메뉴 건너뛰기




Volumn 13, Issue , 2013, Pages

Cloning, overexpression, purification, and characterization of a polyextremophilic β-galactosidase from the Antarctic haloarchaeon Halorubrum lacusprofundi

Author keywords

Biofuels; Extremozymes; Halophiles; Polyextremophiles; Protein stability; Psychrophiles

Indexed keywords

EXTREMOZYMES; HALOPHILES; POLYEXTREMOPHILES; PROTEIN STABILITY; PSYCHROPHILES;

EID: 84872200697     PISSN: None     EISSN: 14726750     Source Type: Journal    
DOI: 10.1186/1472-6750-13-3     Document Type: Article
Times cited : (79)

References (65)
  • 2
    • 84856077927 scopus 로고    scopus 로고
    • The core and unique proteins of haloarchaea
    • 10.1186/1471-2164-13-39, 3287961, 22272718
    • Capes MD, DasSarma P, DasSarma S. The core and unique proteins of haloarchaea. BMC Genomics 2012, 13:39. 10.1186/1471-2164-13-39, 3287961, 22272718.
    • (2012) BMC Genomics , vol.13 , pp. 39
    • Capes, M.D.1    DasSarma, P.2    DasSarma, S.3
  • 6
    • 84873057951 scopus 로고    scopus 로고
    • London: Wiley, Encyclopedia of life sciences
    • DasSarma S, DasSarma P. Halophiles 2012, London: Wiley, Encyclopedia of life sciences.
    • (2012) Halophiles
    • DasSarma, S.1    DasSarma, P.2
  • 7
    • 84868535169 scopus 로고    scopus 로고
    • Genome-wide responses of the model archaeon Halobacterium sp. strain NRC-1 to oxygen limitation
    • 10.1128/JB.01153-12, 22865851
    • DasSarma P, Zamora RC, Müller JA, DasSarma S. Genome-wide responses of the model archaeon Halobacterium sp. strain NRC-1 to oxygen limitation. J Bacteriol 2012, 194:5530-5537. 10.1128/JB.01153-12, 22865851.
    • (2012) J Bacteriol , vol.194 , pp. 5530-5537
    • DasSarma, P.1    Zamora, R.C.2    Müller, J.A.3    DasSarma, S.4
  • 8
    • 84862143520 scopus 로고    scopus 로고
    • Function and biotechnology of extremophilic enzymes in low water activity
    • 10.1186/2046-9063-8-4, 3310334, 22480329
    • Karan R, Capes MD, DasSarma S. Function and biotechnology of extremophilic enzymes in low water activity. Aquat Biosyst 2012, 8:4. 10.1186/2046-9063-8-4, 3310334, 22480329.
    • (2012) Aquat Biosyst , vol.8 , pp. 4
    • Karan, R.1    Capes, M.D.2    DasSarma, S.3
  • 9
    • 33750334684 scopus 로고    scopus 로고
    • Extreme halophiles are models for astrobiology
    • DasSarma S. Extreme halophiles are models for astrobiology. Microbe 2006, 1:120-127.
    • (2006) Microbe , vol.1 , pp. 120-127
    • DasSarma, S.1
  • 12
    • 0041335427 scopus 로고    scopus 로고
    • Biochemical characterization of a beta-galactosidase with a low temperature optimum obtained from an Antarctic Arthrobacter isolate
    • 10.1128/JB.185.18.5473-5482.2003, 193751, 12949099
    • Coker JA, Sheridan PP, Loveland-Curtze J, Gutshall KR, Auman AJ, Brenchley JE. Biochemical characterization of a beta-galactosidase with a low temperature optimum obtained from an Antarctic Arthrobacter isolate. J Bacteriol 2003, 185:5473-5482. 10.1128/JB.185.18.5473-5482.2003, 193751, 12949099.
