메뉴 건너뛰기




Volumn 25, Issue , 2015, Pages 113-119

Exploration of extremophiles for high temperature biotechnological processes

Author keywords

[No Author keywords available]

Indexed keywords

CELLULASE; CHITINASE; ENZYME; HYDROLASE; POLYSACCHARIDE; PROTEINASE; PEPTIDE HYDROLASE;

EID: 84931261553     PISSN: 13695274     EISSN: 18790364     Source Type: Journal    
DOI: 10.1016/j.mib.2015.05.011     Document Type: Review
Times cited : (109)

References (51)
  • 2
    • 0014148305 scopus 로고
    • Life at high temperatures
    • Brock T. Life at high temperatures. Science 1967, 158:1012-1019.
    • (1967) Science , vol.158 , pp. 1012-1019
    • Brock, T.1
  • 3
    • 33749835755 scopus 로고    scopus 로고
    • History of discovery of the first hyperthermophiles
    • Stetter K.O. History of discovery of the first hyperthermophiles. Extremophiles 2006, 10:357-362.
    • (2006) Extremophiles , vol.10 , pp. 357-362
    • Stetter, K.O.1
  • 4
    • 84899789891 scopus 로고    scopus 로고
    • Extremozymes-biocatalysts with unique properties from extremophilic microorganisms
    • Elleuche S., Schröder C., Sahm K., Antranikian G. Extremozymes-biocatalysts with unique properties from extremophilic microorganisms. Curr Opin Biotechnol 2014, 29:116-123.
    • (2014) Curr Opin Biotechnol , vol.29 , pp. 116-123
    • Elleuche, S.1    Schröder, C.2    Sahm, K.3    Antranikian, G.4
  • 5
    • 84890343400 scopus 로고    scopus 로고
    • Biotechnology of cold-active proteases
    • Joshi S., Satyanarayana T. Biotechnology of cold-active proteases. Biology (Basel) 2013, 2:755-783.
    • (2013) Biology (Basel) , vol.2 , pp. 755-783
    • Joshi, S.1    Satyanarayana, T.2
  • 6
    • 0032142867 scopus 로고    scopus 로고
    • Thermozymes: biotechnology and structure-function relationships
    • Zeikus J.G., Vieille C., Savchenko A. Thermozymes: biotechnology and structure-function relationships. Extremophiles 1998, 2:179-183.
    • (1998) Extremophiles , vol.2 , pp. 179-183
    • Zeikus, J.G.1    Vieille, C.2    Savchenko, A.3
  • 8
    • 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
  • 9
    • 84890589568 scopus 로고    scopus 로고
    • Cloning, overexpression and characterization of a thermostable pullulanase from Thermus thermophilus HB27
    • Wu H., Yu X., Chen L., Wu G. Cloning, overexpression and characterization of a thermostable pullulanase from Thermus thermophilus HB27. Protein Expr Purif 2014, 95:22-27.
    • (2014) Protein Expr Purif , vol.95 , pp. 22-27
    • Wu, H.1    Yu, X.2    Chen, L.3    Wu, G.4
  • 10
    • 50649108593 scopus 로고    scopus 로고
    • Biochemical characterization of engineered amylopullulanase from Thermoanaerobacter ethanolicus 39E-implicating the non-necessity of its 100 C-terminal amino acid residues
    • Lin H.Y., Chuang H.H., Lin F.P. Biochemical characterization of engineered amylopullulanase from Thermoanaerobacter ethanolicus 39E-implicating the non-necessity of its 100 C-terminal amino acid residues. Extremophiles 2008, 12:641-650.
