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Volumn 29, Issue 1, 2014, Pages 116-123

Extremozymes-biocatalysts with unique properties from extremophilic microorganisms

Author keywords

[No Author keywords available]

Indexed keywords

ENZYMES; INDUSTRY; MICROORGANISMS;

EID: 84899789891     PISSN: 09581669     EISSN: 18790429     Source Type: Journal    
DOI: 10.1016/j.copbio.2014.04.003     Document Type: Review
Times cited : (272)

References (54)
  • 1
    • 84876726128 scopus 로고    scopus 로고
    • Protein engineering of enzymes for process applications
    • Woodley J.M. Protein engineering of enzymes for process applications. Curr Opin Chem Biol 2013, 17:310-316.
    • (2013) Curr Opin Chem Biol , vol.17 , pp. 310-316
    • Woodley, J.M.1
  • 2
    • 0029055215 scopus 로고
    • Extremozymes: expanding the limits of biocatalysis
    • Adams M.W., Perler F.B., Kelly R.M. Extremozymes: expanding the limits of biocatalysis. Biotechnology (N Y) 1995, 13:662-668.
    • (1995) Biotechnology (N Y) , vol.13 , pp. 662-668
    • Adams, M.W.1    Perler, F.B.2    Kelly, R.M.3
  • 3
    • 84876732154 scopus 로고    scopus 로고
    • Strategies for the discovery and engineering of enzymes for biocatalysis
    • Davids T., Schmidt M., Bottcher D., Bornscheuer U.T. Strategies for the discovery and engineering of enzymes for biocatalysis. Curr Opin Chem Biol 2013, 17:215-220.
    • (2013) Curr Opin Chem Biol , vol.17 , pp. 215-220
    • Davids, T.1    Schmidt, M.2    Bottcher, D.3    Bornscheuer, U.T.4
  • 4
    • 84868374454 scopus 로고    scopus 로고
    • End-to-end gene fusions and their impact on the production of multifunctional biomass degrading enzymes
    • Rizk M., Antranikian G., Elleuche S. End-to-end gene fusions and their impact on the production of multifunctional biomass degrading enzymes. Biochem Biophys Res Commun 2012, 428:1-5.
    • (2012) Biochem Biophys Res Commun , vol.428 , pp. 1-5
    • Rizk, M.1    Antranikian, G.2    Elleuche, S.3
  • 5
    • 84887560848 scopus 로고    scopus 로고
    • Recombinant bacterial amylopullulanases: developments and perspectives
    • Nisha M., Satyanarayana T. Recombinant bacterial amylopullulanases: developments and perspectives. Bioengineered 2013, 4.
    • (2013) Bioengineered , vol.4
    • Nisha, M.1    Satyanarayana, T.2
  • 7
    • 84877143960 scopus 로고    scopus 로고
    • Screening and expression of genes from metagenomes
    • Leis B., Angelov A., Liebl W. Screening and expression of genes from metagenomes. Adv Appl Microbiol 2013, 83:1-68.
    • (2013) Adv Appl Microbiol , vol.83 , pp. 1-68
    • Leis, B.1    Angelov, A.2    Liebl, W.3
  • 8
    • 84882695325 scopus 로고    scopus 로고
    • Dissecting and engineering metabolic and regulatory networks of thermophilic bacteria for biofuel production
    • Lin L., Xu J. Dissecting and engineering metabolic and regulatory networks of thermophilic bacteria for biofuel production. Biotechnol Adv 2013, 31:827-837.
    • (2013) Biotechnol Adv , vol.31 , pp. 827-837
    • Lin, L.1    Xu, J.2
  • 10
    • 70350496788 scopus 로고    scopus 로고
    • Microbial glucoamylases: characteristics and applications
    • Kumar P., Satyanarayana T. Microbial glucoamylases: characteristics and applications. Crit Rev Biotechnol 2009, 29:225-255.