    • (2003) J Bacteriol , vol.185 , pp. 5473-5482
    • Coker, J.A.1    Sheridan, P.P.2    Loveland-Curtze, J.3    Gutshall, K.R.4    Auman, A.J.5    Brenchley, J.E.6
  • 13
    • 33749020794 scopus 로고    scopus 로고
    • Purification and molecular characterization of cold active beta-galactosidase from Arthrobacter psychrolactophilus strain F2
    • 10.1007/s00253-006-0339-0, 16607530
    • Nakagawa T, Fujimoto Y, Ikehata R, Miyaji T, Tomizuka N. Purification and molecular characterization of cold active beta-galactosidase from Arthrobacter psychrolactophilus strain F2. Appl Microbiol Biotechnol 2006, 72:720-725. 10.1007/s00253-006-0339-0, 16607530.
    • (2006) Appl Microbiol Biotechnol , vol.72 , pp. 720-725
    • Nakagawa, T.1    Fujimoto, Y.2    Ikehata, R.3    Miyaji, T.4    Tomizuka, N.5
  • 14
    • 0031036727 scopus 로고    scopus 로고
    • Purification and analysis of an extremely halophilic beta-galactosidase from Haloferax alicantei
    • 10.1016/S0167-4838(96)00174-4, 9048905
    • Holmes ML, Scopes RK, Moritz RL, Simpson RJ, Englert C, Pfeifer F, Dyall-Smith ML. Purification and analysis of an extremely halophilic beta-galactosidase from Haloferax alicantei. Biochim Biophys Acta 1997, 1337:276-286. 10.1016/S0167-4838(96)00174-4, 9048905.
    • (1997) Biochim Biophys Acta , vol.1337 , pp. 276-286
    • Holmes, M.L.1    Scopes, R.K.2    Moritz, R.L.3    Simpson, R.J.4    Englert, C.5    Pfeifer, F.6    Dyall-Smith, M.L.7
  • 15
    • 0032135068 scopus 로고    scopus 로고
    • Thermostable beta-galactosidase from an extreme thermophile, Thermus sp. A4: enzyme purification and characterization, and gene cloning and sequencing
    • 10.1271/bbb.62.1539, 9757561
    • Ohtsu N, Motoshima H, Goto K, Tsukasaki F, Matsuzawa H. Thermostable beta-galactosidase from an extreme thermophile, Thermus sp. A4: enzyme purification and characterization, and gene cloning and sequencing. Biosci Biotechnol Biochem 1998, 62:1539-1545. 10.1271/bbb.62.1539, 9757561.
    • (1998) Biosci Biotechnol Biochem , vol.62 , pp. 1539-1545
    • Ohtsu, N.1    Motoshima, H.2    Goto, K.3    Tsukasaki, F.4    Matsuzawa, H.5
  • 16
    • 34147132399 scopus 로고    scopus 로고
    • Molecular cloning and characterization of the gene encoding cold-active β-galactosidase from a psychrotrophic and halotolerant Planococcus sp. L4
    • 10.1021/jf062910r, 17326654
    • Hu JM, Li H, Cao LX, Wu PC, Zhang CT, Sang SL, Zhang XY, Chen MJ, Lu JQ, Liu YH. Molecular cloning and characterization of the gene encoding cold-active β-galactosidase from a psychrotrophic and halotolerant Planococcus sp. L4. J Agric Food Chem 2007, 55:2217-2224. 10.1021/jf062910r, 17326654.
    • (2007) J Agric Food Chem , vol.55 , pp. 2217-2224
    • Hu, J.M.1    Li, H.2    Cao, L.X.3    Wu, P.C.4    Zhang, C.T.5    Sang, S.L.6    Zhang, X.Y.7    Chen, M.J.8    Lu, J.Q.9    Liu, Y.H.10
  • 17
    • 0036968554 scopus 로고    scopus 로고
    • Trimeric crystal structure of the glycoside hydrolase family 42 beta-galactosidase from Thermus thermophilus A4 and the structure of its complex with galactose
    • 10.1016/S0022-2836(02)00746-5, 12215416
    • Hidaka M, Fushinobu S, Ohtsu N, Motoshima H, Matsuzawa H, Shoun H, Wakagi T. Trimeric crystal structure of the glycoside hydrolase family 42 beta-galactosidase from Thermus thermophilus A4 and the structure of its complex with galactose. J Mol Biol 2002, 322:79-91. 10.1016/S0022-2836(02)00746-5, 12215416.
