메뉴 건너뛰기




Volumn 92, Issue 13, 2012, Pages 2575-2580

Halophilic hydrolases as a new tool for the biotechnological industries

Author keywords

Biochemical characteristics; Halophilic enzymes; Halophilic micro organisms; Industry

Indexed keywords

HYDROLASE;

EID: 84866173954     PISSN: 00225142     EISSN: 10970010     Source Type: Journal    
DOI: 10.1002/jsfa.5860     Document Type: Review
Times cited : (107)

References (70)
  • 1
    • 84873484249 scopus 로고    scopus 로고
    • Food and industrial microbiology. [Online]. Available: Accessed [10 October 2011].
    • Bhalla-Chad T, Nand-Sharma N and Sharma M, Food and industrial microbiology. [Online]. Available: http://nsdl.niscair.res.in/bitstream/123456789/129/1/Metabolites.pdf Accessed [10 October 2011].
    • Bhalla-Chad, T.1    Nand-Sharma, N.2    Sharma, M.3
  • 3
    • 77951664490 scopus 로고    scopus 로고
    • Extracellular hydrolytic enzymes of halophilic bacteria isolated from a subterranean rock salt crystal
    • Cojoc R, Merciu S, Popescu G, Dumitru L, Kamekura M and Enache M, Extracellular hydrolytic enzymes of halophilic bacteria isolated from a subterranean rock salt crystal. Rom Biotechnol Lett 14: 4658-4664 (2009).
    • (2009) Rom Biotechnol Lett , vol.14 , pp. 4658-4664
    • Cojoc, R.1    Merciu, S.2    Popescu, G.3    Dumitru, L.4    Kamekura, M.5    Enache, M.6
  • 4
    • 80052667311 scopus 로고    scopus 로고
    • Diversity of hydrolytic enzymes in haloarchaeal strains isolated from salt lake
    • Makhdoumi
    • Makhdoumi Kakhki A, Amoozegar MA and Mahmodi Khaledi E, Diversity of hydrolytic enzymes in haloarchaeal strains isolated from salt lake. Int J Environ Sci Technol 8: 705-714 (2011).
    • (2011) Int J Environ Sci Technol , vol.8 , pp. 705-714
    • Kakhki, A.1    Amoozegar, M.A.2    Mahmodi Khaledi, E.3
  • 5
    • 0034913744 scopus 로고    scopus 로고
    • Biotechnological uses of archaeal extremoenzymes
    • Eichler J, Biotechnological uses of archaeal extremoenzymes. Biotechnol Adv 19: 261-278 (2001).
    • (2001) Biotechnol Adv , vol.19 , pp. 261-278
    • Eichler, J.1
  • 6
    • 84888023192 scopus 로고    scopus 로고
    • Halophilic microorganisms and their potential applied in the biotechnology
    • Meseguer SI, Halophilic microorganisms and their potential applied in the biotechnology. Cienc Invest 7: 13-17 (2004).
    • (2004) Cienc Invest , vol.7 , pp. 13-17
    • Meseguer, S.I.1
  • 7
    • 0037241080 scopus 로고    scopus 로고
    • Diversity of moderately halophilic bacteria producing extracellular hydrolytic enzymes
    • Sánchez-Porro C, Martín S, Mellado E and Ventosa A, Diversity of moderately halophilic bacteria producing extracellular hydrolytic enzymes. J Appl Microbiol 94: 295-300 (2003).
    • (2003) J Appl Microbiol , vol.94 , pp. 295-300
    • Sánchez-Porro, C.1    Martín, S.2    Mellado, E.3    Ventosa, A.4
  • 8
    • 57649210759 scopus 로고    scopus 로고
    • Characterization of extracellular esterases and lipases activities from five halophilic archaeal strains
    • Ozcan B, Ozylmaz G, Cokmus C and Caliskan M, Characterization of extracellular esterases and lipases activities from five halophilic archaeal strains. J Ind Microbiol Biotechnol 36: 105-110 (2009).
