Acta Scientific Microbiology (ASMI) (ISSN: 2581-3226)

Review Article Volume 3 Issue 1

The Extremes of Life and Extremozymes: Diversity and Perspectives

Jagdish Parihar and Ashima Bagaria*

Department of Physics, Manipal University Jaipur, Rajasthan, India

*Corresponding Author: Ashima Bagaria, Department of Physics, Manipal University Jaipur, Rajasthan, India.

Received: November 12, 2019; Published: December 23, 2019

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Abstract

   In mid 60’s and 70’s the discovery of Thermus aquaticus from Yellowstone National park in USA which could survive at extremely high temperatures of 80°C, opened gates towards exploration of extremophiles that emerged as a new field of microbiology. The microorganisms that can thrive at extreme environmental conditions where normal organisms fail to sustain are known as extremophiles. These microorganisms are found mainly in hot water springs, deep ocean vents, volcano pits, deep ice zones, deserts, saline lakes, mines, rocks beds and radiation zones etc. Since last two decades, the research data on extremophiles has increased exponentially as the enzymes extracted from the extremophilic microorganisms have shown potency in various industries like paper and pulp, leather, detergent, diary textiles, food and beverages, pharma, medicines and biotech industries. The current review encapsulates the knowledge about various extremophiles and their potential therapeutic and biotechnological applications.

