Abstract
The world of halophilic bacteria is quite diverse. We find representatives of three domains of life, archaea, bacteria and eukarya that are adapted to salt concentration upto saturation. The micro-organisms able to grow upto NaCl concentration (>300 g/l) are found all over the small subunit rRNA based tree of life. Their metabolic diversity is high as well encompassing oxygenic and anoxygenic phototrophs, aerobic heterotrophs, denitrifiers, sulfate reducers, fermenters and methanogens. The proteins of halophilic bacteria are magnificently engineered to function in a milieu containing 2–5 M salt. The proteins and encoding genes of halophiles represent a valuable repository and resource for reconstruction and visualizing processes of habitat selection and adaptive evolution. Search for new enzymes endowed with novel activities and enhanced stability continues to be desirable character for important commercial production. These poly extremophiles are excellent source of enzymes and metabolites possessing inherent ability to function in extreme conditions viz high salt, alkaline pH and facilitating catalysis for biotechnological application in food processing, industrial bioconversion and bioremediation. In brief, we have just begun to realize the great potential and true extent of diversity and suitable industrial applications possible from halophiles.
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References
Amoozegar MA, Fatemi ZA, Karbalaei-Heidari HR, Razavi MR (2007) Production of an extracellular alkaline metalloprotease from a newly isolated, moderately halophile, Salinivibrio sp. strain AF-2004. Microbiol Res 162:369–377
Amoozegar MA, Salehghamari E, Khajeh K, Kabiri M, Naddaf S (2008) Production of an extracellular thermohalophilic lipase from a moderately halophilic bacterium, Salinivibrio sp. strain SA-2. J Basic Microbiol 48:160–167
Arakawa T, Timasheff SN (1985) The stabilization of proteins by osmolytes. Biophys J 47:411–414
Aygan A, Arikan B (2008) A new haloalkaliphilic, thermostable endoglucanse from moderately halophilic Bacillus sp. C14 isolated from Van Soda Lake. Int J Agric Biol 10:369–374
Aygan A, Arikan B, Korkmas H, Dincer S, Colak O (2008) Highly thermostable and alkaline α- amylase from a halotolerant alkaliphilic Bacillus sp. AB68. Braz J Microbiol 39:547–553
Bakhtiar S, Estiveira RJ, Hatti-Kaul R (2005) Substrate specificity of alkaline protease from alkaliphilic feather-degrading Nesterenkonia sp. AL20. Enzyme Microb Technol 37:534–540
Balasubramanian S, Pal S, Bagchi B (2002) Dynamics of water molecules at the surface of an aqueous micelle: atomistic molecular dynamics simulation study of a complex system. Curr Sci 82:845–854
Bolobova AV, Simankova MV, Markovitch NA (1992) Cellulase complex of a new halophilic bacterium, Halocella Cellulolytica. Microbiology 61:557–562
Boutaiba S, Bhatnagar T, Hacene H, Mitchell DA, Baratti JC (2006) Preliminary characterization of a lipolytic activity from an extremely halophilic archaeon, Natronococcus sp. J Mol Catal B Enzyme 41:21–26
Britton KL, Baker PJ, Fisher M, Ruzheinikov S, Gilmour DJ, Bonete MJ et al (2006) Analysis of protein solvent interactions in glucose dehydrogenase from the extreme halophile Haloferax mediterranei. Proc Natl Acad Sci 103:4846–4851
Buchalo AS, Nevo E, Wasser SP, Volz PA (2000) Newly discovered halophilic fungi in the Dead Sea (Israel). In: Seckbach J (ed) Journey to diverse microbial worlds. Kluwer, Dordrecht, pp 241–252
Caton TM, Caton IR, Witte LR, Schneegurt MA (2009) Archaeal diversity at the great salt plains of Oklahoma described by cultivation and molecular analyses. Microb Ecol 58(3):519–528