    • (2009) Crit Rev Biotechnol , vol.29 , pp. 225-255
    • Kumar, P.1    Satyanarayana, T.2
  • 11
    • 0036525719 scopus 로고    scopus 로고
    • Starch-hydrolyzing enzymes from thermophilic archaea and bacteria
    • Bertoldo C., Antranikian G. Starch-hydrolyzing enzymes from thermophilic archaea and bacteria. Curr Opin Chem Biol 2002, 6:151-160.
    • (2002) Curr Opin Chem Biol , vol.6 , pp. 151-160
    • Bertoldo, C.1    Antranikian, G.2
  • 13
    • 77955837058 scopus 로고    scopus 로고
    • Extremophiles: a unique source of biocatalysts for industrial biotechnology
    • ASM Press, C. Gerday, N. Glansdorff (Eds.)
    • Antranikian G., Egorova K. Extremophiles: a unique source of biocatalysts for industrial biotechnology. In Physiology and Biochemistry of Extremophiles 2007, 361-406. ASM Press. C. Gerday, N. Glansdorff (Eds.).
    • (2007) In Physiology and Biochemistry of Extremophiles , pp. 361-406
    • Antranikian, G.1    Egorova, K.2
  • 14
    • 0025061657 scopus 로고
    • Extremely thermostable amylolytic enzyme from the archaebacterium Pyrococcus furiosus
    • Koch R., Zablowski P., Spreinat A., Antranikian G. Extremely thermostable amylolytic enzyme from the archaebacterium Pyrococcus furiosus. FEMS Microbiol Lett 1990, 71:21-26.
    • (1990) FEMS Microbiol Lett , vol.71 , pp. 21-26
    • Koch, R.1    Zablowski, P.2    Spreinat, A.3    Antranikian, G.4
  • 15
    • 84860836394 scopus 로고    scopus 로고
    • 2+-independent alpha-amylase from an acidophile Bacillus acidicola and its applicability in starch hydrolysis
    • 2+-independent alpha-amylase from an acidophile Bacillus acidicola and its applicability in starch hydrolysis. Extremophiles 2012, 16:515-522.
    • (2012) Extremophiles , vol.16 , pp. 515-522
    • Sharma, A.1    Satyanarayana, T.2
  • 16
  • 17
    • 0035752915 scopus 로고    scopus 로고
    • Biochemical confirmation and characterization of the family-57-like alpha-amylase of Methanococcus jannaschii
    • Kim J.W., Flowers L.O., Whiteley M., Peeples T.L. Biochemical confirmation and characterization of the family-57-like alpha-amylase of Methanococcus jannaschii. Folia Microbiol (Praha) 2001, 46:467-473.
    • (2001) Folia Microbiol (Praha) , vol.46 , pp. 467-473
    • Kim, J.W.1    Flowers, L.O.2    Whiteley, M.3    Peeples, T.L.4
  • 18
    • 84876681193 scopus 로고    scopus 로고
    • A highly thermoactive and salt-tolerant alpha-amylase isolated from a pilot-plant biogas reactor
    • Jabbour D., Sorger A., Sahm K., Antranikian G. A highly thermoactive and salt-tolerant alpha-amylase isolated from a pilot-plant biogas reactor. Appl Microbiol Biotechnol 2013, 97:2971-2978.
    • (2013) Appl Microbiol Biotechnol , vol.97 , pp. 2971-2978
    • Jabbour, D.1    Sorger, A.2    Sahm, K.3    Antranikian, G.4
  • 20
    • 77949874216 scopus 로고    scopus 로고
    • Pretreatment technologies for an efficient bioethanol production process based on enzymatic hydrolysis: a review
    • Alvira P., Tomas-Pejo E., Ballesteros M., Negro M.J. Pretreatment technologies for an efficient bioethanol production process based on enzymatic hydrolysis: a review. Bioresour Technol 2010, 101:4851-4861.