    • (2008) Extremophiles , vol.12 , pp. 641-650
    • Lin, H.Y.1    Chuang, H.H.2    Lin, F.P.3
  • 11
    • 84879842967 scopus 로고    scopus 로고
    • Characterization of recombinant amylopullulanase (gt-apu) and truncated amylopullulanase (gt-apuT) of the extreme thermophile Geobacillus thermoleovorans NP33 and their action in starch saccharification
    • Nisha M., Satyanarayana T. Characterization of recombinant amylopullulanase (gt-apu) and truncated amylopullulanase (gt-apuT) of the extreme thermophile Geobacillus thermoleovorans NP33 and their action in starch saccharification. Appl Microbiol Biotechnol 2013, 97:6279-6292.
    • (2013) Appl Microbiol Biotechnol , vol.97 , pp. 6279-6292
    • Nisha, M.1    Satyanarayana, T.2
  • 12
    • 84893182884 scopus 로고    scopus 로고
    • Close relationship of a novel Flavobacteriaceae alpha-amylase with archaeal alpha-amylases and good potentials for industrial applications
    • Li C., Du M., Cheng B., Wang L., Liu X., Ma C., Yang C., Xu P. Close relationship of a novel Flavobacteriaceae alpha-amylase with archaeal alpha-amylases and good potentials for industrial applications. Biotechnol Biofuels 2014, 7:18.
    • (2014) Biotechnol Biofuels , vol.7 , pp. 18
    • Li, C.1    Du, M.2    Cheng, B.3    Wang, L.4    Liu, X.5    Ma, C.6    Yang, C.7    Xu, P.8
  • 13
    • 84900831002 scopus 로고    scopus 로고
    • Domain C of thermostable alpha-amylase of Geobacillus thermoleovorans mediates raw starch adsorption
    • Mehta D., Satyanarayana T. Domain C of thermostable alpha-amylase of Geobacillus thermoleovorans mediates raw starch adsorption. Appl Microbiol Biotechnol 2014, 98:4503-4519.
    • (2014) Appl Microbiol Biotechnol , vol.98 , pp. 4503-4519
    • Mehta, D.1    Satyanarayana, T.2
  • 15
    • 84865561632 scopus 로고    scopus 로고
    • Microbial cellulases and their industrial applications
    • Kuhad R.C., Gupta R., Singh A. Microbial cellulases and their industrial applications. Enzyme Res 2011, Article ID: 280696.
    • (2011) Enzyme Res
    • Kuhad, R.C.1    Gupta, R.2    Singh, A.3
  • 17
    • 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
  • 18
    • 84894331221 scopus 로고    scopus 로고
    • Characterization of a heat-active archaeal beta-glucosidase from a hydrothermal spring metagenome
    • Schröder C., Elleuche S., Blank S., Antranikian G. Characterization of a heat-active archaeal 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
  • 20
    • 84931269522 scopus 로고    scopus 로고
    • Biochemical characterization of a recombinant xylanase from Thermus brockianus, suitable for biofuel production
    • Blank S., Schröder C., Schirrmacher G., Reisinger C., Antranikian G. Biochemical characterization of a recombinant xylanase from Thermus brockianus, suitable for biofuel production. JSM Biotechnol Biomed Eng 2014, 2:1027.
    • (2014) JSM Biotechnol Biomed Eng , vol.2 , pp. 1027
    • Blank, S.1    Schröder, C.2    Schirrmacher, G.3    Reisinger, C.4    Antranikian, G.5
  • 22
    • 84883795907 scopus 로고    scopus 로고
    • Production of extremely alkaliphilic, halotolerent, detergent, and thermostable mannanase by the free and immobilized cells of Bacillus halodurans PPKS-2. Purification and characterization
    • Vijayalaxmi S., Prakash P., Jayalakshmi S.K., Mulimani V.H., Sreeramulu K. Production of extremely alkaliphilic, halotolerent, detergent, and thermostable mannanase by the free and immobilized cells of Bacillus halodurans PPKS-2. Purification and characterization. Appl Biochem Biotechnol 2013, 171:382-395.