Chakraborty S, Khopade A, Kokare C, Mahadika K, Chopade B (2009) Isolation and characterization of novel α-amylase from marine Streptomyces sp. D1. J Mol Catal B Enzyme 58:17–23
Chand S, Mishra P (2003) Research and application of microbial enzymes. India’s contribution. Adv Biochem Eng Biotechnol 85:95–124
Chattopadhyay MK, Kern R, Mistou MY, Dandekar AM, Uratsu SL, Richarme G (2004) The chemical chaperone proline relieves the thermosensitivity of a dnaK deletion mutant at 42°C. J Bacteriol 186:8149–8152
Cojoc R, Merciu S, Popescu G, Dumitru L, Kamekura M, Enache M (2009) Extracellular hydrolytic enzymes of halophilic bacteria isolated from a subterranean rock salt crystal. Rom Biotechnol Lett 14:4658–4664
Coronado MJ, Vargas C, Hofemeister J, Ventosa A, Nieto J (2000) Production and biochemical characterization of an α-amylase from the moderate halophile Halomonas meridian. FEMS Microbiol Lett 183:67–71
Dang H, Zhu H, Wang J, Li T (2009) Extracellular hydrolytic enzyme screening of culturable heterotrophic bacteria from deep-sea sediments of the Southern Okinawa Trough. World J Microbiol Biotechnol 25:71–79
Danson MJ, Hough DW (1997) The structural basis of protein halophilicity. Comp Biochem Physiol 117(3):307–312
DasSarma S, Arora P (2001) Halophiles. Encyclopedia of life sciences. Macmillan Press, London
DasSarma P, Coker JA, Huse V, DasSarma S (2010) Halophiles, industrial applications. In: Flickinger MC (ed) Encyclopedia of industrial biotechnology: bioprocess, bioseparation, and cell technology. Wiley, New York
Doukyu N, Ogino H (2010) Organic solvent-tolerant enzymes. Biochem Eng J 48:270–282
Dym O, Menarch M, Sussmann JL (1995) Structural features that stabilize halophilic malate dehydrogenase from an archaebacterium. Science 267:1344–1346
Elshahed MS, Najar FZ, Roe BA, Oren A, Dewers TA, Krumholz LR (2004) Survey of archaeal diversity reveals an abundance of halophilic archaea in a low-salt, sulfide- and sulfur-rich spring. Appl Environ Microbiol 70(4):2230–2239
Empadinhas N, da Costa MS (2008) Osmoadaptation mechanisms in prokaryotes: distribution of compatible solutes. Int Microbiol 11:151–161
Enache M, Kamekura M (2010) The halophilic enzyme and their economical values. Rom J Biochem 47(1):47–59
Essghaier B, Fardeau ML, Cayol JL, Hajlaoui MR, Boudabous A, Jijakli H, Sadfi-Zouaoui N (2009) Biological control of grey mould in strawberry fruits by halophilic bacteria. J Appl Microbiol 106:83–846
Fukushima T, Mizuki T, Echigo A, Inoue A, Usami R (2005) Organic solvent tolerance of halophilic α-amylase from a haloarchaeon, Haloarcula sp. strain S-1. Extremophiles 9:85–89
García MT, Mellado E, Ostos JC, Ventosa A (2004) Halomonas organivorans sp. nov., a moderate halophile able to degrade aromatic compounds. Int J Syst Evol Microbiol 54:1723–1728
Giridhar PV, Chandra TS (2010) Production of novel haloalkali- thermostable xylanase by a newly isolated moderately halophilic and alkali tolerant Gracibacillus sp. TSCPVG. Process Biochem 45:1730–1737
Govender L, Naidoo L, Setati ME (2009) Isolation of hydrolase producing bacteria from Sua pan solar salterns and the production of endo-1,4-β-xylanase from a newly isolated haloalkaliphilic Nesterenkonia sp. Afr J Biotechnol 8:5458–5466
Grant WD, Kamekura M, Mc Genity TJ, Ventosa A (2001) Class III. Halobacteria class. In: Boone DR, Castenholz RW (eds) Bergery’s manual of systematic bacteriology. Springer, New York, pp 294–334
Gunde- Cimerman NS, Zalar P, de Hoog GS, Plemenitas A (2000) Hypersaline waters in salterns-natural ecological niches for black yeasts. FEMS Microbiol Ecol 32(3):235–240
