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Volumn 12, Issue 5, 2011, Pages 2917-2934

A newly isolated thermostable lipase from bacillus sp

Author keywords

Bacillus sp. strain L2; Characterization; Cloning; Molecular expression; Sequencing; Thermostable lipase

Indexed keywords

ASPARTIC ACID; BENZYLSULFONYL FLUORIDE; DITHIOTHREITOL; DNA 16S; EDETIC ACID; GLUTAMIC ACID; HISTIDINE; MERCAPTOETHANOL; PEPSTATIN; RECOMBINANT ENZYME; RNA 16S; SERINE; SIGNAL PEPTIDE; TRIACYLGLYCEROL LIPASE; BACTERIAL PROTEIN;

EID: 79957909903     PISSN: None     EISSN: 14220067     Source Type: Journal    
DOI: 10.3390/ijms12052917     Document Type: Article
Times cited : (45)

References (31)
  • 1
    • 0033214082 scopus 로고    scopus 로고
    • Bacterial lipolytic enzymes: Classification and properties
    • Arpigny, J.L.; Jaeger, K.-E. Bacterial lipolytic enzymes: Classification and properties. Biochem. J. 1999, 343, 177-183.
    • (1999) Biochem. J , vol.343 , pp. 177-183
    • Arpigny, J.L.1    Jaeger, K.-E.2
  • 3
    • 0035725911 scopus 로고    scopus 로고
    • Production, purification, characterization, and applications of lipases
    • Sharma, R.; Chisti, Y.; Banerjee, U.C. Production, purification, characterization, and applications of lipases. Biotech. Adv. 2002, 19, 627-662.
    • (2002) Biotech. Adv , vol.19 , pp. 627-662
    • Sharma, R.1    Chisti, Y.2    Banerjee, U.C.3
  • 4
    • 0026469488 scopus 로고
    • The enzymes from extreme thermophiles: Bacterial sources, thermostabilities and industrial relevance
    • Coolbear, T.; Daniel R.M.; Morgan H.W. The enzymes from extreme thermophiles: Bacterial sources, thermostabilities and industrial relevance. Adv. Biochem. Eng. Biotechnol. 1992, 45, 57-98.
    • (1992) Adv. Biochem. Eng. Biotechnol , vol.45 , pp. 57-98
    • Coolbear, T.1    Daniel, R.M.2    Morgan, H.W.3
  • 5
    • 0035064602 scopus 로고    scopus 로고
    • Taxonomic study of aerobic thermophilic bacilli: Descriptions of Geobacillus subterraneus gen. nov., sp. nov. and Geobacillus uzenensis sp. nov. from petroleum reservoirs and transfer of Bacillus stearothermophilus, Bacillus thermocatenulatus, Bacillus thermoleovorans, Bacillus kaustophilus, Bacillus thermoglucosidasius
    • Nazina, T.N.; Tourova, T.P.; Poltaraus, A.B.; Novikova, E.V.; Grigoryan, A.A.; Ivanova, A.E.; Lysenko, A.M.; Petrunyaka, V.V.; Osipov, G.A.; Belyaev, S.S.; Ivanov, M.V. Taxonomic study of aerobic thermophilic bacilli: Descriptions of Geobacillus subterraneus gen. nov., sp. nov. and Geobacillus uzenensis sp. nov. from petroleum reservoirs and transfer of Bacillus stearothermophilus, Bacillus thermocatenulatus, Bacillus thermoleovorans, Bacillus kaustophilus, Bacillus thermoglucosidasius and Bacillus thermodenitrificans to Geobacillus as the new combinations G. stearothermophilus, G. thermocatenulatus, G. thermoleovorans, G. kaustophilus, G. thermoglucosidasius and G. thermodenitrificans. Int. J. Syst. Evol. Micr. 2001, 51, 433-446.
    • (2001) Int. J. Syst. Evol. Micr , vol.51 , pp. 433-446
    • Nazina, T.N.1    Tourova, T.P.2    Poltaraus, A.B.3    Novikova, E.V.4    Grigoryan, A.A.5    Ivanova, A.E.6    Lysenko, A.M.7    Petrunyaka, V.V.8    Osipov, G.A.9    Belyaev, S.S.10    Ivanov, M.V.11
  • 6
    • 84856013665 scopus 로고    scopus 로고
    • ExPASy Tools. accessed on 14 April 2011
    • ExPASy Tools. ExPASy Proteomics Server. Swiss Institute of Bioinformatics: Lausanne, Switzerland, 2011. Available online: http://www.expasy.org/tool (accessed on 14 April 2011).
    • (2011) ExPASy Proteomics Server
  • 7
    • 84856005087 scopus 로고    scopus 로고
    • Center for Biological Sequence Analysis (CBS): Lyngby, Denmark
    • SignalP Server. SignalP V2.0.b2. Center for Biological Sequence Analysis (CBS): Lyngby, Denmark, 2011. Available online: http://www.cbs.dtu.dk/services/SignalP-2.0/ (accessed on 14 April 2011).
    • (2011) SignalP V2.0.b2
  • 8
  • 10
    • 0034864538 scopus 로고    scopus 로고
    • Optimization of a thermostable lipase from Bacillus stearothermophilus P1: Overexpression, purification, and characterization
