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Volumn 3, Issue 1, 2013, Pages 38-51

Halophilic bacteria as a source of novel hydrolytic enzymes

Author keywords

Extremophiles; Halophiles; Hydrolases; Saline environments

Indexed keywords


EID: 84883133783     PISSN: None     EISSN: 20751729     Source Type: Journal    
DOI: 10.3390/life3010038     Document Type: Review
Times cited : (146)

References (58)
  • 1
    • 84926997740 scopus 로고    scopus 로고
    • Unusual microorganisms from unusual habitats: Hypersaline environments
    • In Logan, N.A., Lppin-Scott, H.M., Oyston, P.C.F., Eds.; Cambridge University Press: Cambridge, UK
    • Ventosa, A. Unusual microorganisms from unusual habitats: hypersaline environments. In Prokaryotic Diversity-Mechanism and Significance; Logan, N.A., Lppin-Scott, H.M., Oyston, P.C.F., Eds.; Cambridge University Press: Cambridge, UK, 2006; pp. 223-253.
    • (2006) Prokaryotic Diversity-Mechanism and Significance , pp. 223-253
    • Ventosa, A.1
  • 2
    • 0001300343 scopus 로고
    • Physiology of halophilic eubacteria
    • In Rodríguez-Varela, F., Ed.; CRC Press: Boca Raton, FL, USA
    • Kushner, D.J.; Kamekura, M. Physiology of halophilic eubacteria. In Halophilic Bacteria; Rodríguez-Varela, F., Ed.; CRC Press: Boca Raton, FL, USA, 1988; pp. 109-138.
    • (1988) Halophilic Bacteria , pp. 109-138
    • Kushner, D.J.1    Kamekura, M.2
  • 3
    • 0033152499 scopus 로고    scopus 로고
    • Thermophilic and halophilic extremophiles
    • Madigan, M.T.; Oren, A. Thermophilic and halophilic extremophiles. Curr. Opin. Microbiol. 1999, 2, 265-269.
    • (1999) Curr. Opin. Microbiol. , vol.2 , pp. 265-269
    • Madigan, M.T.1    Oren, A.2
  • 4
    • 0036160908 scopus 로고    scopus 로고
    • Diversity of halophilic microorganisms: Environments, phylogeny, physiology, and applications
    • Oren, A. Diversity of halophilic microorganisms: Environments, phylogeny, physiology, and applications. J. Ind. Microbiol. Biotechnol. 2002, 28, 58-63.
    • (2002) J. Ind. Microbiol. Biotechnol. , vol.28 , pp. 58-63
    • Oren, A.1
  • 5
    • 5444271013 scopus 로고    scopus 로고
    • Synthesis of osmoprotectants by moderately halophilic bacteria: Genetic and applied aspects
    • Nieto, J.J.; Vargas, C. Synthesis of osmoprotectants by moderately halophilic bacteria: Genetic and applied aspects. Recent. Res. Devel. Microbiol. 2002, 6, 403-418.
    • (2002) Recent. Res. Devel. Microbiol. , vol.6 , pp. 403-418
    • Nieto, J.J.1    Vargas, C.2
  • 6
    • 5444268493 scopus 로고    scopus 로고
    • Biotechnological potential of moderately and extremely halophilic microorganisms
    • In n; Barredo, J.L., Ed.; Research Signpost: Kerala, India
    • Mellado, E.; Ventosa, A. Biotechnological potential of moderately and extremely halophilic microorganisms. In Microorganisms for Health Care, Food and Enzyme Production; Barredo, J.L., Ed.; Research Signpost: Kerala, India, 2003; pp. 233-256.
    • (2003) Microorganisms for Health Care, Food and Enzyme Productio , pp. 233-256
    • Mellado, E.1    Ventosa, A.2
  • 7
    • 11144243173 scopus 로고    scopus 로고
    • The biocatalytic potential of extremophiles and extremozymes
    • Gómez, J.; Steiner, W. The biocatalytic potential of extremophiles and extremozymes. Food Technol. Biotechnol. 2004, 2, 223-235.