    • (2010) Bioresour Technol , vol.101 , pp. 4851-4861
    • Alvira, P.1    Tomas-Pejo, E.2    Ballesteros, M.3    Negro, M.J.4
  • 21
    • 33646937529 scopus 로고    scopus 로고
    • Preliminary results on optimization of pilot scale pretreatment of wheat straw used in coproduction of bioethanol and electricity
    • Thomsen M.H., Thygesen A., Jorgensen H., Larsen J., Christensen B.H., Thomsen A.B. Preliminary results on optimization of pilot scale pretreatment of wheat straw used in coproduction of bioethanol and electricity. Appl Biochem Biotechnol 2006, 129-132:448-460.
    • (2006) Appl Biochem Biotechnol , pp. 448-460
    • Thomsen, M.H.1    Thygesen, A.2    Jorgensen, H.3    Larsen, J.4    Christensen, B.H.5    Thomsen, A.B.6
  • 22
    • 84857923962 scopus 로고    scopus 로고
    • Lignocellulose converting enzymes from thermophiles
    • Springer, K. Horikoshi, G. Antranikian, A.T. Bull, F.T. Robb, K.O. Stetter (Eds.)
    • Klippel B., Antranikian G. Lignocellulose converting enzymes from thermophiles. Extremophiles Handbook 2011, 443-474. Springer. K. Horikoshi, G. Antranikian, A.T. Bull, F.T. Robb, K.O. Stetter (Eds.).
    • (2011) Extremophiles Handbook , pp. 443-474
    • Klippel, B.1    Antranikian, G.2
  • 24
    • 79959422060 scopus 로고    scopus 로고
    • Development of an integrated thermal and enzymatic hydrolysis for lignocellulosic biomass in fixed-bed reactors
    • Kirsch C., Zetzl C., Smirnova I. Development of an integrated thermal and enzymatic hydrolysis for lignocellulosic biomass in fixed-bed reactors. Holzforschung 2011, 65:483-489.
    • (2011) Holzforschung , vol.65 , pp. 483-489
    • Kirsch, C.1    Zetzl, C.2    Smirnova, I.3
  • 25
    • 84873119880 scopus 로고    scopus 로고
    • Improved lignocellulose conversion to biofuels with thermophilic bacteria and thermostable enzymes
    • Bhalla A., Bansal N., Kumar S., Bischoff K.M., Sani R.K. Improved lignocellulose conversion to biofuels with thermophilic bacteria and thermostable enzymes. Bioresour Technol 2013, 128:751-759.
    • (2013) Bioresour Technol , vol.128 , pp. 751-759
    • Bhalla, A.1    Bansal, N.2    Kumar, S.3    Bischoff, K.M.4    Sani, R.K.5
  • 26
    • 84878891688 scopus 로고    scopus 로고
    • Heterologous expression and characterization of a novel thermo-halotolerant endoglucanase Cel5H from Dictyoglomus thermophilum
    • Shi R., Li Z., Ye Q., Xu J., Liu Y. Heterologous expression and characterization of a novel thermo-halotolerant endoglucanase Cel5H from Dictyoglomus thermophilum. Bioresour Technol 2013, 142:338-344.
    • (2013) Bioresour Technol , vol.142 , pp. 338-344
    • Shi, R.1    Li, Z.2    Ye, Q.3    Xu, J.4    Liu, Y.5
  • 30
    • 84859479892 scopus 로고    scopus 로고
    • First crenarchaeal chitinase found in Sulfolobus tokodaii
    • Staufenberger T., Imhoff J.F., Labes A. First crenarchaeal chitinase found in Sulfolobus tokodaii. Microbiol Res 2012, 167:262-269.