    • Sinchaikul, S.; Sookkheo, B.; Phutrakul, S.; Pan, F.M.; Chen, S.T. Optimization of a thermostable lipase from Bacillus stearothermophilus P1: Overexpression, purification, and characterization. Protein Expr. Purif. 2001, 22, 388-398.
    • (2001) Protein Expr. Purif , vol.22 , pp. 388-398
    • Sinchaikul, S.1    Sookkheo, B.2    Phutrakul, S.3    Pan, F.M.4    Chen, S.T.5
  • 11
    • 4544341220 scopus 로고    scopus 로고
    • High level expression of thermostable lipase from Geobacillus sp. Strain T1
    • Leow, T.C.; Rahman, R.N.Z.R.A.; Basri, M.; Salleh, A.B. High level expression of thermostable lipase from Geobacillus sp. Strain T1. Biosci. Biotech. Biochem. 2004, 68, 96-103.
    • (2004) Biosci. Biotech. Biochem , vol.68 , pp. 96-103
    • Leow, T.C.1    Rahman, R.N.Z.R.A.2    Basri, M.3    Salleh, A.B.4
  • 12
    • 0035820995 scopus 로고    scopus 로고
    • Over-expression and properties of a purified recombinant Bacillus licheniformis lipase: A comparative report on Bacillus lipases
    • Nthangeni, M.B.; Patterton, H.G.; van Tonder, A.; Vergeer, W.P. Over-expression and properties of a purified recombinant Bacillus licheniformis lipase: A comparative report on Bacillus lipases. Enzyme Microbial. Technol. 2001, 28, 705-712.
    • (2001) Enzyme Microbial. Technol , vol.28 , pp. 705-712
    • Nthangeni, M.B.1    Patterton, H.G.2    van Tonder, A.3    Vergeer, W.P.4
  • 13
    • 33646591284 scopus 로고    scopus 로고
    • Expression, purification, and characterization of His-tagged Staphylococcus xylosus lipase wild-type and its mutant Asp 290 Ala
    • Mosbah, H.; Sayari, A.; Bezzine, S.; Gargouri, Y. Expression, purification, and characterization of His-tagged Staphylococcus xylosus lipase wild-type and its mutant Asp 290 Ala. Protein Expr. Purif. 2006, 47, 516-523.
    • (2006) Protein Expr. Purif , vol.47 , pp. 516-523
    • Mosbah, H.1    Sayari, A.2    Bezzine, S.3    Gargouri, Y.4
  • 14
    • 0032843146 scopus 로고    scopus 로고
    • Production, purification and characterization of thermophilic lipase from Bacillus sp. THL027
    • Dharmsthiti, S.; Luchai, S. Production, purification and characterization of thermophilic lipase from Bacillus sp. THL027. FEMS Microbiol. Lett. 1999, 179, 241-246.
    • (1999) FEMS Microbiol. Lett , vol.179 , pp. 241-246
    • Dharmsthiti, S.1    Luchai, S.2
  • 16
    • 0031722751 scopus 로고    scopus 로고
    • A novel thermostable lipase from a thermophilic Bacillus sp.: Characterization and esterification studies
    • Nawani, N.; Dosanjh, N.S.; Kaur, J. A novel thermostable lipase from a thermophilic Bacillus sp.: Characterization and esterification studies. Biotechnol. Lett. 1998, 20, 997-1000.
    • (1998) Biotechnol. Lett , vol.20 , pp. 997-1000
    • Nawani, N.1    Dosanjh, N.S.2    Kaur, J.3
  • 17
    • 0035725911 scopus 로고    scopus 로고
    • Production, purification, characterization, and applications of lipases
    • Sharma, R.; Chisti, Y.; Banerjee, U.C. Production, purification, characterization, and applications of lipases. Biotech. Adv. 2002, 19, 627-662.
    • (2002) Biotech. Adv , vol.19 , pp. 627-662
    • Sharma, R.1    Chisti, Y.2    Banerjee, U.C.3
  • 18
    • 0029016003 scopus 로고
    • Thermostable alkaline lipase from a newly isolated themrophilic Bacillus strain, A30-1 (ATCC 53841)
    • Wang, Y.; Srivastava, K.C.; Shen, G.J.; Wang, H.Y. Thermostable alkaline lipase from a newly isolated themrophilic Bacillus strain, A30-1 (ATCC 53841). J. Ferment. Bioengineer. 1995, 79, 433-438.
    • (1995) J. Ferment. Bioengineer , vol.79 , pp. 433-438
    • Wang, Y.1    Srivastava, K.C.2    Shen, G.J.3    Wang, H.Y.4
  • 19
    • 0035807424 scopus 로고    scopus 로고
    • Purification and characterization of two distinct thermostable lipases from the gram-posistive thermophilic bacterium Bacillus thermoleovorans ID-1
    • Lee, D.W.; Kim, H.W.; Lee, K.W.; Kim, B.C.; Choe, E.A.; Lee, H.S.; Kim, D.S.; Pyun, Y.R. Purification and characterization of two distinct thermostable lipases from the gram-posistive thermophilic bacterium Bacillus thermoleovorans ID-1. Enzyme Microbial. Technol. 2001, 29, 363-371.