Keywords: Extremophiles; Extremozymes; Adaptations and Industrial Applications

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References

  1. McClure RS., et al. “Species-specific transcriptomic network inference of interspecies interactions”. The ISME Journal8 (2018): 2011.
  2. Koonin EV and Martin W. “On the origin of genomes and cells within inorganic compartments”. TRENDS in Genetics12 (2005): 647-654.
  3. Rothschild LJ and Mancinelli RL. “Life in extreme environments”. Nature6823 (2001):1092.
  4. Van Den Burg B. “Extremophiles as a source for novel enzymes”. Current Opinion in Microbiology3 (2003): 213-218.
  5. Azlina IN and Norazila Y. “Thermostable alkaline serine protease from thermophilic Bacillus species”. International Research Journal of Biological Sciences 2 (2013): 29-33.
  6. Bekler FM. “Isolation and identification of a novel thermo-alkalophilic Anoxybacillus sp”. Strain KB4 From Kuşburnu Hot Spring in Turkey (2008).
  7. Wilson P and Remigio Z. “Production and characterisation of protease enzyme produced by a novel moderate thermophilic bacterium (EP1001) isolated from an alkaline hot spring, Zimbabwe”. African Journal of Microbiology Research27 (2012): 5542-5551.
  8. Pinzón‐Martínez D., et al. “Thermophilic bacteria from Mexican thermal environments: isolation and potential applications”. Environmental Technology8-9 (2010): 957-966.
  9. Synowiecki J. “Some applications of thermophiles and their enzymes for protein processing”. African Journal of Biotechnology42 (2010): 7020-7025.
  10. Preiss L., et al. “Structure of the mycobacterial ATP synthase Fo rotor ring in complex with the anti-TB drug bedaquiline”. Science Advances 4 (2015): e1500106.
  11. López-Otín C and Bond JS. “Proteases: multifunctional enzymes in life and disease”. Journal of Biological Chemistry (2008).
  12. Bowers KJ., et al. “Biodiversity of poly-extremophilic Bacteria: Does combining the extremes of high salt, alkaline pH and elevated temperature approach a physico-chemical boundary for life?”. Saline Systems1 (2009): 9.
  13. Martins RF., et al. “Starch-hydrolyzing bacteria from Ethiopian soda lakes”. Extremophiles2 (2001): 135-144.
  14. Kozubal M., et al. “Isolation and distribution of a novel iron-oxidizing crenarchaeon from acidic geothermal springs in Yellowstone National Park”. Applied and Environmental Microbiology4 (2008): 942-949.
  15. Cardoso AM., et al. “Archaeal metagenomics: bioprospecting novel genes and exploring new concepts”. Metagenomics: Theory, Methods, and Applications (2010):159-169.
  16. Datta S., et al. “Enzyme immobilization: an overview on techniques and support materials”. 3 Biotech1 (2013):1-9.
  17. De Maayer P., et al. “Some like it cold: understanding the survival strategies of psychrophiles”. EMBO Reports (2014): e201338170.
  18. Demirjian DC., et al. “Enzymes from extremophiles”. Current Opinion in Chemical Biology2 (2001): 144-151.
  19. Yildiz SY., et al. “Genomic analysis of Brevibacillus thermoruber 423 reveals its biotechnological and industrial potential”. Applied Microbiology and Biotechnology 5 (2015): 2277-2289.
  20. Anandharaj M., et al. “Production, purification, and biochemical characterization of thermostable metallo-protease from novel Bacillus alkalitelluris TWI3 isolated from tannery waste”. Applied Biochemistry and Biotechnology8 (2016): 1666-1686.
  21. Rajpal K., et al. “Extremophiles as biofactories of novel antimicrobials and cytotoxics–an assessment of bioactive properties of six fungal species inhabiting Rann of Kutch, India”. Indian Journal of Science and Technology24 (2016).
  22. Chakravorty D., et al. “Multifactorial level of extremostability of proteins: can they be exploited for protein engineering?” Extremophiles3 (2017): 419-444.
  23. Pant G., et al. “Production, optimization and partial purification of protease from Bacillus subtilis”. Journal of Taibah University for Science1 (2015): 50-55.
  24. Sharma J., et al. “Protease Production from Polyextremophilic Bacteria”. International Journal of Current Microbiology and Applied Sciences 5 (2016): 807-815.
  25. Tiwari ON., et al. “Isolation and optimization of alkaline protease producing Bacteria from undisturbed soil of NE-region of India falling under Indo-Burma biodiversity hotspots”. Journal of Applied Biology and Biotechnology 04 (2015): 025-031.
  26. Bhagat D., et al. Production and Characterization of Thermo-Alkalistable Xylanase from Geothermal Spring Isolate (2014).
  27. Danesh A., et al. “Production of haloduracin by Bacillus halodurans using solid-state fermentation”. Biotechnology Letters7 (2011): 1339-1344.