Guo B, Chen XL, Sun CY, Zhou BC, Zhang YZ (2009) Gene cloning, expression and characterization of a new cold-active and salt-tolerant endo-β-xylanase from marine Glaciecola mesophila KMM 241. Appl Microbiol Biotechnol 84:1107–1115
Guzmán MN, Vargas VA, Antezana H, Svoboda M (2008) Lipolytic enzyme production by halophilic/halotolerant microorganisms isolated from Laguna Verde, Bolivia. Revista Boliviana De Química 25(1):14–23
Hanelt I, Muller V (2013) Molecular mechanisms of adaptation of the moderately halophilic bacterium Halobacillus halophilus to its environment. Life 3:234–243
Hatori Y, Sato M, Orishimo K, Yatsunami R, Endo K, Fukui T, Nakamura S (2006) Characterization of recombinant family 18 chitinase from extremely halophilic archaeon Halobacterium salinarum strain NRC-1. Chitin Chitosan Res 12:201
Hiraga K, Nishikata Y, Namwong S, Tanasupawat S, Takada K, Oda K (2005) Purification and characterization of serine proteinase from a halophilic bacterium, Filobacillus sp.RF2-5. Biosci Biotechnol Biochem 69:38–44
Jaeger KE, Holliger P (2010) Chemical biotechnology a marriage of convenience and necessity. Curr Opin Biotechnol 21:711–712
Kamekura M, Onishi H (1976) Effect of magnesium and some nutrients on the growth and nuclease formation of a moderately halophile Micrococcus varians var. halophilus. Can J Microbiol 22:1567–1576
Kamekura M, Onishi H (1983) Inactivation of nuclease H of the moderate halophilic Micrococcus varians sp. halophiles during cultivation in the presence of salting in type salts. Can J Microbiol 29:46–51
Kamekura M, Seno Y (1990) A halophilic extracellular protease from a halophilic archaebacterium strain 172P1. Biochem Cell Biol 68:352–359
Kamekura M, Seno Y, Holmes ML, Dyall-Smith ML (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
Karan R, Singh S, Kapoor S, Khare S (2011) A novel organic solvent tolerant protease from a newly isolated Geomicrobium sp. EMB2 (MTCC 10310): production optimization by response surface methodology. New Biotechnol 28:136–145
Karbalaei-Heidari HR, Amoozegar MA, Hajighasemi M, Ziaee AA, Ventosa A (2009) Production, optimization and purification of a novel extracellular protease from the moderately halophilic bacterium Halobacillus karajensis. J Ind Microbiol Biotechnol 36:21–27
Khunt M, Pandhi N, Rana A (2011) Amylase from moderate halophiles isolated from wild ass excreta. Int J Pharm Biol Sci 1:586–592
Kobayashi T, Kanai H, Aono R, Horikoshi K, Kudo T (1994) Cloning, expression and nucleotide sequencing of α- amylase gene from the haloalkaliphilic archaeon Natronococcus sp. strain Ah-36. J Bacteriol 176:5131–5134
Kolp S, Pietsch M, Galinski EA, Gutschow M (2006) Compatible solutes as protectants for zymogens against proteolysis. Biochim Biophys Acta 1764:1234–1242
Kurz M (2008) Compatible solute influence on nucleic acids: many questions but few answers. Saline Syst 4:6
Lamosa P, Turner DL, Ventura R, Maycock C, Santos H (2003) Protein stabilization by compatible solutes. Effect of diglycerol phosphate on the dynamics of Desulfovibrio gigas rubredoxin studied by NMR. Eur J Biochem 270:4606–4614
Li AN, Li DC (2009) Cloning, expression and characterization of the serine protease gene from Chaetomium thermophilum. J Appl Microbiol 106:369–380
Lin QS, Chen SH, Hu MY, Rizwan-ul-Haq M, Yang L, Li H (2011) Biodegradation of cypermethrin by a newly isolated actinomycetes HU-S-01 from wastewater sludge. Int J Environ Sci Technol 8(1):45–56
Margesin R, Schinner F (2001) Potential of halotolerant and halophilic microorganisms for biotechnology. Extremophiles 5:73–83
