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Keywords
- Extracellular Enzyme
- Halophilic Bacterium
- Halophilic Archaea
- Halophilic Microorganism
- Halobacterium Salinarum
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References
Amann, R.I., Ludwig, W. and Schleifer, K.H. (1995) Phylogenetic identification and in situ detection of individual microbial cells without cultivation. Microbiol. Rev. 59, 143–169.
Amoozegar, M.A., Malekzadeh, F. and Malik K.A. (2003a) Production of amylase by newly isolated moderate halophile, Halobacillus sp. strain MA-2. J. Microbiol. Meth. 52, 353–359.
Amoozegar, M.A., Malekzadeh, F., Malik K.A., Schumann, P. and Spröer, C. (2003b) Halobacillus karajensis sp. nov., a novel moderate halophile. Int. J. Syst. Evol. Microbiol. 53, 1059–1063.
Antón, J., Oren, A., Benlloch, S., Rodríguez-Valera, F., Amann, R.I. and Rosselló-Mora, R. (2002) Salinibacter ruber gen. nov., sp. nov., a novel, extremely halophilic member of the Bacteria from saltern crystallizer ponds. Int. J. Syst. Evol. Microbiol. 52, 485–491.
Béjà, O., Suzuki, M.T., Koonin, E.V., Aravind, L., Hadd, A., Nguyen, L.P., Villacorta, R., Amjadi, M., Garrigues, C., Jovanovich, S.B., Feldman, R.A. and Delong, E.F. (2000) Construction and analysis of bacterial artificial chromosome libraries from a marine microbial assemblage. Environ. Microbiol. 2, 516–529.
Bieger, B., Essen, L.O. and Oesterhelt, D. (2003) Crystal structure of halophilic dodecin: a novel, dodecameric flavin binding protein from Halobacterium salinarum. Structure 11, 375–385.
Chaga, G. and Porath, J. (1993) Isolation and purification of amyloglucosidase from Halobacterium sodomense. Biomed. Chromat. 7, 256–261.
Christian, J.H.B. and Waltho, J.A. (1962) Solute concentrations within cells of halophilic and non-halophilic bacteria. Biochim. Biophys. Acta 65, 506–508.
Coronado, M., Vargas, C., Hofemeister, J., Ventosa, A. and Nieto, J.J. (2000a) Production and biochemical characterization of an α-amylase from the moderate halophile Halomonas meridiana. FEMS Microbiol. Lett. 183, 67–71.
Coronado, M.J., Vargas, C., Mellado, E., Tegos, G., Drainas, C., Nieto, J.J. and Ventosa, A. (2000b) The α-amylase gene amyH of the moderate halophile Halomonas meridiana: cloning and molecular characterization. Microbiology 146, 861–868.
Danson, M.J. and Hough, D.W. (1997) The structural basis of protein halophilicity. Comp. Biochem. Physiol. 117A, 307–312.
Dym, O., Mevarech, M. and Sussman, J.L. (1995) Structural features that stabilize halophilic malate dehydrogenase from an archaebacterium. Science 267, 1344–1346.
Frillingos, S., Linden, A., Niehaus, F., Vargas, C., Nieto, J.J., Ventosa, A., Antranikian, G. and Drainas, C. (2000) Cloning and expression of α-amylase from the hyperthermophilic archaeon Pyrococcus woesei in the moderately halophilic bacteria Halomonas elongata. J. Appl. Microbiol. 88, 495–503.
Frolow, F., Harel, M., Sussman, J.L., Mevarech, M. and Shoham, M. (1996) Insights into protein adaptation to a saturated salt environment from the crystal structure of a halophilic 2Fe-2S ferredoxin. Nature Struct. Biol. 3, 452–458.
Fukuchi, S., Yoshimune, K., Wakayama, M., Moriguchi, M. and Nishikawa, K. (2003) Unique amino acid composition of proteins in halophilic bacteria. J. Mol. Biol. 327, 347–357.
Giménez, M.I., Studdert, C.A., Sánchez, J.J. and De Castro, R.E. (2000) Extracellular protease of Natrialba magadii: purification and biochemical characterization. Extremophiles 4, 181–188.
Ginzburg, M., Sachs, L. and Ginzburg, B.Z. (1970) Ion metabolim in a halobacterium. I. Influence of age of culture on intracellular concentrations. J. Gen. Physiol. 55, 187–207.
Gonzalez, C. and Gutierrez, C. (1970) Presence of lipase among species of extremely halophilic bacteria. Can. J. Microbiol. 16, 1165–1166.