    • (2009) J Ind Microbiol Biotechnol , vol.36 , pp. 105-110
    • Ozcan, B.1    Ozylmaz, G.2    Cokmus, C.3    Caliskan, M.4
  • 9
    • 61349198759 scopus 로고    scopus 로고
    • Screening and isolation of halophilic bacteria producing extracellular hydrolases from Howz Soltan Lake, Iran
    • Rohban R, Amoozegar MA and Ventosa A, Screening and isolation of halophilic bacteria producing extracellular hydrolases from Howz Soltan Lake, Iran. J Ind Microbiol Biotechnol 36: 333-340 (2009).
    • (2009) J Ind Microbiol Biotechnol , vol.36 , pp. 333-340
    • Rohban, R.1    Amoozegar, M.A.2    Ventosa, A.3
  • 11
    • 0004294399 scopus 로고    scopus 로고
    • 10th edn). Pearson Prentice Hall, Mexico, 8, 28, 29, 159, 161, 444-1, 8, 28, 29, 159, 161, 448
    • Madigan MT, Martinko JM and Parker J, Brock Biology of Microorganisms (10th edn). Pearson Prentice Hall, Mexico, pp. 1, 8, 28, 29, 159, 161, 444-448 (2004).
    • (2004) Brock Biology of Microorganisms , pp. 1
    • Madigan, M.T.1    Martinko, J.M.2    Parker, J.3
  • 14
    • 0016139829 scopus 로고
    • Salt dependent properties of proteins from extremely halophilic bacteria
    • Lanyi JK, Salt dependent properties of proteins from extremely halophilic bacteria. Bacteriol Rev 38: 272-290 (1974).
    • (1974) Bacteriol Rev , vol.38 , pp. 272-290
    • Lanyi, J.K.1
  • 15
    • 0042861743 scopus 로고    scopus 로고
    • Strategies of adaptation of halophilic microorganisms and Debaromyces hansenii (halophilic yeast)
    • González JC and Peña A, Strategies of adaptation of halophilic microorganisms and Debaromyces hansenii (halophilic yeast). Rev Latinoam Microbiol 44: 137-156 (2002).
    • (2002) Rev Latinoam Microbiol , vol.44 , pp. 137-156
    • González, J.C.1    Peña, A.2
  • 16
    • 0029027430 scopus 로고
    • A single acidic amino acid mutation enhances the halophilic behavior of malate dehydrogenase from Haloarcula marismortui
    • Madern D, Pfister C and Zaccai G, A single acidic amino acid mutation enhances the halophilic behavior of malate dehydrogenase from Haloarcula marismortui. Eur J Biochem 230: 1088-1095 (1995).
    • (1995) Eur J Biochem , vol.230 , pp. 1088-1095
    • Madern, D.1    Pfister, C.2    Zaccai, G.3
  • 17
    • 0034166764 scopus 로고    scopus 로고
    • Halophilic adaptation of enzymes
    • Madern D, Ebel C and Zaccai G, Halophilic adaptation of enzymes. Extremophiles 4: 91-98 (2000).
    • (2000) Extremophiles , vol.4 , pp. 91-98
    • Madern, D.1    Ebel, C.2    Zaccai, G.3
  • 18
    • 84866145363 scopus 로고    scopus 로고
    • Hydrolytic enzymes of halophilic microorganisms and their economic values
    • Enache M and Kamekura M, Hydrolytic enzymes of halophilic microorganisms and their economic values. Rom Biotechnol Lett 47: 47-59 (2010).
    • (2010) Rom Biotechnol Lett , vol.47 , pp. 47-59
    • Enache, M.1    Kamekura, M.2
  • 19
    • 84873484655 scopus 로고    scopus 로고
    • Halotolerant bacteria isolated of Pilluana, San Martín salines with lipolytic activity
    • Flores-Fernández M, Zavaleta A and Chávez-Hidalgo L, Halotolerant bacteria isolated of Pilluana, San Martín salines with lipolytic activity. Cienc Invest 13: 87-91 (2010).