  28. Sahay H., et al. “Exploration and characterization of agriculturally and industrially important haloalkaliphilic bacteria from environmental samples of hypersaline Sambhar lake, India”. World Journal of Microbiology and Biotechnology11 (2012): 3207-3217.
  29. Khare SD and Fleishman SJ. “Emerging themes in the computational design of novel enzymes and protein–protein interfaces”. FEBS Letters8 (2013): 1147-1154.
  30. Yadav AN., et al. “Prospecting cold deserts of north western Himalayas for microbial diversity and plant growth promoting attributes”. Journal of Bioscience and Bioengineering6 (2015): 683-693.
  31. Cowan DA., et al. “Metagenomics of extreme environments”. Current Opinion in Microbiology 25 (2015): 97-102.
  32. Kristjansson JK. Thermophilic bacteria: CRC press (1991).
  33. Karan R., et al. Halophilic microorganisms as sources of novel enzymes. Microorganisms in sustainable agriculture and biotechnology: Springer (2012): 555-579.
  34. Fujiwara S. “Extremophiles: Developments of their special functions and potential resources”. Journal of Bioscience and Bioengineering6 (2002): 518-525.
  35. DasSarma P., et al. “Survival of halophilic Archaea in Earth's cold stratosphere”. International Journal of Astrobiology4 (2017): 321-327.
  36. Raddadi N., et al. “Halo-alkalitolerant and thermostable cellulases with improved tolerance to ionic liquids and organic solvents from Paenibacillus tarimensis isolated from the Chott El Fejej, Sahara desert, Tunisia”. Bioresource Technology 150 (2013): 121-128.
  37. Jin Q and Kirk MF. “PH as a primary control in environmental microbiology: 1. Thermodynamic perspective”. Frontiers in Environmental Science 6 (2018): 21.
  38. Morozkina E., et al. “Extremophilic microorganisms: biochemical adaptation and biotechnological application”. Applied Biochemistry and Microbiology1 (2010): 1-14.
  39. Wiegel J. “Anaerobic alkaliphiles and alkaliphilic poly-extremophiles”. Extremophiles Handbook: Springer (2011): 81-97.
  40. Dopson M and Holmes DS. “Metal resistance in acidophilic microorganisms and its significance for biotechnologies”. Applied Microbiology and Biotechnology19 (2014): 8133-8144.
  41. Sharma A., et al. “Acidophilic bacteria and archaea: acid stable biocatalysts and their potential applications”. Extremophiles 1 (2012): 1-19.
  42. Falagán C and Johnson DB. “Acidibacter ferrireducens gen. nov., sp. nov.: an acidophilic ferric iron-reducing gammaproteobacterium”. Extremophiles6 (2014): 1067-1073.
  43. Navarro CA., et al. “Heavy metal resistance strategies of acidophilic bacteria and their acquisition: importance for biomining and bioremediation”. Biological Research4 (2013): 363-371.
  44. Carapito C., et al. “Identification of genes and proteins involved in the pleiotropic response to arsenic stress in Caenibacter arsenoxydans, a metalloresistant beta-proteobacterium with an unsequenced genome”. Biochimie6 (2006): 595-606.
  45. Scambelluri M., et al. “Fossil intermediate-depth earthquakes in subducting slabs linked to differential stress release”. Nature Geoscience12 (2017): 960.
  46. Kumar L., et al. “Extremophiles: a novel source of industrially important enzymes”. Biotechnology2 (2011):121-135.
  47. Yano JK and Poulos TL. “New understandings of thermostable and peizostable enzymes”. Current Opinion in Biotechnology4 (2003): 360-365.
  48. Anupama A and Jayaraman G. “Detergent stable, halotolerant α-amylase from Bacillus aquimaris vitp4 exhibits reversible unfolding”. IJABPT 2 (2011): 366-376.
  49. Cavicchioli R., et al. “Biotechnological uses of enzymes from psychrophiles”. Microbial Biotechnology4 (2011): 449-460.
  50. Margesin R., et al. “Cold‐adapted microorganisms: adaptation strategies and biotechnological potential”. Encyclopedia of Environmental Microbiology (2003).
  51. Rolli E., et al. “Improved plant resistance to drought is promoted by the root‐associated microbiome as a water stress‐dependent trait”. Environmental Microbiology2 (2015): 316-331.
  52. Sghaier H., et al. “Basal DNA repair machinery is subject to positive selection in ionizing-radiation-resistant bacteria”. BMC Genomics1 (2008): 297.
  53. Gabani P and Singh OV. “Radiation-resistant extremophiles and their potential in biotechnology and therapeutics”. Applied Microbiology and Biotechnology3 (2013): 993-1004.
  54. Durvasula R and Rao DS. Extremophiles: From biology to biotechnology: CRC Press (2018).
  55. Collins T., et al. “Xylanases, xylanase families and extremophilic xylanases”. FEMS Microbiology Reviews1 (2005): 3-23.
  56. Ahirwar S., et al. “Isolation and screening of thermophilic and thermotolerant fungi for production of hemicellulases from heated environments”. Mycology 3 (2017): 125-134.