    • (2002) J Mol Biol , vol.322 , pp. 79-91
    • Hidaka, M.1    Fushinobu, S.2    Ohtsu, N.3    Motoshima, H.4    Matsuzawa, H.5    Shoun, H.6    Wakagi, T.7
  • 18
    • 0034080264 scopus 로고    scopus 로고
    • Characterization of a salt-tolerant family 42 beta-galactosidase from a psychrophilic antarctic Planococcus isolate
    • 10.1128/AEM.66.6.2438-2444.2000, 110553, 10831422
    • Sheridan PP, Brenchley JE. Characterization of a salt-tolerant family 42 beta-galactosidase from a psychrophilic antarctic Planococcus isolate. Appl Environ Microbiol 2000, 66:2438-2444. 10.1128/AEM.66.6.2438-2444.2000, 110553, 10831422.
    • (2000) Appl Environ Microbiol , vol.66 , pp. 2438-2444
    • Sheridan, P.P.1    Brenchley, J.E.2
  • 19
    • 11244299580 scopus 로고    scopus 로고
    • Beta-galactosidase from Bifidobacterium adolescentis DSM20083 prefers beta(1,4)-galactosides over lactose
    • 10.1007/s00253-004-1745-9, 15480628
    • Hinz SW, Van den Brock LA, Beldman G, Vincken JP, Voragen AG. Beta-galactosidase from Bifidobacterium adolescentis DSM20083 prefers beta(1,4)-galactosides over lactose. Appl Microbiol Biotechnol 2004, 66:276-284. 10.1007/s00253-004-1745-9, 15480628.
    • (2004) Appl Microbiol Biotechnol , vol.66 , pp. 276-284
    • Hinz, S.W.1    Van den Brock, L.A.2    Beldman, G.3    Vincken, J.P.4    Voragen, A.G.5
  • 20
    • 23744504522 scopus 로고    scopus 로고
    • Characterization of an unusual cold-active beta-glucosidase belonging to family 3 of the glycoside hydrolases from the psychrophilic isolate Paenibacillus sp. strain C7
    • Shipkowski S, Brenchley JE. Characterization of an unusual cold-active beta-glucosidase belonging to family 3 of the glycoside hydrolases from the psychrophilic isolate Paenibacillus sp. strain C7. Appl Environ Microbiol 2005, 7:4225-4232.
    • (2005) Appl Environ Microbiol , vol.7 , pp. 4225-4232
    • Shipkowski, S.1    Brenchley, J.E.2
  • 21
    • 33845546936 scopus 로고    scopus 로고
    • Bioinformatic, genetic, and biochemical evidence that some glycoside hydrolase family 42 beta-galactosidases are arabinogalactan type I oligomer hydrolases
    • 10.1128/AEM.01306-06, 1694227, 17056685
    • Shipkowski S, Brenchley JE. Bioinformatic, genetic, and biochemical evidence that some glycoside hydrolase family 42 beta-galactosidases are arabinogalactan type I oligomer hydrolases. Appl Environ Microbiol 2006, 72:7730-7738. 10.1128/AEM.01306-06, 1694227, 17056685.
    • (2006) Appl Environ Microbiol , vol.72 , pp. 7730-7738
    • Shipkowski, S.1    Brenchley, J.E.2
  • 22
    • 68849108440 scopus 로고    scopus 로고
    • Enzymes from solvent-tolerant microbes: useful biocatalysts for non-aqueous enzymology
    • 10.1080/07388550802688797, 19514902
    • Gupta A, Khare SK. Enzymes from solvent-tolerant microbes: useful biocatalysts for non-aqueous enzymology. Crit Rev Biotechnol 2009, 29:44-54. 10.1080/07388550802688797, 19514902.
    • (2009) Crit Rev Biotechnol , vol.29 , pp. 44-54
    • Gupta, A.1    Khare, S.K.2
  • 23
    • 75349100918 scopus 로고    scopus 로고
    • Organic solvent-tolerant enzymes
    • Doukyua N, Ogino H. Organic solvent-tolerant enzymes. Biochem Eng J 2010, 48:270-282.