    • (2004) Food Technol. Biotechnol. , vol.2 , pp. 223-235
    • Gómez, J.1    Steiner, W.2
  • 8
    • 77953700376 scopus 로고    scopus 로고
    • Industrial and environmental applications of halophilic microorganisms
    • Oren, A. Industrial and environmental applications of halophilic microorganisms. Environ. Technol. 2010, 31, 825-834.
    • (2010) Environ. Technol. , vol.31 , pp. 825-834
    • Oren, A.1
  • 10
    • 34247159537 scopus 로고    scopus 로고
    • Lipases from extremophiles and potential for industrial applications
    • Salameh, M.; Wiegel, J. Lipases from extremophiles and potential for industrial applications. Adv. Appl. Microbiol. 2007, 61, 253-283.
    • (2007) Adv. Appl. Microbiol. , vol.61 , pp. 253-283
    • Salameh, M.1    Wiegel, J.2
  • 11
    • 0037241080 scopus 로고    scopus 로고
    • Diversity of moderately halophilic bacteria producing extracellular hydrolytic enzymes
    • Sánchez-Porro, C.; Martín, S.; Mellado, E.; Ventosa, A. Diversity of moderately halophilic bacteria producing extracellular hydrolytic enzymes. J. Appl. Microbiol. 2003, 94, 295-300.
    • (2003) J. Appl. Microbiol. , vol.94 , pp. 295-300
    • Sánchez-Porro, C.1    Martín, S.2    Mellado, E.3    Ventosa, A.4
  • 12
    • 0003024258 scopus 로고
    • Taxonomy of moderately halophilic heterotrophic eubacteria
    • In Rodríguez-Valera, F., Ed.; CRC Press: Boca Raton, FL, USA
    • Ventosa, A. Taxonomy of moderately halophilic heterotrophic eubacteria. In Halophilic bacteria. Rodríguez-Valera, F., Ed.; CRC Press: Boca Raton, FL, USA, 1988; pp. 71-84.
    • (1988) Halophilic bacteria. , pp. 71-84
    • Ventosa, A.1
  • 13
  • 15
    • 61649095228 scopus 로고    scopus 로고
    • Characterization of Salicola sp. IC10, a lipase-and protease-producing extreme halophile
    • Moreno, M.L.; García, M.T.; Ventosa, A.; Mellado, E. Characterization of Salicola sp. IC10, a lipase-and protease-producing extreme halophile. FEMS Microbiol. Ecol. 2009, 68, 59-71.
    • (2009) FEMS Microbiol. Ecol. , vol.68 , pp. 59-71
    • Moreno, M.L.1    García, M.T.2    Ventosa, A.3    Mellado, E.4
  • 17
    • 33746265913 scopus 로고    scopus 로고
    • Salicola marasensis gen. nov., sp. nov., an extremely halophilic bacterium isolated from the Maras solar salterns in Perú
    • Maturrano, L.; Valens-Vadell, M.; Roselló-Mora, R.; Antón, J. Salicola marasensis gen. nov., sp. nov., an extremely halophilic bacterium isolated from the Maras solar salterns in Perú. Int. J. Syst. Evol. Microbiol. 2006, 56, 1685-1691.
    • (2006) Int. J. Syst. Evol. Microbiol. , vol.56 , pp. 1685-1691
    • Maturrano, L.1    Valens-Vadell, M.2    Roselló-Mora, R.3    Antón, J.4
  • 18
    • 61349198759 scopus 로고    scopus 로고
    • Screening and isolation of halophilic bacteria producing extracellular hydrolyses from Howz Soltan Lake, Iran
    • Rohban, R.; Amoozegar, M.A.; Ventosa, A. Screening and isolation of halophilic bacteria producing extracellular hydrolyses from Howz Soltan Lake, Iran. J. Ind. Microbiol. Biotechnol. 2009, 36, 333-340.