    • (2010) Cienc Invest , vol.13 , pp. 87-91
    • Flores-Fernández, M.1    Zavaleta, A.2    Chávez-Hidalgo, L.3
  • 20
    • 0002176470 scopus 로고
    • Life in high salt and solute concentration
    • ed. by Kushner DJ. Academic Press, London
    • Kushner DJ, Life in high salt and solute concentration, in Microbial Life in Extreme Environment, ed. by Kushner DJ. Academic Press, London, pp. 317-368 (1978).
    • (1978) Microbial Life in Extreme Environment , pp. 317-368
    • Kushner, D.J.1
  • 21
    • 0002772862 scopus 로고    scopus 로고
    • Sodium stress
    • ed. by Stroz G and Hengge-Aronis R. ASM Press, Washington, DC
    • Padan C and Krulwich TA, Sodium stress, in Bacterial Stress Responses, ed. by Stroz G and Hengge-Aronis R. ASM Press, Washington, DC, pp. 117-130 (2000).
    • (2000) Bacterial Stress Responses , pp. 117-130
    • Padan, C.1    Krulwich, T.A.2
  • 22
    • 0030696842 scopus 로고    scopus 로고
    • Intracellular proteolytic activity of the haloalkiliphilic archeon Natrococcus occultus, effect of starvation
    • Seitz MKH, Studdert CA, Sánchez JJ and De Castro RE, Intracellular proteolytic activity of the haloalkiliphilic archeon Natrococcus occultus, effect of starvation. J Basic Microbiol 37: 313-322 (1997).
    • (1997) J Basic Microbiol , vol.37 , pp. 313-322
    • Seitz, M.K.H.1    Studdert, C.A.2    Sánchez, J.J.3    De Castro, R.E.4
  • 24
    • 0019618128 scopus 로고
    • Structure and activity of malate dehydrogenase from the extreme halophilic bacteria of the Dead Sea
    • Pundak S and Eisenberg H, Structure and activity of malate dehydrogenase from the extreme halophilic bacteria of the Dead Sea. Eur J Biochem 118: 463-498 (1981).
    • (1981) Eur J Biochem , vol.118 , pp. 463-498
    • Pundak, S.1    Eisenberg, H.2
  • 25
    • 0033051987 scopus 로고    scopus 로고
    • Harmonic behavior of trehalose coated carbon-monoxy-myglobin at high temperature
    • Cordone L, Ferrand M, Vitrano E and Zaccai G, Harmonic behavior of trehalose coated carbon-monoxy-myglobin at high temperature. Biophys J 76: 1043-1047 (1999).
    • (1999) Biophys J , vol.76 , pp. 1043-1047
    • Cordone, L.1    Ferrand, M.2    Vitrano, E.3    Zaccai, G.4
  • 26
    • 77955325659 scopus 로고    scopus 로고
    • Exploring research frontiers in microbiology: recent advances in halophilic and thermophilic extremophiles
    • Averhoff B and Müller V, Exploring research frontiers in microbiology: recent advances in halophilic and thermophilic extremophiles. Res Microbiol 161: 506-514 (2010).
    • (2010) Res Microbiol , vol.161 , pp. 506-514
    • Averhoff, B.1    Müller, V.2
  • 27
    • 79952392152 scopus 로고    scopus 로고
    • Gene identification and molecular characterization of solvent stable protease from a moderately haloalkaliphilic bacterium, Geomicrobium sp. EMB2
    • Karan R, Mohan-Singh RK, Kappor S and Khare K, Gene identification and molecular characterization of solvent stable protease from a moderately haloalkaliphilic bacterium, Geomicrobium sp. EMB2. J Microbiol Biotechnol 21: 129-135 (2011).
    • (2011) J Microbiol Biotechnol , vol.21 , pp. 129-135
    • Karan, R.1    Mohan-Singh, R.K.2    Kappor, S.3    Khare, K.4
  • 28
    • 0344863187 scopus 로고    scopus 로고
    • Correlation between thermal motions and functional conformational changes in bacteriorhodopsin: a neutrons scattering study at different hydration levels
    • Lenhert U, Réat V, Weik M, Zaccai G and Pfister C, Correlation between thermal motions and functional conformational changes in bacteriorhodopsin: a neutrons scattering study at different hydration levels. Biophys J 75: 1945-1952 (1998).