    • (2010) Biochem Eng J , vol.48 , pp. 270-282
    • Doukyua, N.1    Ogino, H.2
  • 26
    • 68849126686 scopus 로고    scopus 로고
    • A new cold-adapted β-D-galactosidase from the Antarctic Arthrobacter sp. 32c - gene cloning, overexpression, purification and properties
    • 10.1186/1471-2180-9-1, 2631447, 19121223
    • Hildebrandt P, Wanarska M, Kur J. A new cold-adapted β-D-galactosidase from the Antarctic Arthrobacter sp. 32c - gene cloning, overexpression, purification and properties. BMC Microbiol 2009, 9:1-11. 10.1186/1471-2180-9-1, 2631447, 19121223.
    • (2009) BMC Microbiol , vol.9 , pp. 1-11
    • Hildebrandt, P.1    Wanarska, M.2    Kur, J.3
  • 28
    • 78650602812 scopus 로고    scopus 로고
    • HaloWeb: the haloarchaeal genomes database
    • 10.1186/1746-1448-6-12, 3023673, 21192823
    • DasSarma SL, Capes MD, DasSarma P, DasSarma S. HaloWeb: the haloarchaeal genomes database. Saline Systems 2010, 6:12. 10.1186/1746-1448-6-12, 3023673, 21192823.
    • (2010) Saline Systems , vol.6 , pp. 12
    • DasSarma, S.L.1    Capes, M.D.2    DasSarma, P.3    DasSarma, S.4
  • 30
    • 0030801002 scopus 로고    scopus 로고
    • Gapped BLAST and PSI-BLAST: a new generation of protein database search programs
    • 10.1093/nar/25.17.3389, 146917, 9254694
    • Altschul SF, Madden TL, Schaffer AA, Zhang J, Zhang Z, Miller W, Lipman DJ. Gapped BLAST and PSI-BLAST: a new generation of protein database search programs. Nucleic Acids Res 1997, 25:3389-3402. 10.1093/nar/25.17.3389, 146917, 9254694.
    • (1997) Nucleic Acids Res , vol.25 , pp. 3389-3402
    • Altschul, S.F.1    Madden, T.L.2    Schaffer, A.A.3    Zhang, J.4    Zhang, Z.5    Miller, W.6    Lipman, D.J.7
  • 31
    • 27144489108 scopus 로고    scopus 로고
    • Protein database searches using compositionally adjusted substitution matrices
    • 10.1111/j.1742-4658.2005.04945.x, 1343503, 16218944
    • Altschul SF, Wootton JC, Gertz EM, Agarwala R, Morgulis A, Schäffer AA, Yu YK. Protein database searches using compositionally adjusted substitution matrices. FEBS J 2005, 272:5101-5109. 10.1111/j.1742-4658.2005.04945.x, 1343503, 16218944.
    • (2005) FEBS J , vol.272 , pp. 5101-5109
    • Altschul, S.F.1    Wootton, J.C.2    Gertz, E.M.3    Agarwala, R.4    Morgulis, A.5    Schäffer, A.A.6    Yu, Y.K.7
  • 32
    • 0031574072 scopus 로고    scopus 로고
    • The CLUSTAL_X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools
    • 10.1093/nar/25.24.4876, 147148, 9396791
    • Thompson JD, Gibson TJ, Plewniak F, Jeanmougin F, Higgins DG. The CLUSTAL_X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools. Nucleic Acids Res 1997, 25:4876-4882. 10.1093/nar/25.24.4876, 147148, 9396791.
    • (1997) Nucleic Acids Res , vol.25 , pp. 4876-4882
    • Thompson, J.D.1    Gibson, T.J.2    Plewniak, F.3    Jeanmougin, F.4    Higgins, D.G.5
  • 33
    • 36048979618 scopus 로고    scopus 로고
    • Transcriptional profiling of the model Archaeon Halobacterium sp. NRC-1: responses to changes in salinity and temperature
    • 10.1186/1746-1448-3-6, 1971269, 17651475
    • Coker JA, DasSarma P, Kumar J, Müller JA, DasSarma S. Transcriptional profiling of the model Archaeon Halobacterium sp. NRC-1: responses to changes in salinity and temperature. Saline Systems 2007, 3:6. 10.1186/1746-1448-3-6, 1971269, 17651475.