    • (2009) J. Ind. Microbiol. Biotechnol. , vol.36 , pp. 333-340
    • Rohban, R.1    Amoozegar, M.A.2    Ventosa, A.3
  • 20
    • 79961162778 scopus 로고    scopus 로고
    • Isolation and Characterization of Some Moderately Halophilic Bacteria with Lipase Activity
    • Ghasemi, Y.; Rasoul-Amini, S.; Kazemi, A.; Zarrini, G.; Morowvat, M.T.; Kargar, M. Isolation and Characterization of Some Moderately Halophilic Bacteria with Lipase Activity. Microbiology 2011, 80, 483-487.
    • (2011) Microbiology , vol.80 , pp. 483-487
    • Ghasemi, Y.1    Rasoul-Amini, S.2    Kazemi, A.3    Zarrini, G.4    Morowvat, M.T.5    Kargar, M.6
  • 22
    • 0037086196 scopus 로고    scopus 로고
    • Metabolic activity of subsurface life in deep-sea sediments
    • D'Hondt, S.; Rutherford, S.; Spivack, A.J. Metabolic activity of subsurface life in deep-sea sediments. Science 2012, 295, 2067-2070.
    • (2012) Science , vol.295 , pp. 2067-2070
    • D'Hondt, S.1    Rutherford, S.2    Spivack, A.J.3
  • 25
    • 57449104900 scopus 로고    scopus 로고
    • Extracellular hydrolytic enzyme screening of culturable heterotrophic bacteria from deep-sea sediments of the Southern Okinawa Trough
    • Dang, H.; Zhu, H.; Wang, J.; Li, T. Extracellular hydrolytic enzyme screening of culturable heterotrophic bacteria from deep-sea sediments of the Southern Okinawa Trough. World J. Microbiol. Biotechnol. 2009, 25, 71-79.
    • (2009) World J. Microbiol. Biotechnol. , vol.25 , pp. 71-79
    • Dang, H.1    Zhu, H.2    Wang, J.3    Li, T.4
  • 26
    • 25844519572 scopus 로고    scopus 로고
    • Extracellular DNA plays a key role in deep-sea ecosystem functioning
    • DelľAnno, A.; Danovaro, R. Extracellular DNA plays a key role in deep-sea ecosystem functioning. Science 2005, 309, 2179.
    • (2005) Science , vol.309 , pp. 2179
    • DelľAnno, A.1    Danovaro, R.2
  • 27
    • 77951664490 scopus 로고    scopus 로고
    • Extracellular hydrolytic enzymes of halophilic bacteria isolated from a subterranean rock salt crystal
    • Cojoc, R.; Merciu, S.; Popescu, G.; Dumitru, L.; Kamekura, M.; Enache, M. Extracellular hydrolytic enzymes of halophilic bacteria isolated from a subterranean rock salt crystal. Rom. Biotechnol. Lett. 2009, 14, 4658-4664.
    • (2009) Rom. Biotechnol. Lett. , vol.14 , pp. 4658-4664
    • Cojoc, R.1    Merciu, S.2    Popescu, G.3    Dumitru, L.4    Kamekura, M.5    Enache, M.6
  • 28
    • 84865303557 scopus 로고    scopus 로고
    • Analysis and characterization of cultivable extremophilic hydrolytic bacterial community in heavy-metal-contaminated soils from the Atacama Desert and their biotechnological potentials
    • Moreno, M.L.; Piubeli, F.; Bonfá, M.R.; García, M.T.; Durrant, L.R.; Mellado, E. Analysis and characterization of cultivable extremophilic hydrolytic bacterial community in heavy-metal-contaminated soils from the Atacama Desert and their biotechnological potentials. J. Appl. Microbiol. 2012, 113, 550-559.
    • (2012) J. Appl. Microbiol. , vol.113 , pp. 550-559
    • Moreno, M.L.1    Piubeli, F.2    Bonfá, M.R.3    García, M.T.4    Durrant, L.R.5    Mellado, E.6
  • 29
    • 33244481748 scopus 로고    scopus 로고
    • The status of the genus name Halovibrio. Fendrich 1988 and the identity of the strains Pseudomonas halophila DSM 3050 and Halomonas. variabilis DSM 3051. Request for an opinion
    • Sorokin, D.Y.; Tindall, B.J. The status of the genus name Halovibrio. Fendrich 1988 and the identity of the strains Pseudomonas halophila DSM 3050 and Halomonas. variabilis DSM 3051. Request for an opinion. Int. J. Syst. Evol. Microbiol. 2006, 56, 487-489.