    • (1998) Biophys J , vol.75 , pp. 1945-1952
    • Lenhert, U.1    Réat, V.2    Weik, M.3    Zaccai, G.4    Pfister, C.5
  • 29
    • 33751408436 scopus 로고    scopus 로고
    • Interactions between macromolecules and ions: the Hofmeister series
    • Zang Y and Cremer PS, Interactions between macromolecules and ions: the Hofmeister series. Curr Opin Chem Biol 10: 658-663 (2006).
    • (2006) Curr Opin Chem Biol , vol.10 , pp. 658-663
    • Zang, Y.1    Cremer, P.S.2
  • 30
    • 0032484699 scopus 로고    scopus 로고
    • Protein-protein and protein-salt interactions in aqueous protein solutions containing concentrated electrolytes
    • Curtis RA, Prausnitz JM and Blanch HM, Protein-protein and protein-salt interactions in aqueous protein solutions containing concentrated electrolytes. Biotechnol Bioeng 57: 11-21 (1998).
    • (1998) Biotechnol Bioeng , vol.57 , pp. 11-21
    • Curtis, R.A.1    Prausnitz, J.M.2    Blanch, H.M.3
  • 31
    • 0019877658 scopus 로고
    • Structural stability of halophilic proteins
    • Rao JM and Argos P, Structural stability of halophilic proteins. Biochemistry 20: 6536-6543 (1981).
    • (1981) Biochemistry , vol.20 , pp. 6536-6543
    • Rao, J.M.1    Argos, P.2
  • 32
    • 77950646412 scopus 로고    scopus 로고
    • Diversity and industrial potential of hydrolase-producing halophilic/halotolerant eubacteria
    • Setati EM, Diversity and industrial potential of hydrolase-producing halophilic/halotolerant eubacteria. Afr J Biotechnol 9: 1555-1560 (2010).
    • (2010) Afr J Biotechnol , vol.9 , pp. 1555-1560
    • Setati, E.M.1
  • 33
    • 33748588406 scopus 로고    scopus 로고
    • Optimization of culture conditions for the production of haloalkaliphilic thermostable protease from an extremely halophilic archeon Halogeometricum sp. TSS101
    • Vidyasagar M, Prakash SB and Sreeramulu K, Optimization of culture conditions for the production of haloalkaliphilic thermostable protease from an extremely halophilic archeon Halogeometricum sp. TSS101. Lett Appl Microbiol 43: 385-391 (2006).
    • (2006) Lett Appl Microbiol , vol.43 , pp. 385-391
    • Vidyasagar, M.1    Prakash, S.B.2    Sreeramulu, K.3
  • 34
    • 80051547257 scopus 로고    scopus 로고
    • A novel thermostable and halostable carboxymethylcellulase from marine bacterium Bacillus licheniformis AU01
    • Annamalai N, Thavasi R, Vijayalakshmi S and Balasubramanian T, A novel thermostable and halostable carboxymethylcellulase from marine bacterium Bacillus licheniformis AU01. World J Microbiol Biotechnol 27: 2111-2115 (2011).
    • (2011) World J Microbiol Biotechnol , vol.27 , pp. 2111-2115
    • Annamalai, N.1    Thavasi, R.2    Vijayalakshmi, S.3    Balasubramanian, T.4
  • 35
    • 85027930333 scopus 로고    scopus 로고
    • Extracellular production of beta-amylase by halophilic isolate Halobacillus sp. LY9
    • Li X and Yu H, Extracellular production of beta-amylase by halophilic isolate Halobacillus sp. LY9. J Ind Microbiol Biotechnol 38: 1837-1843 (2011).
    • (2011) J Ind Microbiol Biotechnol , vol.38 , pp. 1837-1843
    • Li, X.1    Yu, H.2
  • 36
    • 84655176344 scopus 로고    scopus 로고
    • Alkaline inulinase production by a newly isolated bacterium Marinimicrobium sp. LS-A18 and inulin hydrolysis by the enzyme
    • Ai-Xia L, Li-Zhoung G and Wei-Doung L, Alkaline inulinase production by a newly isolated bacterium Marinimicrobium sp. LS-A18 and inulin hydrolysis by the enzyme. World J Microbiol Biotechnol 28: 81-89 (2012).