Good, W.A. and Hartman, P.A. (1970) Properties of the amylase from Halobacterium halobium. J. Bacteriol. 104, 601–603.
Grant, W.D., Kamekura, M., McGenity, T.J. and Ventosa, A. (2001) Class III. Halobacteria class. nov, In: D.R. Boone, R.W. Castenholz and G.M. Garrity (eds.), Bergey’s Manual of Systematic Bacteriology, 2nd ed. Springer-Verlag, New York, pp. 294–299.
Grant, S., Sorokin, D.Y., Grant W.D., Jones, B.E. and Heaphy, S. (2004) A phylogenetic analysis of Wadi el Natrum soda lake cellulase enrichment cultures and identification of cellulase genes from these cultures. Extremophiles 8, 421–429.
Healy, F.G., Ray, R.M., Aldrich, H.C., Wilkie, A.C., Ingram, L.O. and Shanmugam K.T. (1995) Direct isolation of functional genes encoding cellulases from the microbial consortia in a thermophilic, anaerobic digester maintained on lignocellulose. Appl. Microbiol. Biotechnol. 43, 667–674.
Henne, A., Schmitz, R.A., Bömeke, M., Gottschalk, G. and Daniel, R. (2000) Screening of environmental DNA libraries for the presence of genes conferring lipolytic activity on Escherichia coli. Appl. Environ. Microbiol. 66, 3113–3116.
Holmes, M.L., Scopes, R.K., Moritz, R.L., Simpson, R.J., Englert, C., Pfeifer, F. and Dyall-Smith, M.L.(1997) Purification and analysis of an extremely halophilic β-galactosidase from Haloferax alicantei. Biochim. Biophys. Acta 1337, 276–286.
Horikoshi, K. and Grant, W.D. (eds.) (1998) Extremophiles: Microbial Life in Extreme Environments. John Wiley & Sons, New York.
Izotova, L.S., Strongin, A.Y., Chekulaeva, L.N., Ostoslavskaya, V.I., Lyublinskaya, L.A., Timokhina, E.A. and Stepanov, V.M. (1983) Purification and properties of serine protease from Halobacterium halobium. J. Bacteriol. 155, 826–830.
Kamekura, M. (1986) Production and function of enzymes of eubacterial halophiles. FEMS Microbiol. Rev. 39, 145–150.
Kamekura, M. (1995) Halophilic proteases from halophilic archaea, In: F.T. Robb and A.R. Place (eds.), Archaea. A Laboratory Manual. Cold Spring Harbor Laboratory Press, New York, pp. 89–93.
Kamekura, M. (1998) Diversity of extremely halophilic bacteria. Extremophiles 2, 289–295.
Kamekura, M. and Onishi, H. (1974a) Halophilic nuclease from a moderately halophilic Micrococcus varians. J. Bacteriol. 119, 339–344.
Kamekura, M. and Onishi, H. (1974b) Protease formation by a moderately halophilic Bacillus strain. Appl. Microbiol. 27, 809–810.
Kamekura, M. and Onishi, H. (1976) Effect of magnesium and some nutrients on the growth and nuclease formation of a moderate halophile, Micrococcus varians var. halophilus. Can. J. Microbiol. 22, 1567–1576.
Kamekura, M. and Onishi, H. (1978a) Propierties of the halophilic nuclease of a moderate halophile, Micrococcus varians subsp. halophilus. J. Bacteriol. 133, 59–65.
Kamekura, M. and Onishi, H. (1978b) Flocculation and adsorption of enzymes during growth of a moderate halophile, Micrococcus varians var. halophilus. Can. J. Microbiol. 24, 703–709.
Kamekura, M. and Onishi, H. (1979) A medium for commercial production of the halophilic Micrococcus nuclease. Can. J. Microbiol. 25, 1113–1116.
Kamekura, M. and Onishi, H. (1983) Inactivation of nuclease H of the moderate halophile Micrococcus varians ssp. halophilus during cultivation in the presence of salting-in-type salts. Can. J. Microbiol. 29, 46–51.
Kamekura, M. and Seno, Y. (1990) A halophilic extracellular protease from a halophilic archaebacterium strain 172 P1. Biochem. Cell. Biol. 68, 352–359.
Kamekura, M., Hamakawa, T. and Onishi, H. (1982) Application of halophilic nuclease H of Micrococcus varians subsp. halophilus to commercial production of flavoring agent 5′-GMP. Appl. Environ. Microbiol. 44, 994–995.