  57. Unsworth LD., et al. “Hyperthermophilic enzymes− stability, activity and implementation strategies for high temperature applications”. The FEBS Journal16 (2007): 4044-4056.
  58. Gurung N., et al. “A broader view: microbial enzymes and their relevance in industries, medicine, and beyond”. Biomed Research International (2013).
  59. Nigam P and Singh D. “Enzyme and microbial systems involved in starch processing”. Enzyme and Microbial Technology9 (1995): 770-778.
  60. Gupta G., et al. “Extremophiles: an overview of microorganism from extreme environment”. International Journal of Agriculture Environment and Biotechnology2 (2014):371.
  61. Al-Sayegh A., et al. “Microbial enhanced heavy crude oil recovery through biodegradation using bacterial isolates from an Omani oil field”. Microbial Cell Factories1 (2015):141.
  62. Schuster B. “S-layer protein-based biosensors”. Biosensors2 (2018): 40.
  63. Satyanarayana T., et al. “Extremophilic microbes: Diversity and perspectives”. Current Science (2005): 78-90.
  64. David A., et al. “Thermophilic Anaerobic Digestion: Enhanced and Sustainable Methane Production from Co-Digestion of Food and Lignocellulosic Wastes”. Energies8 (2018): 2058.
  65. Polizeli M., et al. “Xylanases from fungi: properties and industrial applications”. Applied Microbiology and Biotechnology5 (2005): 577-591.
  66. Dumorné K. “Biotechnological and Industrial Applications of Enzymes Produced by Extremophilic 1 Bacteria”. A Mini Review 2 (2018).
  67. Pandey A., et al. “New developments in solid state fermentation: I-bioprocesses and products”. Process Biochemistry10 (2000): 1153-1169.
  68. Tao H., et al. “Discrete element method modeling of non-spherical granular flow in rectangular hopper”. Chemical Engineering and Processing: Process Intensification2 (2010): 151-158.
  69. Saqib S., et al. “Sources of β-galactosidase and its applications in food industry”. 3 Biotech1 (2017): 79.
  70. Coker JA. “Extremophiles and biotechnology: current uses and prospects”. F1000 Research (2016): 5.
  71. Zareiforoush H., et al. “Performance evaluation of a 15.5 cm screw conveyor during handling process of rough rice (Oriza Sativa L.) grains”. Nature and Science6 (2010): 66-74.
  72. Taubner R-S., et al. “Assessing the ecophysiology of methanogens in the context of recent astrobiological and planetological studies”. Life 4 (2015): 1652-1686.
  73. Nakagawa T., et al. “Isolation and characterization of psychrophilic yeasts producing cold‐adapted pectinolytic enzymes”. Letters in Applied Microbiology5 (2004): 383-387.
  74. Harvey T., et al. “Thermophilic bioheap leaching of chalcopyrite concentrates”. Ejmp and Ep (European Journal of Mineral Processing and Environmental Protection).3 (2002): 253-263.
  75. Kostudis S., et al. “Leaching of copper from Kupferschiefer by glutamic acid and heterotrophic bacteria”. Minerals Engineering 75 (2015): 38-44.
  76. Tripathi V., et al. “Sustainable clean-up technologies for soils contaminated with multiple pollutants: plant-microbe-pollutant and climate nexus”. Ecological Engineering 82 (2015): 330-335.
  77. Sharma M., et al. “A novel approach of integrated bioprocessing of cane molasses for production of prebiotic and functional bioproducts”. Bioresource Technology 219 (2016): 311-318.
  78. Hatti-Kaul R., et al. “Cold active enzymes in food processing”. Food Biotechnology: CRC Press (2005): 1618-1640.
  79. Luo H., et al. “A thermophilic and acid stable family-10 xylanase from the acidophilic fungus Bispora sp. MEY-1”. Extremophiles 5 (2009): 849-857.
  80. Luisa Tutino M., et al. “Cold-adapted esterases and lipases: from fundamentals to application”. Protein and Peptide Letters10 (2009): 1172-1180.
  81. Ueda M., et al. “A novel cold-adapted cellulase complex from Eisenia foetida: characterization of a multienzyme complex with carboxymethylcellulase, β-glucosidase, β-1, 3 glucanase, and β-xylosidase”. Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology1 (2010): 26-32.
  82. Binod P., et al. Industrial Enzymes-Present status and future perspectives for India (2013).
  83. Huang S-X., et al. “Erythronolides H and I, new erythromycin congeners from a new halophilic actinomycete Actinopolyspora sp. YIM90600”. Organic Letters6 (2009): 1353-1356.
  84. Kirk O., et al. “Industrial enzyme applications”. Current Opinion in Biotechnology4 (2002): 345-351.
  85. Kohli U., et al. “Thermostable, alkalophilic and cellulase free xylanase production by Thermoactinomyces thalophilus subgroup C”. Enzyme and Microbial Technology7-8 (2001): 606-610.
  86. Stuart W. Industrial enzymology: Macmillan Press (1996).
  87. Gomes J and Steiner W. “The biocatalytic potential of extremophiles and extremozymes”. Food Technology and Biotechnology4 (2004): 223-235.
