Cloning, expression and characterization of a novel esterase from a South China Sea sediment metagenome

Hao Zhang; Fuchao Li; Huaxin Chen; Jin Zhao; Jinfei Yan; Peng Jiang; Ronggui Li; Baoli Zhu

doi:10.1007/s00343-015-4170-2

Your Location：

Home >

Browse articles >

Cloning, expression and characterization of a novel esterase from a South China Sea sediment metagenome

Updated：2023-05-16

- Cloning, expression and characterization of a novel esterase from a South China Sea sediment metagenome
- Journal of Oceanology and Limnology Vol. 33, Issue 4, Pages: 819-827(2015)
- Affiliations：
  
  1. Laboratory of Microbiology Shandong Province Qingdao University
  2. Key Laboratory of Experimental Marine Biology Institute of Oceanology Chinese Academy of Sciences
  3. Third Institute of Oceanography State Oceanic Administration
  4. Key Laboratory of Pathogenic Microbiology and Immunology Institute of Microbiology Chinese Academy of Sciences
- Author bio：
- Funds：
- DOI：10.1007/s00343-015-4170-2
  CLC：
- Online First：30 June 2015，
  
  Published：2015
- Accepted：
Scan QR Code
Zhang, H., Li, F., Chen, H. et al. Cloning, expression and characterization of a novel esterase from a South China Sea sediment metagenome., Chin. J. Ocean. Limnol. 33, 819–827 (2015). https://doi.org/10.1007/s00343-015-4170-2
DOI：

Zhang, H., Li, F., Chen, H. et al. Cloning, expression and characterization of a novel esterase from a South China Sea sediment metagenome., Chin. J. Ocean. Limnol. 33, 819–827 (2015). https://doi.org/10.1007/s00343-015-4170-2 DOI：

摘要

Abstract

Lipolytic enzymes

including esterases and lipases

represent a group of hydrolases that catalyze the cleavage and formation of ester bonds. A novel esterase gene

scsEst01

was cloned from a South China Sea sediment metagenome. The scsEst01 gene consisted of 921 bp encoding 307 amino acid residues. The predicted amino acid sequence shared less than 90% identity with other lipolytic enzymes in the NCBI nonredundant protein database. ScsEst01 was successfully co-expressed in Escherichia coli BL21 (DE3) with chaperones (dnaK-dnaJ-grpE) to prevent the formation of inclusion bodies. The recombinant protein was purified on an immobilized metal ion affinity column containing chelating Sepharose charged with Ni2+. The enzyme was characterized using p -nitrophenol butyrate as a substrate. ScsEst01 had the highest lipolytic activity at 35°C and pH 8.0

indicative of a meso-thermophilic alkaline esterase. ScsEst01 was thermostable at 20°C. The lipolytic activity of scsEst01 was strongly increased by Fe2+

Mn2+ and 1% Tween 80 or Tween 20.

关键词

Keywords

references

Amann R I, Ludwig W, Schleifer K H. 1995. Phylogenetic identification and in situ detection of individual microbial cells without cultivation. Microbiol. Rev., 59(1): 143–169.

Arpigny J L, Jaeger K E. 1999. Bacterial lipolytic enzymes: classification and properties. Biochem. J., 343: 177–183.

Bayer S, Kunert A, Ballschmiter M, Greiner-Stoeffele T. 2010. Indication for a new lipolytic enzyme family: isolation and characterization of two esterases from a metagenomic library. J. Mol. Microbiol. Biotechnol., 18(3): 181–187.

Bornscheuer U T. 2002. Microbial carboxyl esterases: classification, properties and application in biocatalysis. FEMS Microbiol. Rev., 26(1): 73–81.

Bradford M M. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem., 72(1–2): 248–254.

Chu X M, He H Z, Guo C Q, Sun B L. 2008. Identification of two novel esterases from a marine metagenomic library derived from South China Sea. Appl. Microbiol. Biotechnol., 80(4): 615–625.