    • (2012) Microbiol Res , vol.167 , pp. 262-269
    • Staufenberger, T.1    Imhoff, J.F.2    Labes, A.3
  • 31
    • 84888241634 scopus 로고    scopus 로고
    • Production of a thermostable and alkaline chitinase by Bacillus thuringiensis subsp. kurstaki strain HBK-51
    • Kuzu S.B., Guvenmez H.K., Denizci A.A. Production of a thermostable and alkaline chitinase by Bacillus thuringiensis subsp. kurstaki strain HBK-51. Biotechnol Res Int 2012, 2012:1354-1398.
    • (2012) Biotechnol Res Int , vol.2012 , pp. 1354-1398
    • Kuzu, S.B.1    Guvenmez, H.K.2    Denizci, A.A.3
  • 33
    • 84896696122 scopus 로고    scopus 로고
    • Functional expression and characterization of a chitinase from the marine archaeon Halobacterium salinarum CECT 395 in Escherichia coli
    • Garcia-Fraga B., da Silva A.F., Lopez-Seijas J., Sieiro C. Functional expression and characterization of a chitinase from the marine archaeon Halobacterium salinarum CECT 395 in Escherichia coli. Appl Microbiol Biotechnol 2013, 98:2133-2143.
    • (2013) Appl Microbiol Biotechnol , vol.98 , pp. 2133-2143
    • Garcia-Fraga, B.1    da Silva, A.F.2    Lopez-Seijas, J.3    Sieiro, C.4
  • 34
    • 79959965453 scopus 로고    scopus 로고
    • Selection of psychrotolerant microorganisms producing cold-active pectinases for biotechnological processes at low temperature
    • Cabeza M.S., Baca F.L., Muñoz Puntes E., Loto F., Baigorí M.D., Morata V.I. Selection of psychrotolerant microorganisms producing cold-active pectinases for biotechnological processes at low temperature. Food Technol Biotechnol 2011, 49:187-195.
    • (2011) Food Technol Biotechnol , vol.49 , pp. 187-195
    • Cabeza, M.S.1    Baca, F.L.2    Muñoz Puntes, E.3    Loto, F.4    Baigorí, M.D.5    Morata, V.I.6
  • 35
    • 84876066165 scopus 로고    scopus 로고
    • Commercial proteases: present and future
    • Li Q., Yi L., Marek P., Iverson B.L. Commercial proteases: present and future. FEBS Lett 2013, 587:1155-1163.
    • (2013) FEBS Lett , vol.587 , pp. 1155-1163
    • Li, Q.1    Yi, L.2    Marek, P.3    Iverson, B.L.4
  • 37
    • 84884276510 scopus 로고    scopus 로고
    • Proteolysin, a novel highly thermostable and cosolvent-compatible protease from the thermophilic bacterium Coprothermobacter proteolyticus
    • Toplak A., Wu B., Fusetti F., Quaedflieg P.J., Janssen D.B. Proteolysin, a novel highly thermostable and cosolvent-compatible protease from the thermophilic bacterium Coprothermobacter proteolyticus. Appl Environ Microbiol 2013, 79:5625-5632.
    • (2013) Appl Environ Microbiol , vol.79 , pp. 5625-5632
    • Toplak, A.1    Wu, B.2    Fusetti, F.3    Quaedflieg, P.J.4    Janssen, D.B.5
  • 39
    • 77951768870 scopus 로고    scopus 로고
    • A cold-adapted esterase of a novel marine isolate, Pseudoalteromonas arctica: gene cloning, enzyme purification and characterization
    • Al Khudary R., Venkatachalam R., Katzer M., Elleuche S., Antranikian G. A cold-adapted esterase of a novel marine isolate, Pseudoalteromonas arctica: gene cloning, enzyme purification and characterization. Extremophiles 2010, 14:273-285.
    • (2010) Extremophiles , vol.14 , pp. 273-285
    • Al Khudary, R.1    Venkatachalam, R.2    Katzer, M.3    Elleuche, S.4    Antranikian, G.5
  • 41
    • 83555177202 scopus 로고    scopus 로고
    • Phytases: crystal structures, protein engineering and potential biotechnological applications
    • Yao M.Z., Zhang Y.H., Lu W.L., Hu M.Q., Wang W., Liang A.H. Phytases: crystal structures, protein engineering and potential biotechnological applications. J Appl Microbiol 2012, 112:1-14.
