics with 5 mmol/L AlCl 3 , CuCl 2 , and LiCl. The characterization of the biochemical properties of Lip1C enhances our understanding of this novel moonlighting enzyme isolated from a soil metagenome.
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titleA novel β-glucosidase with lipolytic activity from a soil metagenome
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abstractMoonlighting proteins have two different functions within a single polypeptide chain. Exploring moonlighting enzymes from the environment using the metagenomic approach is interesting. In the present study, a novel β-glucosidase gene, designated as bgl1D , with lipolytic activity (renamed Lip1C) was cloned through function-based screening of a metagenomic library from uncultured soil microorganisms. The deduced amino acid sequence comparison and phylogenetic analysis also indicated that Lip1C and other putative lipases are closely related. Biochemical characterization demonstrated that the maximum activity of the recombinant Lip1C protein occurs at pH 8.0 and 30°C using 4-nitrophenyl butyrate as substrate. The putative lipase had an apparent K m value of 0.88 mmol/L, a k cat value of 212/min, and a k cat / K m value of 241 L/mmol/min. Lip1C exhibited habitat-specific characteristics with 5 mmol/L AlCl 3 , CuCl 2 , and LiCl. The characterization of the biochemical properties of Lip1C enhances our understanding of this novel moonlighting enzyme isolated from a soil metagenome.
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doi10.1007/s12223-011-0083-4
pages563-570
date2011-11