  88. Verma A., et al. “Microbial keratinases: industrial enzymes with waste management potential”. Critical Reviews in Biotechnology4 (2017): 476-491.
  89. Tortorella E., et al. “Antibiotics from deep-sea microorganisms: Current discoveries and perspectives”. Marine Drugs10 (2018): 355.
  90. Sohail M., et al. “Production of cellulase from Aspergillus terreus MS105 on crude and commercially purified substrates”. 3 Biotech 1 (2016): 103.
  91. Białkowska AM., et al. “Extremophilic proteases as novel and efficient tools in short peptide synthesis”. Journal of Industrial Microbiology and Biotechnology9 (2017): 1325-1342.
  92. Sellek GA and Chaudhuri JB. “Biocatalysis in organic media using enzymes from extremophiles”. Enzyme and Microbial Technology6 (1999): 471-482.
  93. Luef KP., et al. “Poly (hydroxy alkanoate) s in medical applications”. Chemical and Biochemical Engineering Quarterly2 (2015): 287-297.
  94. Ghoumrassi-Barr S and Aliouche D. “A rheological study of Xanthan polymer for enhanced oil recovery”. Journal of Macromolecular Science, Part B 8 (2016):793-809.
  95. Gerday C., et al. “Cold-adapted enzymes: from fundamentals to biotechnology”. Trends in Biotechnology3 (2000): 103-107.
  96. Demarche P., et al. “Harnessing the power of enzymes for environmental stewardship”. Biotechnology Advances5 (2012): 933-953.
  97. Saeedi P., et al. “Site-directed mutagenesis in bacteriorhodopsin mutants and their characterization for bioelectrical and biotechnological equipment”. Biotechnology Letters3 (2012): 455-462.
  98. Goswami S and Das M. “Extremophiles-A Clue to Origin of Life and Biology of Other Planets”. Everymans Science1 (2016): 17-25.
  99. Babamiri B., et al. “Ultrasensitive electrochemiluminescence immunoassay for simultaneous determination of CA125 and CA15-3 tumor markers based on PAMAM-sulfanilic acid-Ru (bpy) 32+ and PAMAM-CdTe@ CdS nanocomposite”. Biosensors and Bioelectronics 99 (2018): 353-360.
  100. Dalmaso GZ., et al. “Extracellular peptidases from Deinococcus radiodurans”. Extremophiles5 (2015): 989-999.
  101. Czech L., et al. “Role of the extremolytes ectoine and hydroxyectoine as stress protectants and nutrients: genetics, phylogenomics, biochemistry, and structural analysis”. Genes 4 (2018): 177.
  102. Shivanand P and Mugeraya G. “Halophilic bacteria and their compatible solutes–osmoregulation and potential applications”. Current Science (2011): 1516-1521.
  103. Joseph B., et al. “Cold active microbial lipases: some hot issues and recent developments”. Biotechnology Advances5 (2008): 457-470.
  104. Kunamneni A., et al. “Engineering and applications of fungal laccases for organic synthesis”. Microbial Cell Factories1 (2008): 32.
  105. Kiokias S., et al. “A review of the structure, biosynthesis, absorption of carotenoids-analysis and properties of their common natural extracts”. Current Research in Nutrition and Food Science Journal 4 (2016): 25-37.
  106. Quillaguaman J., et al. “Poly (β‐hydroxybutyrate) production by a moderate halophile, Halomonas boliviensis LC1 using starch hydrolysate as substrate”. Journal of Applied Microbiology1 (2005):151-157.
  107. Carpenter BL., et al. “Synthesis, characterization, and antimicrobial efficacy of photomicrobicidal cellulose paper”. Biomacromolecules 8 (2015): 2482-2492.
  108. Brim H., et al. “Engineering Deinococcus geothermalis for bioremediation of high-temperature radioactive waste environments”. Applied and Environmental Microbiology 8 (2003): 4575-4582.
  109. Hii SL., et al. “Pullulanase: role in starch hydrolysis and potential industrial applications”. Enzyme Research (2012).
  110. Turrens J. Superoxide dismutase and catalase (2018).
  111. Reed CJ., et al. “Protein adaptations in archaeal extremophiles”. Archaea (2013).
  112. Ortega G., et al. “Halophilic protein adaptation results from synergistic residue-ion interactions in the folded and unfolded states”. Chemistry and Biology12 (2015): 1597-1607.
  113. Amoozegar MA., et al. “Systematics of haloarchaea and biotechnological potential of their hydrolytic enzymes”. Microbiology5 (2017): 623-645.
  114. Mevarech M., et al. “Halophilic enzymes: proteins with a grain of salt”. Biophysical Chemistry2-3 (2000): 155-164.
  115. DasSarma S and DasSarma P. “Halophiles and their enzymes: negativity put to good use”. Current Opinion in Microbiology 25 (2015): 120-126.
  116. Georlette D., et al. “Cofactor binding modulates the conformational stabilities and unfolding patterns of NAD+-dependent DNA ligases from Escherichia coli and Thermus scotoductus”. Journal of Biological Chemistry50 (2003): 49945-49953.
  117. De Maayer P., et al. “Some like it cold: understanding the survival strategies of psychrophiles”. EMBO Reports 5 (2014): 508-517.