Maturrano L, Valens-Vadell M, Roselló-Mora R, Antón J (2006) Salicola marasensis gen. nov., sp. nov., an extremely halophilic bacterium isolated from the Maras solar salterns in Perú. Int J Syst Evol Microbiol 56:1685–1691
Mevarech M, Frolow F, Gloss LM (2000) Halophilic enzymes: proteins with a grain of salt. Biophys Chem 86:155–164
Mohapatra BR, Banerjee UC, Bapuji M (1998) Characterization of a fungal amylase from Mucor sp. associated with the marine sponge Spirastella sp. J Biotechnol 60:113–117
Moreno ML, García MT, Ventosa A, Mellado E (2009) Characterization of Salicola sp. IC10, a lipase- and protease-producing extreme halophile. FEMS Microbiol Ecol 68:59–71
Moreno MDL, Dolores P, María TG, Encarnación M (2013) Halophilic bacteria as a source of novel hydrolytic enzymes. Life 3:38–51
Oh D, Porter K, Russ B, Burns D, Dyall-Smith M (2009) Diversity of Haloquadratum and other haloarchaea in three, geographically distant, Australian saltern crystallizer ponds. Extremophiles 14(2):161–169
Onishi H, Hidaka O (1978) Purification and properties of amylase produced by a moderately halophilic Acinetobacter sp. Can J Microbiol 24:1017–1023
Onishi H, 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 L, Kobayashi T, Kamekura M (1983) Halophilic nuclease of a moderately halophilic Bacillus sp.: production, purification and characterization. Appl Environ Microbiol 45:24–30
Oren A (2002) Diversity of halophilic microorganisms: environments, phylogeny, physiology, and applications. J Ind Microbiol Biotechnol 28:58–63
Oren A (2010) Industrial and environmental applications of halophilic microorganisms. Environ Technol 31:825–834
Oren A, Heldal M, Norland S (1997) X-ray microanalysis of intracellular ions in the anaerobic halophilic eubacterium Haloanaerobium praevalens. Can J Microbiol 43:588–592
Ovreas L, Bourne D, Sandaa RA, Casamayor EO, Benlloch S, Goddard V (2003) Response of bacterial and viral communities to nutrient manipulations in sea water mesocosms. Aquat Microb Ecol 31:109–121
Pandey A, Nigam P, Soccol CR, Soccol VT, Singh D, Mohan R (2000) Advances in microbial amylases. Biotechnol Appl Biochem 31:135–152
Pandit AS, Joshi MN, Bhargava P, Ayachit GN, Shaikh IM, Saiyed ZM, Saxena AK, Bagatharia SB (2014) Metagenomes from the saline desert of Kutch. Genome A 2(3):1
Park JH, Ha HJ, Lee WK, Généreux-Vincent T, Kazlauskas RJ (2009) Molecular basis for the stereoselective ammoniolysis of N-alkyl aziridine-2-carboxylates catalyzed by Candida antarctica lipase B. Chembiochem 10:2213–2222
Patel S, Jain N, Madamwar D (1993) Production of α-amylase from Halobacterium halobium. World J Microbiol Biotechnol 9:25–28
Perez-Pomares F, Bautista V, Ferrer J, Pire C, Marhuenda-Egea FC, Bonete MJ (2003) α-Amylase activity from the halophilic archaeon Haloferax mediterranei. Extremophiles 7:299–306
Pikuta EV, Hoover RB, Tang J (2007) Microbial extremophiles at the limits of life. Crit Rev Microbiol 33:183–209
Prakash B, Vidyasagar M, Madhukumar MS, Muralikrishna G, Sreeramulu K (2009) Production, purification, and characterization of two extremely halotolerant, thermostable, and alkali-stable α-amylase from Chromohalobacter sp. TVSP 101. Process Biochem 44:210–215
Raj E, Suman CE (2010) Purification and characterization of a new hyperthermostable, allosamidin-insensitive and denaturation-resistant chitinase from the hyper thermophilic archaeon Thermococcus chitonophagus. Extremophiles 7:43–53
Ratnakar D (2013) Use of halophile physiology and adaptations in various industrial applications. Res J Biotechnol 8(2):1–3
Roberts MF (2005) Organic compatible solutes of halotolerant and halophilic microorganisms. Saline Syst 1:5