    • (2001) Enzyme Microbial. Technol , vol.29 , pp. 363-371
    • Lee, D.W.1    Kim, H.W.2    Lee, K.W.3    Kim, B.C.4    Choe, E.A.5    Lee, H.S.6    Kim, D.S.7    Pyun, Y.R.8
  • 20
    • 0031613603 scopus 로고    scopus 로고
    • Gene cloning and characterisation of thermostable lipase from Bacillus stearothermophilus
    • Kim, H.-K.; Park, S.-Y.; Lee, J.-K.; Oh, T.-K. Gene cloning and characterisation of thermostable lipase from Bacillus stearothermophilus. Biosci. Biotech. Biochem. 1998, 62, 66-71.
    • (1998) Biosci. Biotech. Biochem , vol.62 , pp. 66-71
    • Kim, H.-K.1    Park, S.-Y.2    Lee, J.-K.3    Oh, T.-K.4
  • 21
    • 0002967367 scopus 로고
    • Stabilization of enzymes with soluble additives
    • Gupta, M.N., Ed.; Narosa: New Delhi, India
    • Gary, C.J. Stabilization of enzymes with soluble additives. In Thermostability of Enzyme; Gupta, M.N., Ed.; Narosa: New Delhi, India, 1995; pp. 124-143.
    • (1995) Thermostability of Enzyme , pp. 124-143
    • Gary, C.J.1
  • 22
    • 0034672122 scopus 로고    scopus 로고
    • Estimation of protein secondary structure from circular dichroism spectra: Inclusion of denatured proteins with native proteins in the analysis
    • Sreerama, N.; Venyaminov, S.Y.; Woody, R.W. Estimation of protein secondary structure from circular dichroism spectra: Inclusion of denatured proteins with native proteins in the analysis. Anal. Biochem. 2000, 287, 243-251.
    • (2000) Anal. Biochem , vol.287 , pp. 243-251
    • Sreerama, N.1    Venyaminov, S.Y.2    Woody, R.W.3
  • 23
    • 0034815186 scopus 로고    scopus 로고
    • Towards the three-dimensional structure of the Escherichia coli DNA-binding protein H-NS: A CD and fluorescence study
    • Schröder, O.; Tippner, D.; Wagner, R. Towards the three-dimensional structure of the Escherichia coli DNA-binding protein H-NS: A CD and fluorescence study. Biochem. Biop. Res. Co. 2001, 282, 219-227.
    • (2001) Biochem. Biop. Res. Co , vol.282 , pp. 219-227
    • Schröder, O.1    Tippner, D.2    Wagner, R.3
  • 24
    • 0022503457 scopus 로고
    • Calculation of protein conformation from circular dichroism
    • Yang, J.T.; Wu, C.S.C.; Martinez, H.M. Calculation of protein conformation from circular dichroism. Meth. Enzymol. 1986, 130, 208-269.
    • (1986) Meth. Enzymol , vol.130 , pp. 208-269
    • Yang, J.T.1    Wu, C.S.C.2    Martinez, H.M.3
  • 27
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson, J.D.; Higgins, D.G.; Gibson, T.J. CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucl. Acids Res. 1994, 22, 4673-4680.
    • (1994) Nucl. Acids Res , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 28
    • 84856002140 scopus 로고    scopus 로고
    • USA, SDSC Biology Workbench, accessed on 14 April 2011
    • SDSC Biology Workbench. San Diego Supercomputer Center: San Diego, USA, 2011. Available online: http://workbench.sdsc.edu/ (accessed on 14 April 2011).
    • (2011) San Diego Supercomputer Center: San Diego
  • 29
    • 84870490179 scopus 로고    scopus 로고
    • MD, USA NCBI/BLAST-Basic Logic Alignment Search Tool, accessed on 14 April 2011
    • NCBI/BLAST-Basic Logic Alignment Search Tool. National Center for Biotechnology Information (NCBI): Bethesda, MD, USA, 2011. Available online: http://blast.ncbi.nlm.nih.gov/Blast.cgi (accessed on 14 April 2011).
    • (2011) National Center For Biotechnology Information (NCBI): Bethesda
  • 30
    • 51649151571 scopus 로고
    • A simple and rapid colorimetric method for determination of free fatty acids for lipase assay
    • Kwon, D.K.; Rhee, J.S. A simple and rapid colorimetric method for determination of free fatty acids for lipase assay. J. Am. Oil. Chem. Soc. 1986, 63, 89-92.
    • (1986) J. Am. Oil. Chem. Soc , vol.63 , pp. 89-92
    • Kwon, D.K.1    Rhee, J.S.2
  • 31
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970, 227, 380-685.
    • (1970) Nature , vol.227 , pp. 380-685
    • Laemmli, U.K.1


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