    • (2013) Appl Biochem Biotechnol , vol.171 , pp. 382-395
    • Vijayalaxmi, S.1    Prakash, P.2    Jayalakshmi, S.K.3    Mulimani, V.H.4    Sreeramulu, K.5
  • 23
    • 80052960642 scopus 로고    scopus 로고
    • Expression and characterization of an extremely thermostable beta-glycosidase (mannosidase) from the hyperthermophilic archaeon Pyrococcus furiosus DSM3638
    • Park S.H., Park K.H., Oh B.C., Alli I., Lee B.H. Expression and characterization of an extremely thermostable beta-glycosidase (mannosidase) from the hyperthermophilic archaeon Pyrococcus furiosus DSM3638. N Biotechnol 2011, 28:639-648.
    • (2011) N Biotechnol , vol.28 , pp. 639-648
    • Park, S.H.1    Park, K.H.2    Oh, B.C.3    Alli, I.4    Lee, B.H.5
  • 24
    • 84874360110 scopus 로고    scopus 로고
    • Microbial pectinase: sources, characterization and applications
    • Sharma N., Rathore M., Sharma M. Microbial pectinase: sources, characterization and applications. Rev Environ Sci Bio/Technol 2013, 12:45-60.
    • (2013) Rev Environ Sci Bio/Technol , vol.12 , pp. 45-60
    • Sharma, N.1    Rathore, M.2    Sharma, M.3
  • 25
    • 84874889317 scopus 로고    scopus 로고
    • Potential application of pectinase in developing functional foods
    • Khan M., Nakkeeran E., Umesh-Kumar S. Potential application of pectinase in developing functional foods. Annu Rev Food Sci Technol 2013, 4:21-34.
    • (2013) Annu Rev Food Sci Technol , vol.4 , pp. 21-34
    • Khan, M.1    Nakkeeran, E.2    Umesh-Kumar, S.3
  • 26
    • 84898754300 scopus 로고    scopus 로고
    • Cloning, expression and characterization of a novel thermophilic polygalacturonase from Caldicellulosiruptor bescii DSM 6725
    • Chen Y., Sun D., Zhou Y., Liu L., Han W., Zheng B., Wang Z., Zhang Z. Cloning, expression and characterization of a novel thermophilic polygalacturonase from Caldicellulosiruptor bescii DSM 6725. Int J Mol Sci 2014, 15:5717-5729.
    • (2014) Int J Mol Sci , vol.15 , pp. 5717-5729
    • Chen, Y.1    Sun, D.2    Zhou, Y.3    Liu, L.4    Han, W.5    Zheng, B.6    Wang, Z.7    Zhang, Z.8
  • 27
    • 84881615666 scopus 로고    scopus 로고
    • Chitinolytic enzymes: an appraisal as a product of commercial potential
    • Chavan S.B., Deshpande M.V. Chitinolytic enzymes: an appraisal as a product of commercial potential. Biotechnol Prog 2013, 29:833-846.
    • (2013) Biotechnol Prog , vol.29 , pp. 833-846
    • Chavan, S.B.1    Deshpande, M.V.2
  • 28
    • 84879411416 scopus 로고    scopus 로고
    • Biochemical and molecular characterization of a thermostable chitosanase produced by the strain Paenibacillus sp. 1794 newly isolated from compost
    • Zitouni M., Fortin M., Scheerle R.K., Letzel T., Matteau D., Rodrigue S., Brzezinski R. Biochemical and molecular characterization of a thermostable chitosanase produced by the strain Paenibacillus sp. 1794 newly isolated from compost. Appl Microbiol Biotechnol 2013, 97:5801-5813.
    • (2013) Appl Microbiol Biotechnol , vol.97 , pp. 5801-5813
    • Zitouni, M.1    Fortin, M.2    Scheerle, R.K.3    Letzel, T.4    Matteau, D.5    Rodrigue, S.6    Brzezinski, R.7
  • 29
    • 84891804220 scopus 로고    scopus 로고
    • MEROPS: the database of proteolytic enzymes, their substrates and inhibitors
    • Rawlings N.D., Waller M., Barrett A.J., Bateman A. MEROPS: the database of proteolytic enzymes, their substrates and inhibitors. Nucleic Acids Res 2014, 42:D503-D509.