Elend C, Schmeisser C, Hoebenreich H, Steele H L, Streit W R. 2007. Isolation and characterization of a metagenomederived and cold-active lipase with high stereospecificity for (R)-ibuprofen esters. J. Biotechnol., 130(4): 370–377.

Fu C Z, Hu Y F, Xie F, Guo H, Ashforth E J, Polyak S W, Zhu B L, Zhang L X. 2011. Molecular cloning and characterization of a new cold-active esterase from a deep-sea metagenomic library. Appl. Microbiol. Biotechnol., 90(3): 961–970.

Handelsman J, Rondon M R, Brady S F, Clardy J, Goodman R M. 1998. Molecular biological access to the chemistry of unknown soil microbes: a new frontier for natural products. Chem. Biol., 5(10): R245–R249.

Hardeman F, Sjöling S. 2007. Metagenomic approach for the isolation of a novel low-temperature-active lipase from uncultured bacteria of marine sediment. FEMS Microbiol. Ecol., 59(2): 524–534.

Hu Y F, Fu C Z, Huang Y P, Yin Y S, Cheng G, Lei F, Lu N, Li J, Ashforth E J, Zhang L X, Zhu B L. 2010. Novel lipolytic genes from the microbial metagenomic library of the South China Sea marine sediment. FEMS Microbiol. Ecol., 72(2): 228–237.

Jeon J H, Kim J T, Kang S G, Lee J H, Kim S G. 2008. Characterization and its potential application of two esterases derived from the arctic sediment metagenome. Mar. Biotechnol., 11(3): 307–316.

Jeon J H, Kim J T, Kim Y J, Kim H K, Lee H S, Kang S G, Kim S J, Lee J H. 2009. Cloning and characterization of a new cold-active lipase from a deep-sea sediment metagenome. Appl. Microbiol. Biotechnol., 81(5): 865–874.

Jia M W, Li Y D. 2005. The relationship among gene expression, folding free energy and codon usage bias in Escherichia coli. FEBS Lett., 579(24): 5 333–5 337.

Jiang X W, Xu X W, Huo Y Y, Wu Y H, Zhu X F, Zhang X Q, Wu M. 2012. Identification and characterization of novel esterases from a deep-sea sediment metagenome. Arch. Microbiol., 194(3): 207–214.

Kennedy J, Marchesi J R, Dobson A D W. 2008. Marine metagenomics: strategies for the discovery of novel enzymes with biotechnological applications from marine environments. Microb. Cell Fact., 7: 27.

Kim E Y, Oh K H, Lee M H, Kang C H, Oh T K, Yoon J H. 2009. Novel cold-adapted alkaline lipase from an intertidal flat metagenome and proposal for a new family of bacterial lipases. Appl. Environ. Microbiol., 75(1): 257–260.

Kim Y J, Choi G S, Kim S B, Yoon G S, Kim Y S, Ryu Y W. 2006. Screening and characterization of a novel esterase from a metagenomic library. Protein Expres. Purif., 45(2): 315–323.

Lämmle K, Zipper H, Breuer M, Hauer B, Buta C, Brunner H, Rupp S. 2007. Identification of novel enzymes with different hydrolytic activities by metagenome expression cloning. J. Biotechnol., 127(4): 575–592.

Lee M H, Hong K S, Malhotra S, Park J H, Hwang E C, Choi H K, Kim Y S, Tao W X, Lee S W. 2010. A new esterase EstD2 isolated from plant rhizosphere soil metagenome. Appl. Microbiol. Biotechnol., 88(5): 1 125–1 134.

Lee M H, Lee C H, Oh T K, Song J K, Yoon J H. 2006. Isolation and characterization of a novel lipase from a metagenomic library of tidal flat sediments: evidence for a new family of bacteria lipases? Appl. Environ. Microbiol., 72(11): 7 406–7 409.

Nakamura Y, Gojobori T, Ikemura T. 2000. Codon usage tabulated from international DNA sequence databases: status for the year 2000. Nucl. Acids Res., 28(1): 292.