    • (2007) Saline Systems , vol.3 , pp. 6
    • Coker, J.A.1    DasSarma, P.2    Kumar, J.3    Müller, J.A.4    DasSarma, S.5
  • 34
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • 10.1016/0003-2697(76)90527-3, 942051
    • Bradford MM. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 1976, 72:248-254. 10.1016/0003-2697(76)90527-3, 942051.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 35
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • 10.1038/227680a0, 5432063
    • Laemmli UK. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970, 227:680-685. 10.1038/227680a0, 5432063.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 36
    • 0037108887 scopus 로고    scopus 로고
    • Empirical statistical model to estimate the accuracy of peptide identifications made by MS/MS and database search
    • 10.1021/ac025747h, 12403597
    • Keller A, Nesvizhskii AI, Kolker E, Aebersold R. Empirical statistical model to estimate the accuracy of peptide identifications made by MS/MS and database search. Anal Chem 2002, 74:5383-5392. 10.1021/ac025747h, 12403597.
    • (2002) Anal Chem , vol.74 , pp. 5383-5392
    • Keller, A.1    Nesvizhskii, A.I.2    Kolker, E.3    Aebersold, R.4
  • 37
    • 0034767491 scopus 로고    scopus 로고
    • Understanding the adaptation of Halobacterium species NRC-1 to its extreme environment through computational analysis of its genome sequence
    • 10.1101/gr.190201, 311145, 11591641
    • Kennedy SP, Ng WV, Salzberg SL, Hood L, DasSarma S. Understanding the adaptation of Halobacterium species NRC-1 to its extreme environment through computational analysis of its genome sequence. Genome Res 2001, 11:1641-1650. 10.1101/gr.190201, 311145, 11591641.
    • (2001) Genome Res , vol.11 , pp. 1641-1650
    • Kennedy, S.P.1    Ng, W.V.2    Salzberg, S.L.3    Hood, L.4    DasSarma, S.5
  • 39
    • 0024602106 scopus 로고
    • Characterization of the small endogenous plasmid of Halobacterium strain SB3 and its use in transformation of H. halobium
    • 10.1139/m89-013, 2720495
    • Hackett NR, DasSarma S. Characterization of the small endogenous plasmid of Halobacterium strain SB3 and its use in transformation of H. halobium. Can J Microbiol 1989, 35:86-91. 10.1139/m89-013, 2720495.
    • (1989) Can J Microbiol , vol.35 , pp. 86-91
    • Hackett, N.R.1    DasSarma, S.2
  • 40
    • 0031922353 scopus 로고    scopus 로고
    • Suppressor mutation analysis of the sensory rhodopsin I-transducer complex: insights into the color-sensing mechanism
    • 107127, 9555883
    • Jung KH, Spudich JL. Suppressor mutation analysis of the sensory rhodopsin I-transducer complex: insights into the color-sensing mechanism. J Bacteriol 1998, 180:2033-2042. 107127, 9555883.
    • (1998) J Bacteriol , vol.180 , pp. 2033-2042
    • Jung, K.H.1    Spudich, J.L.2
  • 41
    • 0027408494 scopus 로고
    • The rightward gas vesicle operon in Halobacterium plasmid pNRC100: identification of the gvpA and gvpC gene products by use of antibody probes and genetic analysis of the region downstream of gvpC
    • 196206, 8423144
    • Halladay JT, Jones JG, Lin F, MacDonald AB, DasSarma S. The rightward gas vesicle operon in Halobacterium plasmid pNRC100: identification of the gvpA and gvpC gene products by use of antibody probes and genetic analysis of the region downstream of gvpC. J Bacteriol 1993, 175:684-692. 196206, 8423144.