    • (2012) World J Microbiol Biotechnol , vol.28 , pp. 81-89
    • Ai-Xia, L.1    Li-Zhoung, G.2    Wei-Doung, L.3
  • 37
    • 11144243173 scopus 로고    scopus 로고
    • The biocatalytic potential of extremophiles and extremoenzymes
    • Gomes J and Steiner W, The biocatalytic potential of extremophiles and extremoenzymes. Food Technol Biotechnol 42: 223-235 (2004).
    • (2004) Food Technol Biotechnol , vol.42 , pp. 223-235
    • Gomes, J.1    Steiner, W.2
  • 38
    • 72449203758 scopus 로고    scopus 로고
    • Biodiversity of poly-extremophilic bacteria: does combining the extremes of high salt, alkaline pH and elevated temperature approach a physico-chemical boundary for life?
    • Bowers KJ, Mesbah NM and Wiegel J, 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 Syst 5: 9-17 (2009).
    • (2009) Saline Syst , vol.5 , pp. 9-17
    • Bowers, K.J.1    Mesbah, N.M.2    Wiegel, J.3
  • 39
    • 1842535955 scopus 로고    scopus 로고
    • Stability and enzymatic studies of glucose dehydrogenase from the archeon Haloferax mediterranei in reverse micelles
    • Pire C, Marhuenda-Egea FC, Esclapez J, Alcaraz L, Ferrer J and Bonete MJ, Stability and enzymatic studies of glucose dehydrogenase from the archeon Haloferax mediterranei in reverse micelles. Biocatal Biotransform 22: 17-23 (2011).
    • (2011) Biocatal Biotransform , vol.22 , pp. 17-23
    • Pire, C.1    Marhuenda-Egea, F.C.2    Esclapez, J.3    Alcaraz, L.4    Ferrer, J.5    Bonete, M.J.6
  • 40
    • 77953700376 scopus 로고    scopus 로고
    • Industrial and environmental application of halophilic microorganisms
    • Oren A, Industrial and environmental application of halophilic microorganisms. Environ Technol 31: 825-834 (2010).
    • (2010) Environ Technol , vol.31 , pp. 825-834
    • Oren, A.1
  • 41
    • 84866167172 scopus 로고    scopus 로고
    • Enzyme vs. extremoenzyme, what makes extremoenzymes function under harsh conditions?
    • Kumar S, Enzyme vs. extremoenzyme, what makes extremoenzymes function under harsh conditions? Resonance 3: 32-40 (1998).
    • (1998) Resonance , vol.3 , pp. 32-40
    • Kumar, S.1
  • 43
    • 14644442998 scopus 로고    scopus 로고
    • Organic solvent tolerance of halophilic α-amylase from a haloarchaeon, Haloarcula sp. strain S-1
    • Fukishima T, Mizuki T, Echigo A, Inoue A and Usami R, Organic solvent tolerance of halophilic α-amylase from a haloarchaeon, Haloarcula sp. strain S-1. Extremophiles 9: 321-331 (2005).
    • (2005) Extremophiles , vol.9 , pp. 321-331
    • Fukishima, T.1    Mizuki, T.2    Echigo, A.3    Inoue, A.4    Usami, R.5
  • 44
    • 0014864156 scopus 로고
    • Properties of the amylase from Halobacterium halobium
    • Good WA and Hartman PA, Properties of the amylase from Halobacterium halobium. J Bacteriol 104(1): 601-603 (1970).
    • (1970) J Bacteriol , vol.104 , Issue.1 , pp. 601-603
    • Good, W.A.1    Hartman, P.A.2
  • 45
    • 0026628849 scopus 로고
    • Haloalkaliphilic maltotriose-forming α-amylase from the archeobacterium Natrococcus sp. strain Ah-36
    • Kobayashi T, Kamai H, Aono R, Hirikoshi K and Kudo T, Haloalkaliphilic maltotriose-forming α-amylase from the archeobacterium Natrococcus sp. strain Ah-36. J Bacteriol 174: 3439-3444 (1992).