Kamekura, M., Seno, Y., Holmes, M.L. and Dyall-Smith, M. (1992) Molecular cloning and sequencing of the gene for a halophilic alkaline serine protease (halolysin) from an unidentified halophilic archaea strain (172P1) and expression of the gene in Haloferax volcanii. J. Bacteriol. 174, 736–742.
Kamekura, M., Seno, Y. and Dyall-Smith, M. (1996) Halolysin R4, a serine proteinase from the halophilic archaeon Haloferax mediterranei; gene cloning, expression and estructural studies. Biochim. Biophys. Acta 1294, 159–167.
Khire, J.M. (1994) Production of moderately halophilic amylase by newly isolated Micrococcus sp. 4 from a salt pan. Lett. Appl. Microbiol. 19, 210–212.
Knietsch, A., Waschkowitz, T., Bowien, S., Henne, A. and Daniel, R. (2003) Construction and screening of metagenomic libraries derived from enrichment cultures: generation of a gene bank for genes conferring alcohol oxidoreductase activity on Escherichia coli. Appl. Environ. Microbiol. 69, 1408–1416.
Kobayashi, T., Kamekura, M., Kanlayakrit, W. and Onishi, H. (1986) Production, purification, and characterization of an amylase from the moderate halophile, Micrococcus varians subspecies halophilus. Microbios 46, 165–177.
Kobayashi, T., Kanai, H., Hayashi, T., Akiba, T., Akaboshi, R. and Horikoshi, K. (1992) Haloalkaliphilic maltotriose-forming α-amylase from the archaebacterium Natronococcus sp. strain Ah-36. J. Bacteriol. 174, 3439–3444.
Kobayashi, T., Kanai, H., Aono, R., Horikoshi, K. and Kudo, T. (1994) Cloning, expression, and nucleotide sequence of the α-amylase gene from the haloalkaliphilic archaeon Natronococcus sp. strain Ah-36. J. Bacteriol. 176, 5131–5134.
Kushner, D.J. (1968) Halophilic bacteria. Adv. Appl. Microbiol. 10, 73–99.
Li, N., Patel, B.K., Mijts, B.N. and Swaminathan, K. (2002) Crystallization of an alpha-amylase, amyA, from the thermophilic halophile Halothermothrix orenii. Acta Crystallogr. D. Biol. Crystallogr. 58, 2125–2126.
Madern, D., Ebel, C. and Zaccai, G. (2000) Halophilic adaptation of enzymes. Extremophiles 4, 91–98.
Madigan, M.T. and Oren, A. (1999) Thermophilic and halophilic extremophiles. Curr. Opin. Microbiol 2, 265–269.
Majernik, A., Gottschalk, G. and Daniel, R. (2001) Screening of environmental DNA libraries for the presence of genes conferring Na+ (Li+)/H+ antiporter activity on Escherichia coli: characterization of the recovered genes and the corresponding gene products. J. Bacteriol. 183, 6645–6653.
Martín, S., Márquez, M.C., Sánchez-Porro, C., Mellado, E., Arahal, D.R. and Ventosa, A. (2003) Marinobacter lipolyticus sp. nov., a novel moderate halophile with lipolytic activity. Int. J. Syst. Evol. Microbiol. 53, 1383–1387.
Mellado, E. and Ventosa, A. (2003) Biotechnological potential of moderately and extremely halophilic microorganisms, In: J.L. Barredo (ed.), Microorganisms for Health Care, Food and Enzyme Production. Research Signpost, Kerala, pp. 233–256.
Mellado, E., Sánchez-Porro, C., Martín, S. and Ventosa, A. (2004) Extracellular hydrolytic enzymes produced by moderately halophilic bacteria, In: A. Ventosa (ed.), Halophilic Microorganisms. Springer-Verlag, Berlin, pp. 285–295.
Mevarech, M., Frolow, F. and Gloss, L.M. (2000) Halophilic enzymes: proteins with a grain of salt. Biophys. Chem. 86, 155–164.
Mijts, B.N. and Patel, B.K. (2002) Cloning, sequencing and expression of an alpha-amylase gene, amyA, from the thermophilic halophile Halothermothrix orenii and purification and biochemical characterization of the recombinant enzyme. Microbiology 148, 2343–2349.
Nieto, J.J. and Vargas, C. (2002) Synthesis of osmoprotectants by moderately halophilic bacteria: Genetic and applied aspects, In: S.G. Pandalai (ed.), Recent Research Developments in Microbiology, Vol. 6. Research Signpost, Trivandrum, pp. 403–418.