    • (1993) J Bacteriol , vol.175 , pp. 684-692
    • Halladay, J.T.1    Jones, J.G.2    Lin, F.3    MacDonald, A.B.4    DasSarma, S.5
  • 43
    • 0035319361 scopus 로고    scopus 로고
    • Cold-adapted beta-galactosidase from the Antarctic psychrophile Pseudoalteromonas haloplanktis
    • 10.1128/AEM.67.4.1529-1535.2001, 92765, 11282601
    • Hoyoux A, Jennes I, Dubois P, Genicot S, Dubail F, François JM, Baise E, Feller G, Gerday C. Cold-adapted beta-galactosidase from the Antarctic psychrophile Pseudoalteromonas haloplanktis. Appl Environ Microbiol 2001, 67:1529-1535. 10.1128/AEM.67.4.1529-1535.2001, 92765, 11282601.
    • (2001) Appl Environ Microbiol , vol.67 , pp. 1529-1535
    • Hoyoux, A.1    Jennes, I.2    Dubois, P.3    Genicot, S.4    Dubail, F.5    François, J.M.6    Baise, E.7    Feller, G.8    Gerday, C.9
  • 44
    • 80053439614 scopus 로고    scopus 로고
    • Recombinant microbial systems for improved β-galactosidase production and biotechnological applications
    • Oliveira C, Guimarães PM, Domingues L. Recombinant microbial systems for improved β-galactosidase production and biotechnological applications. Biotechnol Adv 2011, 29:600-609.
    • (2011) Biotechnol Adv , vol.29 , pp. 600-609
    • Oliveira, C.1    Guimarães, P.M.2    Domingues, L.3
  • 46
    • 84866927713 scopus 로고    scopus 로고
    • Optimization to low temperature activity in psychrophilic enzymes
    • 10.3390/ijms130911643, 3472767, 23109875
    • Struvay C, Feller G. Optimization to low temperature activity in psychrophilic enzymes. Int J Mol Sci 2012, 13:11643-11665. 10.3390/ijms130911643, 3472767, 23109875.
    • (2012) Int J Mol Sci , vol.13 , pp. 11643-11665
    • Struvay, C.1    Feller, G.2
  • 47
    • 0034166764 scopus 로고    scopus 로고
    • Halophilic adaptation of enzymes
    • 10.1007/s007920050142, 10805563
    • Madern D, Ebel C, Zaccai G. Halophilic adaptation of enzymes. Extremophiles 2000, 4:91-98. 10.1007/s007920050142, 10805563.
    • (2000) Extremophiles , vol.4 , pp. 91-98
    • Madern, D.1    Ebel, C.2    Zaccai, G.3
  • 48
    • 0035805436 scopus 로고    scopus 로고
    • Hydrophobic interaction chromatography of proteins
    • 10.1016/S0168-1656(01)00237-1, 11278038
    • Queiroz JA, Tomaz CT, Cabral JM. Hydrophobic interaction chromatography of proteins. J Biotechnol 2001, 87:143-159. 10.1016/S0168-1656(01)00237-1, 11278038.
    • (2001) J Biotechnol , vol.87 , pp. 143-159
    • Queiroz, J.A.1    Tomaz, C.T.2    Cabral, J.M.3
  • 49
    • 77953754385 scopus 로고    scopus 로고
    • Purification and characterization of a solvent stable protease from Geomicrobium sp. EMB2
    • Karan R, Khare SK. Purification and characterization of a solvent stable protease from Geomicrobium sp. EMB2. Environ Technol 2010, 10:1061-1072.
    • (2010) Environ Technol , vol.10 , pp. 1061-1072
    • Karan, R.1    Khare, S.K.2
  • 50
    • 0025115569 scopus 로고
    • Efficient high performance liquid chromatographic system for the purification of a halobacterial serine protease
    • Schmitt W, Rdest U, Goebel W. Efficient high performance liquid chromatographic system for the purification of a halobacterial serine protease. J Chromatogr 1990, 521:211-220.
    • (1990) J Chromatogr , vol.521 , pp. 211-220
    • Schmitt, W.1    Rdest, U.2    Goebel, W.3
  • 53
    • 77955848869 scopus 로고    scopus 로고
    • A novel metagenome-derived beta-galactosidase: gene cloning, overexpression, purification and characterization
    • 10.1007/s00253-010-2744-7, 20614217
    • Wang K, Li G, Yu SQ, Zhang CT, Liu YH. A novel metagenome-derived beta-galactosidase: gene cloning, overexpression, purification and characterization. Appl Microbiol Biotechnol 2010, 88:155-165. 10.1007/s00253-010-2744-7, 20614217.