    • (2006) Int. J. Syst. Evol. Microbiol. , vol.56 , pp. 487-489
    • Sorokin, D.Y.1    Tindall, B.J.2
  • 30
    • 5444225550 scopus 로고    scopus 로고
    • Halomonas. organivorans sp. nov., a moderate halophile able to degrade aromatic compounds
    • García, M.T.; Mellado, E.; Ostos, J.C.; Ventosa, A. Halomonas. organivorans sp. nov., a moderate halophile able to degrade aromatic compounds. Int. J. Syst. Evol. Microbiol. 2004, 54, 1723-1728.
    • (2004) Int. J. Syst. Evol. Microbiol. , vol.54 , pp. 1723-1728
    • García, M.T.1    Mellado, E.2    Ostos, J.C.3    Ventosa, A.4
  • 31
    • 0025321409 scopus 로고
    • Salinicoccus. roseus gen. nov., a new moderately halophilic Gram-positive coccus
    • Ventosa, A.; Marquez, M.C.; Ruiz-Berraquero, F.; Kocur, M. Salinicoccus. roseus gen. nov., a new moderately halophilic Gram-positive coccus. Syst. Appl. Microbiol. 1990, 13, 29-33.
    • (1990) Syst. Appl. Microbiol. , vol.13 , pp. 29-33
    • Ventosa, A.1    Marquez, M.C.2    Ruiz-Berraquero, F.3    Kocur, M.4
  • 32
    • 84894346731 scopus 로고    scopus 로고
    • Amylase from moderate halophiles isolated from wild ass excreta
    • Khunt, M.; Pandhi, N.; Rana, A. Amylase from moderate halophiles isolated from wild ass excreta. Int. J. Pharm. Bio. Sci. 2011, 1, 586-592.
    • (2011) Int. J. Pharm. Bio. Sci. , vol.1 , pp. 586-592
    • Khunt, M.1    Pandhi, N.2    Rana, A.3
  • 33
    • 1942538348 scopus 로고    scopus 로고
    • Developments in the use of Bacillus species for industrial production
    • Schallmey, M.; Singh, A.; Ward, O.P. Developments in the use of Bacillus species for industrial production. Can. J. Microbiol. 2004, 50, 1-17.
    • (2004) Can. J. Microbiol. , vol.50 , pp. 1-17
    • Schallmey, M.1    Singh, A.2    Ward, O.P.3
  • 35
    • 31044446981 scopus 로고    scopus 로고
    • Substrate specificity and kinetic properties of enzymes belonging to the hormone-sensitive lipase family: Comparison with non-lipolytic and lipolytic carboxyl esterases
    • Chahinian, H.; Ali, Y.B.; Abousalham, A.; Petry, S.; Mandrich, L.; Manco, G.; Canaan, S.; Sarda, L. Substrate specificity and kinetic properties of enzymes belonging to the hormone-sensitive lipase family: Comparison with non-lipolytic and lipolytic carboxyl esterases. Biochim. Biophys. Acta. 2005, 1738, 29-36.
    • (2005) Biochim. Biophys. Acta. , vol.1738 , pp. 29-36
    • Chahinian, H.1    Ali, Y.B.2    Abousalham, A.3    Petry, S.4    Mandrich, L.5    Manco, G.6    Canaan, S.7    Sarda, L.8
  • 36
    • 4344584774 scopus 로고    scopus 로고
    • Lipases and their industrial applications: An overview
    • Houde, A.; Kademi, A.; Leblanc, D. Lipases and their industrial applications: An overview. Appl. Biochem. Biotechnol. 2004, 46, 155-170.