    • (1992) J Bacteriol , vol.174 , pp. 3439-3444
    • Kobayashi, T.1    Kamai, H.2    Aono, R.3    Hirikoshi, K.4    Kudo, T.5
  • 47
    • 0033955301 scopus 로고    scopus 로고
    • Production and biochemical characterization of an α-amylase from the moderate halophile Halomonas meridiana
    • Coronado MJ, Vargas C, Hofmeister J, Ventosa A and Nieto J, Production and biochemical characterization of an α-amylase from the moderate halophile Halomonas meridiana. FEMS Microbiol Lett 183: 67-71 (2000).
    • (2000) FEMS Microbiol Lett , vol.183 , pp. 67-71
    • Coronado, M.J.1    Vargas, C.2    Hofmeister, J.3    Ventosa, A.4    Nieto, J.5
  • 49
    • 79952677403 scopus 로고    scopus 로고
    • Isolation, purification and characterization of haloalkaline xylanase from a marine Bacillus pumilus strain, GESF-1
    • Menon G, Mody K, Keshri J and Jha B, Isolation, purification and characterization of haloalkaline xylanase from a marine Bacillus pumilus strain, GESF-1. Biotechnol Bioprocess Eng 15: 998-1005 (2010).
    • (2010) Biotechnol Bioprocess Eng , vol.15 , pp. 998-1005
    • Menon, G.1    Mody, K.2    Keshri, J.3    Jha, B.4
  • 50
    • 0037089443 scopus 로고    scopus 로고
    • Enzymatic properties, crystallization and deduced amino acid sequence of an alkaline endoglucanase from Bacillus circulans
    • Hakamada Y, Endo K, Takisawa S, Kobayashi T, Shirai T, Yamane T, et al, Enzymatic properties, crystallization and deduced amino acid sequence of an alkaline endoglucanase from Bacillus circulans. Biochim Biophys Acta 1570: 174-180 (2002).
    • (2002) Biochim Biophys Acta , vol.1570 , pp. 174-180
    • Hakamada, Y.1    Endo, K.2    Takisawa, S.3    Kobayashi, T.4    Shirai, T.5    Yamane, T.6
  • 51
    • 1842503015 scopus 로고    scopus 로고
    • Purification and characterization of alkaline cellulase produced by a novel isolate Bacillus sphaericus JS1
    • Singh J, Batra N and Sobti RC, Purification and characterization of alkaline cellulase produced by a novel isolate Bacillus sphaericus JS1. J Ind Microbiol Biotechnol 31: 51-56 (2004).
    • (2004) J Ind Microbiol Biotechnol , vol.31 , pp. 51-56
    • Singh, J.1    Batra, N.2    Sobti, R.C.3
  • 52
    • 49449093938 scopus 로고    scopus 로고
    • A new moderately halo-alkaliphilic, thermo-stable endoglucanase from moderately halophilic Bacillus sp. C14 isolated from Van Soda Lake
    • Ashabil A and Burhan A, A new moderately halo-alkaliphilic, thermo-stable endoglucanase from moderately halophilic Bacillus sp. C14 isolated from Van Soda Lake. Int J Agric Biol 10: 369-374 (2008).
    • (2008) Int J Agric Biol , vol.10 , pp. 369-374
    • Ashabil, A.1    Burhan, A.2
  • 53
    • 33745138590 scopus 로고    scopus 로고
    • Preliminary characterization of a lipolytic activity from an extremely halophilic archaeon Natrococcus sp
    • Boutaiba S, Bathatnagar T, Hacence H, Mitchell DA and Baratti JC, Preliminary characterization of a lipolytic activity from an extremely halophilic archaeon Natrococcus sp. J Mol Catal B 41: 21-26 (2006).