    • (2012) J Appl Microbiol , vol.112 , pp. 1-14
    • Yao, M.Z.1    Zhang, Y.H.2    Lu, W.L.3    Hu, M.Q.4    Wang, W.5    Liang, A.H.6
  • 43
    • 84879507421 scopus 로고    scopus 로고
    • Biochemical characterization of an extracellular polyextremophilic alpha-amylase from the halophilic archaeon Halorubrum xinjiangense
    • Moshfegh M., Shahverdi A.R., Zarrini G., Faramarzi M.A. Biochemical characterization of an extracellular polyextremophilic alpha-amylase from the halophilic archaeon Halorubrum xinjiangense. Extremophiles 2013, 17:677-687.
    • (2013) Extremophiles , vol.17 , pp. 677-687
    • Moshfegh, M.1    Shahverdi, A.R.2    Zarrini, G.3    Faramarzi, M.A.4
  • 44
    • 79551472575 scopus 로고    scopus 로고
    • Molecular cloning and biochemical characterization of a heat-stable type I pullulanase from Thermotoga neapolitana
    • Kang J., Park K.M., Choi K.H., Park C.S., Kim G.E., Kim D., Cha J. Molecular cloning and biochemical characterization of a heat-stable type I pullulanase from Thermotoga neapolitana. Enzyme Microb Technol 2011, 48:260-266.
    • (2011) Enzyme Microb Technol , vol.48 , pp. 260-266
    • Kang, J.1    Park, K.M.2    Choi, K.H.3    Park, C.S.4    Kim, G.E.5    Kim, D.6    Cha, J.7
  • 45
    • 84855306511 scopus 로고    scopus 로고
    • Purification and characterization of intracellular and extracellular alpha-glucosidases from Geobacillus toebii strain E134
    • Cihan A.C., Benli M., Cokmus C. Purification and characterization of intracellular and extracellular alpha-glucosidases from Geobacillus toebii strain E134. Cell Biochem Funct 2011, 30:69-81.
    • (2011) Cell Biochem Funct , vol.30 , pp. 69-81
    • Cihan, A.C.1    Benli, M.2    Cokmus, C.3
  • 46
    • 84862787763 scopus 로고    scopus 로고
    • Purification and characterization of novel organic-solvent-tolerant beta-amylase and serine protease from a newly isolated Salimicrobium halophilum strain LY20
    • Li X., Yu H.Y. Purification and characterization of novel organic-solvent-tolerant beta-amylase and serine protease from a newly isolated Salimicrobium halophilum strain LY20. FEMS Microbiol Lett 2012, 329:204-211.
    • (2012) FEMS Microbiol Lett , vol.329 , pp. 204-211
    • Li, X.1    Yu, H.Y.2
  • 47
    • 84879485955 scopus 로고    scopus 로고
    • Overexpression and characterization of a glucose-tolerant β-glucosidase from Thermotoga thermarum DSM 5069T with high catalytic efficiency of ginsenoside Rb1 to Rd
    • Zhao L., Xie J., Zhang X., Cao F., Pei J. Overexpression and characterization of a glucose-tolerant β-glucosidase from Thermotoga thermarum DSM 5069T with high catalytic efficiency of ginsenoside Rb1 to Rd. J Mol Catal B Enzym 2013, 95:62-69.
    • (2013) J Mol Catal B Enzym , vol.95 , pp. 62-69
    • Zhao, L.1    Xie, J.2    Zhang, X.3    Cao, F.4    Pei, J.5
  • 48
    • 84894331221 scopus 로고    scopus 로고
    • Characterization of a heat-active archael beta-glucosidase from a hydrothermal spring metagenome
    • Schröder C., Elleuche S., Blank S., Antranikian G. Characterization of a heat-active archael beta-glucosidase from a hydrothermal spring metagenome. Enzyme Microb Technol 2014, 57:48-54.