Norberg, P. and Hofsten, B.V. (1969) Proteolytic enzymes from extremely halophilic bacteria. J. Gen. Microbiol. 55, 251–256.
Onishi, H. (1972) Halophilic amylase from a moderately halophilic Micrococcus. J. Bacteriol. 109, 570–574.
Onishi, H. and Hidaka, O. (1978) Purification and properties of amylase produced by a moderate halophilic Acinetobacter sp. Can. J. Microbiol. 24, 1017–1023.
Onishi, H and Kamekura, M. (1972) Micrococcus halobius sp. n. Int. J. Syst. Bacteriol. 22, 233–236.
Onishi, H. and Sonoda, K. (1979) Purification and some properties of an extracellular amylase from a moderate halophile, Micrococcus halobius. Appl. Environ. Microbiol. 38, 616–620.
Onishi, H., Mori, T., Takeuchi, S., Tani, K., Kobayashi, T. and Kamekura, M. (1983) Halophilic nuclease of a moderately halophilic Bacillus sp.: production, purification and characterization. Appl. Environ. Microbiol. 45, 24–30.
Onishi, H., Kobayashi, T. and Kamekura, M. (1984) Purification and some properties of an extracellular halophilic 5′-nucleotidase from a moderate halophile, Micrococcus varians subsp. halophilus. FEMS Microbiol. Lett. 24, 303–306.
Onishi, H., Kamekura, M., Yokoi, H. and Kobayashi, T. (1988) Production of 5′ nucleotide by using halophilic nuclease H preferentially adsorbed on flocculated cells of the halophile Micrococcus varians subsp. halophilus. Appl. Environ. Microbiol. 54, 2632–2635.
Onishi, H., Yokoi, H. and Kamekura, M. (1991) An application of a bioreactor with flocculated cells of halophilic Micrococcus varians subsp. halophilus which preferentially adsorbed halophilic nuclease H to 5′-nucleotide production, In: F. Rodriguez-Valera (ed.), General and Applied Aspects of Halophilic Microorganisms. Plenum Press, New York, pp. 341–349.
Oren, A. (1983) A thermophilic amyloglucosidase from Halobacterium sodomense, a halophilic bacterium from the Dead Sea. Cur. Microbiol. 8, 225–230.
Oren, A. (2002) Diversity of halophilic microorganisms: environments, phylogeny, physiology, and applications. J. Ind. Microbiol. Biotechnol. 28, 56–63.
Patenge, N., Haase, A., Bolhuis, H. and Oesterhelt, D. (2000) The gene for a halophilic beta-galactosidase (bgaH) of Haloferax alicantei as a reporter gene for promoter analyses in Halobacterium salinarum. Mol. Microbiol. 36, 105–113.
Pérez-Pomares, F., Bautista, V., Ferrer, J., Pire, C., Marhuenda-Egea, F.C. and Bonete M.J. (2003) α-amylase activity from the halophilic archaeon Haloferax mediterranei. Extremophiles 7, 299–306.
Pieper, U., Kapadia, G., Mevarech, M. and Herzberg, O. (1998) Structural features of halophilicity derived from the crystal structure of dihydrofolate reductase from the Dead Sea halophilic archaeon, Haloferax volcanii. Structure 15, 75–88.
Rees, H.C., Grant, S., Jones, B., Grant, W.D. and Heaphy, S. (2003a) Detecting cellulase and esterase enzyme activities encoded by novel genes present in environmental DNA libraries. Extremophiles 7, 415–421.
Rees, H.C., Jones, B.E., Grant, W.D. and Heaphy, S. (2003b) Diversity of Kenyan soda lake alkaliphiles assessed by molecular methods. Extremophiles 8, 63–71.
Richard, S.B., Madern, D., Garcin, E. and Zaccai, G. (2000) Halophilic adaptation: novel solvent protein interactions observed in the 2.9 and 2.6 Å resolution structures of the wild type and a mutant of malate dehydrogenase from Haloarcula marismortui. Biochemistry 39, 992–1000.
Richardson, T.H., Tan, X., Frey, G., Callen, W., Cabell, M., Lam, D., Macomber, J., Short, J.M., Robertson, D.E. and Miller, C. (2002) A novel, high performance enzyme for starch liquefaction. Discovery and optimization of a low-pH, termostable alpha-amylase. J. Biol. Chem. 277, 26501–26507
Ryu, K., Kim, J. and Dordick, J.S. (1994) Catalytic properties and potential of an extracellular protease from an extreme halophile. Enzyme Microb. Technol. 16, 266–275.