    • (2004) Appl. Biochem. Biotechnol. , vol.46 , pp. 155-170
    • Houde, A.1    Kademi, A.2    Leblanc, D.3
  • 38
    • 70349408130 scopus 로고    scopus 로고
    • Molecular basis for the stereoselective ammoniolysis of N-alkyl aziridine-2-carboxylates catalyzed by Candida antarctica lipase B
    • Park, J.H.; Ha, H.J.; Lee, W.K.; Généreux-Vincent, T.; Kazlauskas, R.J. Molecular basis for the stereoselective ammoniolysis of N-alkyl aziridine-2-carboxylates catalyzed by Candida antarctica lipase B. Chembiochem 2009, 10, 2213-2222.
    • (2009) Chembiochem , vol.10 , pp. 2213-2222
    • Park, J.H.1    Ha, H.J.2    Lee, W.K.3    Généreux-Vincent, T.4    Kazlauskas, R.J.5
  • 39
    • 40849098782 scopus 로고    scopus 로고
    • Novel chromatographic resolution of chiral diacylglycerols and analysis of the stereoselective hydrolysis of triacylglycerols by lipases
    • Rodriguez, J.A.; Mendoza, L.D.; Pezzotti, F.; Vanthuyne, N.; Leclaire, J.; Verger, R.; Buono, G.; Carriere, F.; Fotiadu, F. Novel chromatographic resolution of chiral diacylglycerols and analysis of the stereoselective hydrolysis of triacylglycerols by lipases. Anal. Biochem. 2008, 375, 196-208.
    • (2008) Anal. Biochem. , vol.375 , pp. 196-208
    • Rodriguez, J.A.1    Mendoza, L.D.2    Pezzotti, F.3    Vanthuyne, N.4    Leclaire, J.5    Verger, R.6    Buono, G.7    Carriere, F.8    Fotiadu, F.9
  • 40
    • 10944270620 scopus 로고    scopus 로고
    • Acinetobacter lipases: Molecular biology, biochemical properties and biotechnological potential
    • Snellman, E.A.; Colwell, R.R. Acinetobacter lipases: molecular biology, biochemical properties and biotechnological potential. J. Ind. Microbiol. Biotechnol. 2004, 31, 391-400.
    • (2004) J. Ind. Microbiol. Biotechnol. , vol.31 , pp. 391-400
    • Snellman, E.A.1    Colwell, R.R.2
  • 43
    • 78349307290 scopus 로고    scopus 로고
    • Chemical biotechnology a marriage of convenience and necessity
    • Jaeger, K.E.; Holliger, P. Chemical biotechnology a marriage of convenience and necessity. Curr. Opin. Biotechnol. 2010, 21,711-712.
    • (2010) Curr. Opin. Biotechnol. , vol.21 , pp. 711-712
    • Jaeger, K.E.1    Holliger, P.2
  • 44
    • 0032167489 scopus 로고    scopus 로고
    • Microbial lipases form versatile tools for biotechnology
    • Jaeger, K.E.; Reetz, M.T. Microbial lipases form versatile tools for biotechnology. Trends Biotechnol. 1998, 16, 396-403.
    • (1998) Trends Biotechnol. , vol.16 , pp. 396-403
    • Jaeger, K.E.1    Reetz, M.T.2
  • 45
    • 0036445837 scopus 로고    scopus 로고
    • Purification and properties of the extracellular lipase, LipA of Acinetobacter. sp. RAG-1
    • Snellman, E.A.; Sullivan, E.R.; Colwell, R.R. Purification and properties of the extracellular lipase, LipA of Acinetobacter. sp. RAG-1. FEBS. J. 2002, 269, 5771-5779.
    • (2002) FEBS. J. , vol.269 , pp. 5771-5779
    • Snellman, E.A.1    Sullivan, E.R.2    Colwell, R.R.3
  • 47
    • 34547263402 scopus 로고    scopus 로고
    • Microbial extremophiles at the limits of life
    • Pikuta, E.V.; Hoover, R.B.; Tang, J. Microbial extremophiles at the limits of life. Crit. Rev. Microbiol. 2007, 33, 183-209.