    • (2014) Enzyme Microb Technol , vol.57 , pp. 48-54
    • Schröder, C.1    Elleuche, S.2    Blank, S.3    Antranikian, G.4
  • 49
    • 84864282393 scopus 로고    scopus 로고
    • Kinetic and thermodynamic study of cloned thermostable endo-1,4-beta-xylanase from Thermotoga petrophila in mesophilic host
    • ul Haq I., Hussain Z., Khan M.A., Muneer B., Afzal S., Majeed S., Akram F. Kinetic and thermodynamic study of cloned thermostable endo-1,4-beta-xylanase from Thermotoga petrophila in mesophilic host. Mol Biol Rep 2012, 39:7251-7261.
    • (2012) Mol Biol Rep , vol.39 , pp. 7251-7261
    • ul Haq, I.1    Hussain, Z.2    Khan, M.A.3    Muneer, B.4    Afzal, S.5    Majeed, S.6    Akram, F.7
  • 50
    • 70350780467 scopus 로고    scopus 로고
    • Thermostable lipases from the extreme thermophilic anaerobic bacteria Thermoanaerobacter thermohydrosulfuricus SOL1 and Caldanaerobacter subterraneus subsp. tengcongensis
    • Royter M., Schmidt M., Elend C., Hobenreich H., Schafer T., Bornscheuer U.T., Antranikian G. Thermostable lipases from the extreme thermophilic anaerobic bacteria Thermoanaerobacter thermohydrosulfuricus SOL1 and Caldanaerobacter subterraneus subsp. tengcongensis. Extremophiles 2009, 13:769-783.
    • (2009) Extremophiles , vol.13 , pp. 769-783
    • Royter, M.1    Schmidt, M.2    Elend, C.3    Hobenreich, H.4    Schafer, T.5    Bornscheuer, U.T.6    Antranikian, G.7
  • 52
    • 84873185153 scopus 로고    scopus 로고
    • History of discovery of extremophiles
    • Springer, K. Horikoshi, G. Antranikian, A.T. Bull, F.T. Robb, K.O. Stetter (Eds.)
    • Stetter K.O. History of discovery of extremophiles. Extremophiles Handbook 2011, 403-425. Springer. K. Horikoshi, G. Antranikian, A.T. Bull, F.T. Robb, K.O. Stetter (Eds.).
    • (2011) Extremophiles Handbook , pp. 403-425
    • Stetter, K.O.1
  • 53
    • 80054110691 scopus 로고    scopus 로고
    • Physiology, metabolism and enzymology of thermoacidophiles
    • Springer, K. Horikoshi, G. Antranikian, A.T. Bull, F.T. Robb, K.O. Stetter (Eds.)
    • Zaparty M., Siebers B. Physiology, metabolism and enzymology of thermoacidophiles. Extremophiles Handbook 2011, 601-639. Springer. K. Horikoshi, G. Antranikian, A.T. Bull, F.T. Robb, K.O. Stetter (Eds.).
    • (2011) Extremophiles Handbook , pp. 601-639
    • Zaparty, M.1    Siebers, B.2
  • 54
    • 84899833830 scopus 로고    scopus 로고
    • Thermophilic protein folding systems
    • Springer, K. Horikoshi, G. Antranikian, A.T. Bull, F.T. Robb, K.O. Stetter (Eds.)
    • Luo H., Robb F.T. Thermophilic protein folding systems. Extremophiles Handbook 2011, 583-599. Springer. K. Horikoshi, G. Antranikian, A.T. Bull, F.T. Robb, K.O. Stetter (Eds.).
    • (2011) Extremophiles Handbook , pp. 583-599
    • Luo, H.1    Robb, F.T.2


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