Roessler M, Muller V (2001) Chloride dependence of glycine betaine transport in Halobacillus halophilus. FEBS Lett 489:125–128
Rohban R, Amoozegar MA, Ventosa A (2009) Screening and isolation of halophilic bacteria producing extracellular hydrolyses from Howz Soltan Lake, Iran. J Ind Microbiol Biotechnol 36:333–340
Rothschild LJ, Mancinelli RL (2001) Life in extreme environments. Nature 409:1092–1101
Ryu K, Kim J, Dordick JS (1994) Catalytic properties and potential of an extracellular protease from an extreme halophile. Enzyme Microb Technol 16:266–275
Sanchez-Porro C, Martin S, Mellado E, Ventosa A (2003) Diversity of moderately halophilic bacteria producing extracellular hydrolytic enzymes. J Appl Microbiol 94:295–300
Satyanarayana T, Raghukumar C, Shivaji S (2005) Extremophilic microbes: diversity and perspectives. Curr Sci 89(1):78–90
Shivanand P, Jayaraman G (2009) Production of extracellular protease from halotolerant bacterium, Bacillus aquimaris strain VITP4 isolated from Kumta coast. Process Biochem 44:1088–1094
Siglioccolo A, Paiardini A, Piscitelli M, Pascarella S (2011) Structural adaptation of extreme halophilic proteins through decrease of conserved hydrophobic contact surface. BMC Struct Biol 11:1–12
Sinha R, Khare SK (2014) Effect of organic solvents on the structure and activity of moderately halophilic Bacillus sp. EMB9 protease. Extremophiles. doi:10.1007/s00792-014-0683-4
Sinsuwan S, Rodtong S, Yongsawatdigul J (2010) A NaCl-stable serine proteinase from Virgibacillus sp. SK33 isolated from Thai fish sauce. Food Chem 119:573–579
Sorokin DY, Tindall BJ (2006) The status of the genus name Halovibrio fendrich 1989 and the identity of the strains Pseudomonas halophila DSM 3050 and Halomonas variabilis DSM 3051. Int J Syst Evol Microbiol 56:487–489
Tan TC, Mijts BN, Swaminathan K, Patel BKC, Divine C (2008) Crystal structure of the polyextremophilic alpha-amylase AmyB from Halothermothrix orenii: details of a productive enzyme-substrate complex and an N domain with a role in binding raw starch. J Mol Biol 378:852–870
Upasani V, Desai S (1990) Sambhar Salt Lake: chemical composition of the brines and studies on haloalkaliphilic archaebacteria. Arch Microbiol 154:589–593
Ventosa A, Marquez MC, Ruiz-Berraquero F, Kocur M (1990) Salinicoccus roseus gen. nov., sp. nov., a new moderately halophilic Gram-positive coccus. Syst Appl Microbiol 13:29–33
Ventosa A, Nieto JJ, Oren A (1998) Biology of moderately halophilic aerobic bacteria. Microbiol Mol Biol Rev 62:504–544
Vidyasagar M, Prakash S, Mahajan V, Shouche YS, Sreeramulu K (2009) Purification and characterization of an extreme halothermophilic protease from a halophilic bacterium Chromohalobacter sp. TVSP101. Braz J Microbiol 40:12–19
Voget S, Steele HL, Streit WR (2006) Characterization of a metagenome-derived halotolerant cellulase. J Biotechnol 126:26–36
Wang CY, Hsieh YR, Ng CC, Chan H, Lin HT, Tzeng WS, Shyu YT (2009) Purification and characterization of a novel halostable cellulase from Salinivibrio sp. strain NTU05. Enzyme Microb Technol 44:373–379
Warren JC, Stowring L, Morales MF (1966) The effect of structure-disrupting ions on the activity of myosin and other enzymes. J Biol Chem 241:309–316
Zalar P, de Hoog GS, Gunde- Cimerman NS (1999) Ecology of halotolerant dothideaceous black yeasts. Stud Mycol 43:38–48
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Patel, S., Saraf, M. (2015). Perspectives and Application of Halophilic Enzymes. In: Maheshwari, D., Saraf, M. (eds) Halophiles. Sustainable Development and Biodiversity, vol 6. Springer, Cham. https://doi.org/10.1007/978-3-319-14595-2_15
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