Sánchez-Porro, C., Martín, S., Mellado, E. and Ventosa, A. (2003a) Diversity of moderately halophilic bacteria producing extracellular hydrolytic enzymes. J. Appl. Microbiol. 94, 295–300.
Sánchez-Porro, C., Mellado, E., Bertoldo, C., Antranikian, G. and Ventosa, A. (2003b) Screening and characterization of the protease CP1 produced by the moderately halophilic bacterium Pseudoalteromonas sp. strain CP76. Extremophiles 7, 221–228.
Sánchez-Porro, C., Martín, S., Mellado, E. and Ventosa, A. (2004) Extracellular enzymes produced by halophilic archaea and bacteria, In: M.M. Watanabe, K. Suzuki and T. Seki (eds.), Innovative Roles of Biological Resource Centers. World Federation for Culture Collections, Tokyo, pp. 123–129.
Stackebrandt, E., Koch, C., Gvozdiak, O. and Schumann, P. (1995) Taxonomic dissection of the genus Micrococcus: Kocuria gen. nov., Nesterenkonia gen. nov., Kitococcus gen. nov., Dermacoccus gen. nov., and Micrococcus Cohn 1872 gen. emend. Int. J. Syst. Bacteriol. 45, 682–692.
Stepanov, V.M., Rudenskaya, G.N., Revina, L.P., Gryaznova, Y.B., Lysogorskaya, E.N., Filippova, I.Yu. and Ivanova, I.I. (1992) A serine proteinase of an archaebacterium, Halobacterium mediterranei. A homologue of eubacterial subtilisins. Biochem. J. 285, 281–286.
Streit, W.R. and Schmitz, R.A. (2004) Metagenomics-the key to the uncultured microbes. Curr. Opin. Microbiol. 7, 492–498.
Studdert, C., De Castro, R.E., Seitz, K.H. and Sánchez, J.J. (1997) Detection and preliminary characterization of extracellular proteolytic activities of the haloalkaliphilic archaeon Natronococcus occultus. Arch. Microbiol. 168, 532–535.
Studdert, C.A., Herrera Seitz, M.K., Plasencia Gil, M.I., Sánchez, J.J. and De Castro R.E. (2001) Purification and biochemical characterization of the haloalkaliphilic archaeon Natronoccocus occultus extracellular serine protease. J. Basic Microbiol. 41, 375–383.
Tan, T.C., Yien, Y.Y., Patel, B.K., Mijts, B.N. and Swaminathan, K. (2003) Crystallization of a novel alphaamylase, AmyB, from the thermophilic halophile Halothermothrix orenii. Acta. Crystallogr. D. Biol. Crystallogr. 59, 2257–2258.
Van Qua, D, Simidu, U. and Taga, N. (1981) Purification and some properties of halophilic protease produced by a moderately halophilic marine Pseudomonas sp. Can. J. Microbiol. 27, 505–510.
Ventosa, A., García, M.T., Kamekura, M., Onishi, H. and Ruíz-Berraquero, F. (1989) Bacillus halophilus sp. nov., a moderately halophilic Bacillus species. System. Appl. Microbiol. 12, 162–166.
Ventosa, A., Nieto, J.J. and Oren, A. (1998) Biology of moderately halophilic aerobic bacteria. Microbiol. Mol. Biol. Rev. 62, 504–544.
Wainø, M. and Ingvorsen, K. (2003) Production of β-xylanase and β-xylosidase by the extremely halophilic archaeon Halorhabdus utahensis. Extremophiles 7, 87–93.
Yamada, Y., Fujiwara, T., Sato, T., Igarashi, N. and Tanaka, N. (2002) The 2.0 Å crystal structure of catalaseperoxidase from Haloarcula marismortui. Nat. Struct. Biol. 9, 691–695.
Yu, T.X. (1991) Protease of haloalkaliphiles, In: K. Horikoshi and W.D. Grant (eds.) Superbugs. Microorganisms in extreme environments. Springer-Verlag, Tokyo, pp. 76–83.
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Ventosa, A., Sánchez-Porro, C., Martín, S., Mellado, E. (2005). Halophilic Archaea and Bacteria as a Source of Extracellular Hydrolytic Enzymes. In: Gunde-Cimerman, N., Oren, A., Plemenitaš, A. (eds) Adaptation to Life at High Salt Concentrations in Archaea, Bacteria, and Eukarya. Cellular Origin, Life in Extreme Habitats and Astrobiology, vol 9. Springer, Dordrecht. https://doi.org/10.1007/1-4020-3633-7_23
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