    • (2006) J Mol Catal B , vol.41 , pp. 21-26
    • Boutaiba, S.1    Bathatnagar, T.2    Hacence, H.3    Mitchell, D.A.4    Baratti, J.C.5
  • 54
    • 47649103512 scopus 로고    scopus 로고
    • Production of an extracellular thermo-halophilic lipase from a moderately halophilic bacterium, Salinivibrio sp. strain SA-2
    • Amoozegar MA, Salehghamari E, Khajeh K, Kabiri M and Naddaf S, Production of an extracellular thermo-halophilic lipase from a moderately halophilic bacterium, Salinivibrio sp. strain SA-2. J Basic Microbiol 48: 160-167 (2008).
    • (2008) J Basic Microbiol , vol.48 , pp. 160-167
    • Amoozegar, M.A.1    Salehghamari, E.2    Khajeh, K.3    Kabiri, M.4    Naddaf, S.5
  • 55
    • 84856349841 scopus 로고    scopus 로고
    • Characterization of recombinant family 18 chitinase from extremely halophilic archaeon Halobacterium salinarum strain NRC-1
    • Hatori Y, Sato M, Orishimo K, Yatsunami R, Endo K, Fuki T, et al, Characterization of recombinant family 18 chitinase from extremely halophilic archaeon Halobacterium salinarum strain NRC-1. Chitin Chitosan Res 12: 201 (2006).
    • (2006) Chitin Chitosan Res , vol.12 , pp. 201
    • Hatori, Y.1    Sato, M.2    Orishimo, K.3    Yatsunami, R.4    Endo, K.5    Fuki, T.6
  • 56
    • 77952236980 scopus 로고    scopus 로고
    • Production and partial characterization of chitinase from a halotolerant Planococcus rifitoensis strain M2-26
    • Essghaeir B, Rouassi M, Boudabous A, Jijkali H and Sadfi-Zouaoui N, Production and partial characterization of chitinase from a halotolerant Planococcus rifitoensis strain M2-26. World J Microbiol Biotechnol 26(6): 977-984 (2010).
    • (2010) World J Microbiol Biotechnol , vol.26 , Issue.6 , pp. 977-984
    • Essghaeir, B.1    Rouassi, M.2    Boudabous, A.3    Jijkali, H.4    Sadfi-Zouaoui, N.5
  • 57
    • 0036160908 scopus 로고    scopus 로고
    • Diversity of halophilic microorganisms: environments, phylogeny, physiology and applications
    • Oren A, Diversity of halophilic microorganisms: environments, phylogeny, physiology and applications. J Ind Microbiol Biotechnol 28: 56-63 (2002).
    • (2002) J Ind Microbiol Biotechnol , vol.28 , pp. 56-63
    • Oren, A.1
  • 58
    • 0017893492 scopus 로고
    • Properties of the halophilic nuclease of a moderate halophile, Microcococcus varians subsp. halophilus
    • Kamekura M and Onishi H, Properties of the halophilic nuclease of a moderate halophile, Microcococcus varians subsp. halophilus. J Bacteriol 133: 59-65 (1979).
    • (1979) J Bacteriol , vol.133 , pp. 59-65
    • Kamekura, M.1    Onishi, H.2
  • 59
    • 0016139745 scopus 로고
    • Halophilic nuclease from a moderately halophilic Micrococcus varians
    • Kamekura M and Onishi H, Halophilic nuclease from a moderately halophilic Micrococcus varians. J Bacteriol 119: 339-344 (1974).
    • (1974) J Bacteriol , vol.119 , pp. 339-344
    • Kamekura, M.1    Onishi, H.2
  • 60
    • 0018164297 scopus 로고
    • Purification and properties of amylase produced by a moderately halophilic Acetinobacter sp
    • Onishi H and Hidaka O, Purification and properties of amylase produced by a moderately halophilic Acetinobacter sp. Can J Microbiol 24: 1017-1023 (1978).
    • (1978) Can J Microbiol , vol.24 , pp. 1017-1023
    • Onishi, H.1    Hidaka, O.2
  • 61
    • 0034694154 scopus 로고    scopus 로고
    • Enzymatic synthesis of oligosaccharides: product removal during a kinetically controlled reaction
    • Boon MA, Van't Riet K and Janssen AE, Enzymatic synthesis of oligosaccharides: product removal during a kinetically controlled reaction. Biotechnol Bioeng 70: 411-420 (2000).