    • (2014) Nucleic Acids Res , vol.42 , pp. D503-D509
    • Rawlings, N.D.1    Waller, M.2    Barrett, A.J.3    Bateman, A.4
  • 30
    • 84931264848 scopus 로고
    • Verfahren zum Reinigen von Wäschestücken aller Art
    • US Patent
    • Röhm O: Verfahren zum Reinigen von Wäschestücken aller Art. US Patent 1913.
    • (1913)
    • Röhm, O.1
  • 32
    • 84894228773 scopus 로고    scopus 로고
    • A new pepstatin-insensitive thermopsin-like protease overproduced in peptide-rich cultures of Sulfolobus solfataricus
    • Gogliettino M., Riccio A., Cocca E., Rossi M., Palmieri G., Balestrieri M. A new pepstatin-insensitive thermopsin-like protease overproduced in peptide-rich cultures of Sulfolobus solfataricus. Int J Mol Sci 2014, 15:3204-3219.
    • (2014) Int J Mol Sci , vol.15 , pp. 3204-3219
    • Gogliettino, M.1    Riccio, A.2    Cocca, E.3    Rossi, M.4    Palmieri, G.5    Balestrieri, M.6
  • 33
    • 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
  • 35
    • 84899977441 scopus 로고    scopus 로고
    • Cloning, expression, purification and characterization of an oligomeric His-tagged thermophilic esterase from Thermus thermophilus HB27
    • Fuciños P., Atanes E., Lopez-Lopez O., Solaroli M., Cerdan M.E., Gonzalez-Siso M.I., Pastrana L., Rua M.L. Cloning, expression, purification and characterization of an oligomeric His-tagged thermophilic esterase from Thermus thermophilus HB27. Process Biochem 2014, 49:927-935.
    • (2014) Process Biochem , vol.49 , pp. 927-935
    • Fuciños, P.1    Atanes, E.2    Lopez-Lopez, O.3    Solaroli, M.4    Cerdan, M.E.5    Gonzalez-Siso, M.I.6    Pastrana, L.7    Rua, M.L.8
  • 36
    • 84907870626 scopus 로고    scopus 로고
    • Biochemical characterization of a carboxylesterase from the archaeon Pyrobaculum sp. 1860 and a rational explanation of its substrate specificity and thermostability
    • Shao H., Xu L., Yan Y. Biochemical characterization of a carboxylesterase from the archaeon Pyrobaculum sp. 1860 and a rational explanation of its substrate specificity and thermostability. Int J Mol Sci 2014, 15:16885-16910.
    • (2014) Int J Mol Sci , vol.15 , pp. 16885-16910
    • Shao, H.1    Xu, L.2    Yan, Y.3
  • 37
    • 84865647014 scopus 로고    scopus 로고
    • Characterization of a new thermophilic and acid tolerant esterase from Thermotoga maritima capable of hydrolytic resolution of racemic ketoprofen ethyl ester
    • Tao W., Shengxue F., Duobin M., Xuan Y., Congcong D., Xihua W. Characterization of a new thermophilic and acid tolerant esterase from Thermotoga maritima capable of hydrolytic resolution of racemic ketoprofen ethyl ester. J Mol Catal B Enz 2013, 85-86:23-30.
    • (2013) J Mol Catal B Enz , pp. 23-30
    • Tao, W.1    Shengxue, F.2    Duobin, M.3    Xuan, Y.4    Congcong, D.5    Xihua, W.6
  • 38
    • 84908264609 scopus 로고    scopus 로고
    • Newly identified thermostable esterase from Sulfobacillus acidophilus: properties and performance in phthalate ester degradation
    • Zhang X.Y., Fan X., Qiu Y.J., Li C.Y., Xing S., Zheng Y.T., Xu J.H. Newly identified thermostable esterase from Sulfobacillus acidophilus: properties and performance in phthalate ester degradation. Appl Environ Microbiol 2014, 80:6870-6878.