    • (2007) Crit. Rev. Microbiol. , vol.33 , pp. 183-209
    • Pikuta, E.V.1    Hoover, R.B.2    Tang, J.3
  • 50
    • 84865660875 scopus 로고    scopus 로고
    • Identification of amino acids involved in the hydrolytic activity of lipase LipBL from Marinobacter lipolyticus
    • Pérez, D.; Kovacic, F.; Wilhelm, S.; Jaeger, K.E.; García, M.T.; Ventosa, A.; Mellado, E. Identification of amino acids involved in the hydrolytic activity of lipase LipBL from Marinobacter lipolyticus. Microbiology 2012, 158, 2192-2203.
    • (2012) Microbiology , vol.158 , pp. 2192-2203
    • Pérez, D.1    Kovacic, F.2    Wilhelm, S.3    Jaeger, K.E.4    García, M.T.5    Ventosa, A.6    Mellado, E.7
  • 52
    • 58549119191 scopus 로고    scopus 로고
    • Cloning, expression and characterization of the serine protease gene from Chaetomium thermophilum
    • Li, A.N.; Li, D.C. Cloning, expression and characterization of the serine protease gene from Chaetomium thermophilum. J. Appl. Microbiol. 2009, 106, 369-380.
    • (2009) J. Appl. Microbiol. , vol.106 , pp. 369-380
    • Li, A.N.1    Li, D.C.2
  • 53
    • 1542649404 scopus 로고    scopus 로고
    • Screening and characterization of the protease CP1 produced by the moderately halophilic bacterium Pseudoalteromonas ruthenica. sp. strain CP76
    • Sánchez-Porro, C.; Mellado, E.; Bertoldo, C.; Antranikian, G.; Ventosa, A. Screening and characterization of the protease CP1 produced by the moderately halophilic bacterium Pseudoalteromonas ruthenica. sp. strain CP76. Extremophiles. 2003, 7, 221-228.
    • (2003) Extremophiles. , vol.7 , pp. 221-228
    • Sánchez-Porro, C.1    Mellado, E.2    Bertoldo, C.3    Antranikian, G.4    Ventosa, A.5
  • 55
    • 57649225420 scopus 로고    scopus 로고
    • Production, optimization and purification of a novel extracellular protease from the moderately halophilic bacterium Halobacillus karajensis
    • Karbalaei-Heidari, H.R.; Amoozegar, M.A.; Hajighasemi, M.; Ziaee, A.A.; Ventosa, A. Production, optimization and purification of a novel extracellular protease from the moderately halophilic bacterium Halobacillus karajensis. J. Ind. Microbiol. Biotechnol. 2009, 36, 21-27.
    • (2009) J. Ind. Microbiol. Biotechnol. , vol.36 , pp. 21-27
    • Karbalaei-Heidari, H.R.1    Amoozegar, M.A.2    Hajighasemi, M.3    Ziaee, A.A.4    Ventosa, A.5
  • 57
    • 84863213938 scopus 로고    scopus 로고
    • Purification and characterization of a halophilic α-amylase with increased activity in the presence of organic solvents from the moderately halophilic Nesterenkonia sp. strain F
    • Shafiei, M.; Ziaee, A.A.; Amoozegar, M.A. Purification and characterization of a halophilic α-amylase with increased activity in the presence of organic solvents from the moderately halophilic Nesterenkonia sp. strain F. Extremophiles 2012, 16, 627-635.
    • (2012) Extremophiles , vol.16 , pp. 627-635
    • Shafiei, M.1    Ziaee, A.A.2    Amoozegar, M.A.3
  • 58
    • 84865472168 scopus 로고    scopus 로고
    • Characterization of an organic solvent-tolerant α-amylase from a halophilic isolate, Thalassobacillus sp. LY18
    • Li, X.; Yu, H.Y. Characterization of an organic solvent-tolerant α-amylase from a halophilic isolate, Thalassobacillus sp. LY18. Folia Microbiol. 2012, 57, 447-453.
    • (2012) Folia Microbiol. , vol.57 , pp. 447-453
    • Li, X.1    Yu, H.Y.2


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