    • (2010) Appl Microbiol Biotechnol , vol.88 , pp. 155-165
    • Wang, K.1    Li, G.2    Yu, S.Q.3    Zhang, C.T.4    Liu, Y.H.5
  • 54
    • 0141670507 scopus 로고    scopus 로고
    • The cloning, purification and characterization of a cold-active β-galactosidase from the psychrotolerant antarctic bacterium Arthrobacter sp. C2-2
    • Karasova-Lipovova P, Strnad H, Spiwok V, Mala S, Kralova B, Russell N. The cloning, purification and characterization of a cold-active β-galactosidase from the psychrotolerant antarctic bacterium Arthrobacter sp. C2-2. Enz Microb, Technol 2003, 33:836-844.
    • (2003) Enz Microb, Technol , vol.33 , pp. 836-844
    • Karasova-Lipovova, P.1    Strnad, H.2    Spiwok, V.3    Mala, S.4    Kralova, B.5    Russell, N.6
  • 55
    • 79953286439 scopus 로고    scopus 로고
    • Molecular characterization of cold-inducible beta-galactosidase from Arthrobacter sp. ON14 isolated from Antarctica
    • Xu K, Tang X, Gai Y, Mehmood M, Xiao X, Wang F. Molecular characterization of cold-inducible beta-galactosidase from Arthrobacter sp. ON14 isolated from Antarctica. J Microbiol Biotechnol 2011, 21:236-242.
    • (2011) J Microbiol Biotechnol , vol.21 , pp. 236-242
    • Xu, K.1    Tang, X.2    Gai, Y.3    Mehmood, M.4    Xiao, X.5    Wang, F.6
  • 56
    • 83255162703 scopus 로고    scopus 로고
    • A novel cold-active β-D-galactosidase from the Paracoccus sp. 32d-gene cloning, purification and characterization
    • 10.1186/1475-2859-10-108, 3268748, 22166118
    • Wierzbicka-Woś A, Cieśliński H, Wanarska M, Kozłowska-Tylingo K, Hildebrandt P, Kur J. A novel cold-active β-D-galactosidase from the Paracoccus sp. 32d-gene cloning, purification and characterization. Microb Cell Fact 2011, 10:108. 10.1186/1475-2859-10-108, 3268748, 22166118.
    • (2011) Microb Cell Fact , vol.10 , pp. 108
    • Wierzbicka-Woś, A.1    Cieśliński, H.2    Wanarska, M.3    Kozłowska-Tylingo, K.4    Hildebrandt, P.5    Kur, J.6
  • 57
    • 79551495193 scopus 로고    scopus 로고
    • A novel organic solvent tolerant protease from a newly isolated Geomicrobium sp. EMB2 (MTCC 10310): production optimization by response surface methodology
    • 10.1016/j.nbt.2010.10.007, 20970529
    • Karan R, Singh SP, Kapoor S, Khare SK. A novel organic solvent tolerant protease from a newly isolated Geomicrobium sp. EMB2 (MTCC 10310): production optimization by response surface methodology. N Biotechnol 2011, 28:136-145. 10.1016/j.nbt.2010.10.007, 20970529.
    • (2011) N Biotechnol , vol.28 , pp. 136-145
    • Karan, R.1    Singh, S.P.2    Kapoor, S.3    Khare, S.K.4
  • 58
    • 33846409885 scopus 로고    scopus 로고
    • Effect of organic solvents on the activity and stability of an extracellular protease secreted by the haloalkaliphilic archaeon Natrialba magadii
    • 10.1007/s10295-006-0174-4, 17024426
    • Ruiz DM, De Castro RE. Effect of organic solvents on the activity and stability of an extracellular protease secreted by the haloalkaliphilic archaeon Natrialba magadii. J Ind Microbiol Biotechnol 2007, 34:111-115. 10.1007/s10295-006-0174-4, 17024426.