    • (2000) Biotechnol Bioeng , vol.70 , pp. 411-420
    • Boon, M.A.1    Van't Riet, K.2    Janssen, A.E.3
  • 63
    • 0030796841 scopus 로고    scopus 로고
    • β-Agarase from Pseudomonas sp. W7: purification of the recombinant enzyme from Escherichia coli and the effects of salt on its activity
    • Ha JC, Kim GT, Kim SK, Oh TK, Yu JH and Kong IS, β-Agarase from Pseudomonas sp. W7: purification of the recombinant enzyme from Escherichia coli and the effects of salt on its activity. Biotechnol Appl Biochem 26: 1-6 (1997).
    • (1997) Biotechnol Appl Biochem , vol.26 , pp. 1-6
    • Ha, J.C.1    Kim, G.T.2    Kim, S.K.3    Oh, T.K.4    Yu, J.H.5    Kong, I.S.6
  • 64
    • 84866158556 scopus 로고
    • Agarase system from Alteromonas strain 2-40. US Patent 5418156
    • Stosz SK, Weiner RM and Coyne VE, Agarase system from Alteromonas strain 2-40. US Patent 5418156 (1995).
    • (1995)
    • Stosz, S.K.1    Weiner, R.M.2    Coyne, V.E.3
  • 65
    • 0031763685 scopus 로고    scopus 로고
    • Alterococcus agarolyticus, gene.nov., sp.nov., a halophilic thermophilic bacterium capable of agar degradation
    • Shieh W and Jean WD, Alterococcus agarolyticus, gene.nov., sp.nov., a halophilic thermophilic bacterium capable of agar degradation. Can J Microbiol 44: 637-645 (1998).
    • (1998) Can J Microbiol , vol.44 , pp. 637-645
    • Shieh, W.1    Jean, W.D.2
  • 66
    • 0028414129 scopus 로고
    • Catalytic properties and potential of an extracellular protease from an extreme halophile
    • Ryu K, Kim J and Dordick JS, Catalytic properties and potential of an extracellular protease from an extreme halophile. Enzyme Microb Technol 16: 266-275 (1994).
    • (1994) Enzyme Microb Technol , vol.16 , pp. 266-275
    • Ryu, K.1    Kim, J.2    Dordick, J.S.3
  • 68
    • 33748588406 scopus 로고    scopus 로고
    • Optimization of culture conditions for the production of haloalkaliphilic thermostable protease from an extremely halophilic archeon Halogeometricum sp. TSS101
    • Vidyasagar M, Prakash SB and Sreeramulu K, Optimization of culture conditions for the production of haloalkaliphilic thermostable protease from an extremely halophilic archeon Halogeometricum sp. TSS101. Lett Appl Microbiol 43: 385-391 (2006).
    • (2006) Lett Appl Microbiol , vol.43 , pp. 385-391
    • Vidyasagar, M.1    Prakash, S.B.2    Sreeramulu, K.3
  • 69
    • 84862143520 scopus 로고    scopus 로고
    • Function and biotechnology of extremophilic enzymes in low water activity
    • Karan R, Capes MD and DasSarma S, Function and biotechnology of extremophilic enzymes in low water activity. Aquat Biosyst 8: 1-15 (2012).
    • (2012) Aquat Biosyst , vol.8 , pp. 1-15
    • Karan, R.1    Capes, M.D.2    DasSarma, S.3
  • 70
    • 0026545026 scopus 로고
    • Isolation and characterization of anextremely halophilic archaeobacterium from traditionally fermented Thai fish sauce (nam pla)
    • Thongthai C, McGenity TJ, Suntinanalert P and Grant WD, Isolation and characterization of anextremely halophilic archaeobacterium from traditionally fermented Thai fish sauce (nam pla), Lett Appl Microbiol 14: 111-114 (1992).
    • (1992) Lett Appl Microbiol , vol.14 , pp. 111-114
    • Thongthai, C.1    McGenity, T.J.2    Suntinanalert, P.3    Grant, W.D.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.