    • (2014) Appl Environ Microbiol , vol.80 , pp. 6870-6878
    • Zhang, X.Y.1    Fan, X.2    Qiu, Y.J.3    Li, C.Y.4    Xing, S.5    Zheng, Y.T.6    Xu, J.H.7
  • 39
    • 84928879558 scopus 로고    scopus 로고
    • Characterization of a thermostable, recombinant carboxylesterase from the hyperthermophilic Archaeon Metallosphaera sedula DSM5348
    • Killens-Cade R., Turner R., MacInnes C., Grunden A. Characterization of a thermostable, recombinant carboxylesterase from the hyperthermophilic Archaeon Metallosphaera sedula DSM5348. Adv Enzyme Res 2014, 2:1-13.
    • (2014) Adv Enzyme Res , vol.2 , pp. 1-13
    • Killens-Cade, R.1    Turner, R.2    MacInnes, C.3    Grunden, A.4
  • 41
    • 84924302954 scopus 로고    scopus 로고
    • Bringing functions together with fusion enzymes-from nature's inventions to biotechnological applications
    • Elleuche S. Bringing functions together with fusion enzymes-from nature's inventions to biotechnological applications. Appl Microbiol Biotechnol 2015, 99:1545-1556.
    • (2015) Appl Microbiol Biotechnol , vol.99 , pp. 1545-1556
    • Elleuche, S.1
  • 42
    • 77955135682 scopus 로고    scopus 로고
    • Parallel incorporation of different fluorinated amino acids: on the way to "teflon" proteins
    • Merkel L., Schauer M., Antranikian G., Budisa N. Parallel incorporation of different fluorinated amino acids: on the way to "teflon" proteins. Chembiochem 2010, 11:1505-1507.
    • (2010) Chembiochem , vol.11 , pp. 1505-1507
    • Merkel, L.1    Schauer, M.2    Antranikian, G.3    Budisa, N.4
  • 43
    • 77949913204 scopus 로고    scopus 로고
    • Alpha-Amylase: an ideal representative of thermostable enzymes
    • Prakash O., Jaiswal N: Alpha-Amylase: an ideal representative of thermostable enzymes. Appl Biochem Biotechnol 2010, 160:2401-2414.
    • (2010) Appl Biochem Biotechnol , vol.160 , pp. 2401-2414
    • Prakash, O.1    Jaiswal, N.2
  • 44
    • 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
  • 45
  • 46
    • 84876321656 scopus 로고    scopus 로고
    • Characterization and application of an acidophilic and thermostable beta-glucosidase from Thermofilum pendens
    • Li D., Li X., Dang W., Tran P.L., Park S.H., Oh B.C., Hong W.S., Lee J.S., Park K.H. Characterization and application of an acidophilic and thermostable beta-glucosidase from Thermofilum pendens. J Biosci Bioeng 2013, 115:490-496.
    • (2013) J Biosci Bioeng , vol.115 , pp. 490-496
    • Li, D.1    Li, X.2    Dang, W.3    Tran, P.L.4    Park, S.H.5    Oh, B.C.6    Hong, W.S.7    Lee, J.S.8    Park, K.H.9
  • 48
    • 84931268009 scopus 로고    scopus 로고
    • Characterization of an extracellular thermophilic chitinase from Paenibacillus thermoaerophilus strain TC22-2b isolated from compost
    • Ueda J., Kurosawa N. Characterization of an extracellular thermophilic chitinase from Paenibacillus thermoaerophilus strain TC22-2b isolated from compost. World J Microbiol Biotechnol 2015, 31:135-143.
    • (2015) World J Microbiol Biotechnol , vol.31 , pp. 135-143
    • Ueda, J.1    Kurosawa, N.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.