    • (2007) J Ind Microbiol Biotechnol , vol.34 , pp. 111-115
    • Ruiz, D.M.1    De Castro, R.E.2
  • 59
    • 14644442998 scopus 로고    scopus 로고
    • Organic solvent tolerance of halophilic α-amylase from a Haloarchaeon, Haloarcula sp. strain S-1
    • 10.1007/s00792-004-0423-2, 15378403
    • Fukushima T, Mizuki T, Echigo A, Inoue A, Usami R. Organic solvent tolerance of halophilic α-amylase from a Haloarchaeon, Haloarcula sp. strain S-1. Extremophiles 2005, 9:85-89. 10.1007/s00792-004-0423-2, 15378403.
    • (2005) Extremophiles , vol.9 , pp. 85-89
    • Fukushima, T.1    Mizuki, T.2    Echigo, A.3    Inoue, A.4    Usami, R.5
  • 60
    • 0038035415 scopus 로고    scopus 로고
    • Microwave-assisted synthesis of galacto-oligosaccharides from lactose with immobilized beta-galactosidase from Kluyveromyces lactis
    • 10.1023/A:1023060030558, 12882156
    • Maugard T, Gaunt D, Legoy MD, Besson T. Microwave-assisted synthesis of galacto-oligosaccharides from lactose with immobilized beta-galactosidase from Kluyveromyces lactis. Biotechnol Lett 2003, 25:623-629. 10.1023/A:1023060030558, 12882156.
    • (2003) Biotechnol Lett , vol.25 , pp. 623-629
    • Maugard, T.1    Gaunt, D.2    Legoy, M.D.3    Besson, T.4
  • 61
    • 79952200265 scopus 로고    scopus 로고
    • The effects of organic solvents on the efficiency and regioselectivity of N-acetyl-lactosamine synthesis, using the β-galactosidase from Bacillus circulans in hydro-organic media
    • 10.1002/btpr.445, 20568279
    • Bridiau N, Issaoui N, Maugard T. The effects of organic solvents on the efficiency and regioselectivity of N-acetyl-lactosamine synthesis, using the β-galactosidase from Bacillus circulans in hydro-organic media. Biotechnol Prog 2010, 26:1278-1289. 10.1002/btpr.445, 20568279.
    • (2010) Biotechnol Prog , vol.26 , pp. 1278-1289
    • Bridiau, N.1    Issaoui, N.2    Maugard, T.3
  • 62
    • 0031172560 scopus 로고    scopus 로고
    • Solvent effect on enzyme-catalyzed synthesis of β-D-glucosides using the reverse hydrolysis method: Application to the preparative-scale synthesis of 2-hydroxybenzyl and octyl β-D-glucopyranosides
    • Vic G, Thomas D, Crout DHG. Solvent effect on enzyme-catalyzed synthesis of β-D-glucosides using the reverse hydrolysis method: Application to the preparative-scale synthesis of 2-hydroxybenzyl and octyl β-D-glucopyranosides. Enzym Microb Tech 1997, 20:597-603.
    • (1997) Enzym Microb Tech , vol.20 , pp. 597-603
    • Vic, G.1    Thomas, D.2    Crout, D.H.G.3
  • 64
    • 0036491184 scopus 로고    scopus 로고
    • Searching for liquid water in Europa by using surface observatories
    • Khurana KK, Kivelson MG, Russell CT. Searching for liquid water in Europa by using surface observatories. Astrobiol 2002, 2:93-103.
    • (2002) Astrobiol , vol.2 , pp. 93-103
    • Khurana, K.K.1    Kivelson, M.G.2    Russell, C.T.3
  • 65
    • 4444254210 scopus 로고    scopus 로고
    • The search for life on Europa: limiting environmental factors, potential habitats, and Earth analogues
    • Marion GM, Fritsen CH, Eicken H, Payne MC. The search for life on Europa: limiting environmental factors, potential habitats, and Earth analogues. Astrobiol 2003, 3:785-811.
    • (2003) Astrobiol , vol.3 , pp. 785-811
    • Marion, G.M.1    Fritsen, C.H.2    Eicken, H.3    Payne, M.C.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.