Nishihara K, Kanemori M, Kitagawa M, Yanagi H, Yura T. 1998. Chaperone coexpression plasmids: Differential and synergistic roles of DnaK-DnaJ-GrpE and GroEL-GroES in assisting folding of an allergen of Japanese cedar pollen, Cryj2, in Escheric h ia coli. Appl. Environ. Microbiol., 64(5): 1 694–1 699.

Nishihara K, Kanemori M, Yanagi H, Yura T. 2000. Overexpression of trigger factor prevents aggregation of recombinant proteins in Escherichia coli. Appl. Environ. Microbiol., 66(3): 884–889.

Park H J, Jeon J H, Kang S G, Lee J H, Lee S A, Kim H K. 2007. Functional expression and refolding of new alkaline esterase, EM2L8 from deep-sea sediment metagenome. Protein Expres. Purif., 52(2): 340–347.

Ranjan R, Grover A, Kapardar R K, Sharma R. 2005. Isolation of novel lipolytic genes from uncultured bacteria of pond water. Biochem. Biophys. Res. Commun., 335(1): 57–65.

Roh C, Villatte F. 2008. Isolation of a low-temperature adapted lipolytic enzyme from uncultivated micro-organism. J. Appl. Microbiol., 105(1): 116–123.

Schmeisser C, Steele H, Streit W R. 2007. Metagenomics, biotechnology with non-culturable microbes. Appl. Microbiol. Biotechnol., 75(5): 955–962.

Sheridan P P, Panasik N, Coombs J M, Brenchley J E. 2000. Approaches for deciphering the structural basis of low temperature enzyme activity. Biochim. Biophys. Acta, 1543(2): 417–433.

Tamura K, Dudley J, Nei M, Kumar S. 2007. MEGA4: molecular evolutionary genetics analysis (MEGA) software version 4.0. Mol. Biol. Evol., 24(8): 1 596–1 599.

Thomas J G, Ayling A, Baneyx F. 1997. Molecular chaperones, folding catalysts, and the recovery of active recombinant proteins from E. coli. To fold or to refold. Appl. Biochem. Biotechnol., 66(3): 197–238.

Thompson J D, Gibson T J, Plewniak F, Jeanmougin F, Higgins D G. 1997. The CLUSTAL_X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools. Nucl. Acids Res., 25(24): 4 876–4 882.

Views

Downloads

CSCD

Alert me when the article has been cited

Submit

Tools

Publicity Resources

Diversity and community structure of eukaryotic microalgae in surface sediments in the central Bohai Sea, China, based on a metabarcoding approach

The role of Smad6 in immunity of the pearl oyster Pinctada fucata martensii

Cloning of catalase gene and antioxidant genes in Scophthalmus maximus response to metalloprotease of Vibrio anguillarum stress

Triterpenoid saponin biosynthesis genes and their expression patterns during the development of sea cucumber Apostichopus japonicus

Distribution pattern and geochemical analysis of rare earth elements in deep-ocean sediments

Related Author

Zhaohui WANG

Chaofan WANG

Maoting WANG

Weiguo LI

Wencong ZHONG

Lei LIU

Tao JIANG

Yu SHI

Related Institution

School of Ocean, Yantai University

Engineering Research Center of Tropical and Subtropical Aquatic Ecological Engineering, Ministry of Education

College of Life Science and Technology, Jinan University

Southern Marine Science and Engineering Guangdong Laboratory (Guangzhou)

CAS Key Laboratory of Tropical Marine Bio-resources and Ecology, Guangdong Provincial Key Laboratory of Applied Marine Biology, South China Sea Institute of Oceanology, Chinese Academy of Sciences

Address：Editorial Office of JOL, 88 Haijun Rd. Qingdao, 266000, China
Tel：+86-532-82898754 Email：jol@qdio.ac.cn
Technical support is provided by Beijing Founder electronics co., LTD 京ICP备09064830号-19 京公网安备11010802024621
It is recommended to read the content of this site in Chrome&IE9+. Please switch to extreme mode in browser 360.
Cookies We use cookies to help provide and enhance our service and tailor content. By continuing, you agree to the use of cookies.

⁰