  118. Kumar V., et al. “In Silico Analysis of-Galactosidases Primary and Secondary Structure in relation to Temperature Adaptation”. Journal of Amino Acids (2014).
  119. Angelaccio S. “Extremophilic SHMTs: from structure to biotechnology”. Biomed Research International (2013).
  120. Huston AL., et al. “Cold adaptation of enzymes: Structural, kinetic and microcalorimetric characterizations of an aminopeptidase from the Arctic psychrophile Colwellia psychrerythraea and of human leukotriene A4 hydrolase”. Biochimica et Biophysica Acta (BBA)-Proteins and Proteomics11 (2008): 1865-1872.
  121. Michetti D., et al. “A comparative study of cold-and warm-adapted Endonucleases A using sequence analyses and molecular dynamics simulations”. PloS one 2 (2017): e0169586.
  122. Gianese G., et al. “Comparative structural analysis of psychrophilic and meso‐and thermophilic enzymes”. Proteins: Structure, Function, and Bioinformatics2 (2002): 236-249.
  123. Martinez N., et al. “High protein flexibility and reduced hydration water dynamics are key pressure adaptive strategies in prokaryotes”. Scientific Reports 6 (2016): 32816.
  124. Kawano H., et al. “Differential pressure resistance in the activity of RNA polymerase isolated from Shewanella violacea and Escherichia coli”. Extremophile 5 (2004): 367-375.
  125. Nagae T., et al. “Structural analysis of 3-isopropylmalate dehydrogenase from the obligate piezophile Shewanella benthica DB21MT-2 and the nonpiezophile Shewanella oneidensis MR-1”. Acta Crystallographica Section F: Structural Biology and Crystallization Communications3 (2012): 265-268.
  126. Shimada H., et al. “Complete polar lipid composition of Thermoplasma acidophilum HO-62 determined by high-performance liquid chromatography with evaporative light-scattering detection”. Journal of Bacteriology2 (2002): 556-563.
  127. Golyshina OV., et al. “Ferroplasma acidiphilum gen. nov., sp. nov., an acidophilic, autotrophic, ferrous-iron-oxidizing, cell-wall-lacking, mesophilic member of the Ferroplasmaceae fam. nov., comprising a distinct lineage of the Archaea”. International Journal of Systematic and Evolutionary Microbiology3 (2000): 997-1006.
  128. Batrakov SG., et al. “β-D-Glucopyranosyl caldarchaetidylglycerol is the main lipid of the acidophilic, mesophilic, ferrous iron-oxidising archaeon Ferroplasma acidiphilum”. Biochimica et Biophysica Acta (BBA)-Molecular and Cell Biology of Lipids1-2 (2002): 29-35.
  129. Pivovarova T., et al. “Phenotypic features of Ferroplasma acidiphilum strains YT and Y-2”. Microbiology 6 (2002): 698-706.
  130. Macalady J and Banfield JF. “Molecular geomicrobiology: genes and geochemical cycling”. Earth and Planetary Science Letters1-2 (2003): 1-17.
  131. Serour E and Antranikian G. “Novel thermoactive glucoamylases from the thermoacidophilic Archaea Thermoplasma acidophilum, Picrophilus torridus and Picrophilus oshimae”. Antonie Van Leeuwenhoek 1-4 (2002): 73-83.
  132. Van de Vossenberg JL., et al. “The essence of being extremophilic: the role of the unique archaeal membrane lipids”. Extremophiles3 (1998): 163-170.
  133. Van de Vossenberg JL., et al. “Bioenergetics and cytoplasmic membrane stability of the extremely acidophilic, thermophilic archaeon Picrophilus oshimae”. Extremophiles2 (1998): 67-74.
  134. Baker-Austin C and Dopson M. “Life in acid: pH homeostasis in acidophiles”. Trends in Microbiology 4 (2007): 165-171.
  135. Horikoshi K. “Alkaliphiles: some applications of their products for biotechnology”. Microbiology and Molecular Biology Reviews 4 (1999): 735-750.
  136. Ma Y., et al. “Alkalimonas amylolytica gen. nov., sp. nov., and Alkalimonas delamerensis gen. nov., sp. nov., novel alkaliphilic bacteria from soda lakes in China and East Africa”. Extremophiles3 (2004): 193-200.
  137. Minton KW and Daly MJ. “A model for repair of radiation‐induced DNA double‐strand breaks in the extreme radiophile Deinococcus radiodurans”. Bioessays5 (1995): 457-464.
  138. Brim H., et al. “Engineering Deinococcus radiodurans for metal remediation in radioactive mixed waste environments”. Nature Biotechnology1 (2000): 85.
  139. Nies DH. “Heavy metal-resistant bacteria as extremophiles: molecular physiology and biotechnological use of Ralstonia sp. CH34”. Extremophiles 2 (2000): 77-82.
  140. Adrian L and Görisch H. “Microbial transformation of chlorinated benzenes under anaerobic conditions”. Research in Microbiology3 (2002): 131-137.
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Citation

Citation: Jagdish Parihar and Ashima Bagaria. "The Extremes of Life and Extremozymes: Diversity and Perspectives". Acta Scientific Microbiology 3.1 (2020): 107-119.




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