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Volumn 2, Issue 1, 2006, Pages 51-57

Purification and characterization of a thermostable, haloalkaliphilic extracellular serine protease from the extreme halophilic archaeon Halogeometricum borinquense strain TSS101

Author keywords

Calcium chloride; Cetyltrimethylammonium bromide; Halophilic serine protease; Metal ions; Osmolytes; Protease inhibitors

Indexed keywords

ARCHAEA; HALOGEOMETRICUM BORINQUENSE;

EID: 33748106363     PISSN: 14723646     EISSN: None     Source Type: Journal    
DOI: 10.1155/2006/430763     Document Type: Article
Times cited : (58)

References (36)
  • 1
    • 33751155047 scopus 로고
    • Enzymes from microorganisms in extreme environments
    • Adams, M.W.W. and R.M. Kelly. 1995. Enzymes from microorganisms in extreme environments. Chem. Eng. News 73:32-42.
    • (1995) Chem. Eng. News , vol.73 , pp. 32-42
    • Adams, M.W.W.1    Kelly, R.M.2
  • 2
    • 0029239715 scopus 로고
    • Thermostability of high activity alkaline protease from Conidiobolus coronatus (NCL 86.8.20)
    • Bhosale, S.H., M.B. Rao, V.V. Deshpande and M.C. Srinivasan. 1995. Thermostability of high activity alkaline protease from Conidiobolus coronatus (NCL 86.8.20). Enzyme Microb. Technol. 17: 136-139.
    • (1995) Enzyme Microb. Technol. , vol.17 , pp. 136-139
    • Bhosale, S.H.1    Rao, M.B.2    Deshpande, V.V.3    Srinivasan, M.C.4
  • 3
    • 0019967719 scopus 로고
    • Proteolytic activity of rumen microorganisms and effect of proteinase inhibitors
    • Brock, F.M., C.W. Frosberg and J.G. Buchanan-Smith. 1982. Proteolytic activity of rumen microorganisms and effect of proteinase inhibitors. Appl. Environ. Microbiol. 44:561-569.
    • (1982) Appl. Environ. Microbiol. , vol.44 , pp. 561-569
    • Brock, F.M.1    Frosberg, C.W.2    Buchanan-Smith, J.G.3
  • 4
    • 0020479358 scopus 로고
    • Purification and some properties of an extracellular protease (caldolysin) from an extreme thermophile
    • Cowan, D.A. and R.M. Daniel. 1982. Purification and some properties of an extracellular protease (caldolysin) from an extreme thermophile. Biochim. Biophys. Acta 705:293-305.
    • (1982) Biochim. Biophys. Acta , vol.705 , pp. 293-305
    • Cowan, D.A.1    Daniel, R.M.2
  • 6
    • 0031195026 scopus 로고    scopus 로고
    • The structural basis of protein halophilicity
    • Danson, M.J. and D.W. Hough. 1997. The structural basis of protein halophilicity. Comp. Biochem. Physiol. 117:307-312.
    • (1997) Comp. Biochem. Physiol. , vol.117 , pp. 307-312
    • Danson, M.J.1    Hough, D.W.2
  • 7
    • 0023258971 scopus 로고
    • Novel alkaline protease and heat stable serine protease from alkaliphilic Bacillus sp. strain GX6638
    • Durhan, D.R., D.B. Stewart and E.J. Stellwag. 1987. Novel alkaline protease and heat stable serine protease from alkaliphilic Bacillus sp. strain GX6638. J. Bacteriol. 169:2762-2768.
    • (1987) J. Bacteriol. , vol.169 , pp. 2762-2768
    • Durhan, D.R.1    Stewart, D.B.2    Stellwag, E.J.3
  • 8
    • 0027303817 scopus 로고
    • Compatible solute of halophilic eubacteria: Molecular principles, water solute interaction, stress protection
    • Galinski, E.A. 1993. Compatible solute of halophilic eubacteria: molecular principles, water solute interaction, stress protection. Experientia 49:487-496.
    • (1993) Experientia , vol.49 , pp. 487-496
    • Galinski, E.A.1
  • 9
    • 0034199501 scopus 로고    scopus 로고
    • Extracellular protease of Natrialba magadii; purification and biochemical characterization
    • Gimenez, M.I., C.A. Studdert, J.J. Sanchez and R.E. De Castro. 2000. Extracellular protease of Natrialba magadii; purification and biochemical characterization. Extremophiles 4:181-188.
    • (2000) Extremophiles , vol.4 , pp. 181-188
    • Gimenez, M.I.1    Studdert, C.A.2    Sanchez, J.J.3    De Castro, R.E.4
  • 10
    • 11144243173 scopus 로고    scopus 로고
    • The biocatalytic potential of extremophiles and extremozymes
    • Gomes, J. and W. Steiner. 2004. The biocatalytic potential of extremophiles and extremozymes. Food Technol. Biotechnol. 42: 223-235.
    • (2004) Food Technol. Biotechnol. , vol.42 , pp. 223-235
    • Gomes, J.1    Steiner, W.2
  • 11
    • 0032950882 scopus 로고    scopus 로고
    • Bleach stable alkaline protease from Bacillus sp.
    • Gupta, R.K., R.K. Saxena and K. Seema. 1999. Bleach stable alkaline protease from Bacillus sp. Biotechnol. Lett. 21:135-138.
    • (1999) Biotechnol. Lett. , vol.21 , pp. 135-138
    • Gupta, R.K.1    Saxena, R.K.2    Seema, K.3
  • 15
    • 0001300343 scopus 로고
    • Physiology of halophilic eubacteria
    • Ed. F. Rodriguez-Valera. CRC Press, Boca Raton, FL
    • Kushner, D. and M. Kamekura. 1988. Physiology of halophilic eubacteria. In Halophilic Bacteria. Ed. F. Rodriguez-Valera. CRC Press, Boca Raton, FL, pp 109-138.
    • (1988) Halophilic Bacteria , pp. 109-138
    • Kushner, D.1    Kamekura, M.2
  • 16
    • 0025112926 scopus 로고
    • A halophilic extracellular protease from a halophilic archaebacterium strain 172p1
    • Kamekura, M. and Y. Seno. 1990. A halophilic extracellular protease from a halophilic archaebacterium strain 172p1. Biochem. Cell Biol. 68:352-359.
    • (1990) Biochem. Cell Biol. , vol.68 , pp. 352-359
    • Kamekura, M.1    Seno, Y.2
  • 17
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during assembly of the head of bacteriophage T4
    • Laemmli, U.K. 1970. Cleavage of structural proteins during assembly of the head of bacteriophage T4. Nature 277:680-685.
    • (1970) Nature , vol.277 , pp. 680-685
    • Laemmli, U.K.1
  • 19
    • 0034166764 scopus 로고    scopus 로고
    • Halophilic adaptation of enzymes
    • Madern, D., C. Ebel and G. Zaccai. 2000. Halophilic adaptation of enzymes. Extremophiles 4:91-98.
    • (2000) Extremophiles , vol.4 , pp. 91-98
    • Madern, D.1    Ebel, C.2    Zaccai, G.3
  • 20
    • 0023893391 scopus 로고
    • Thermostable alkaline protease produced by Bacillus thermoruber - A new species of Bacillus
    • Manachini, P.L., M.G. Fortina and C. Parmi. 1988. Thermostable alkaline protease produced by Bacillus thermoruber - a new species of Bacillus. Appl. Microbiol. Biotechnol. 28:409-413.
    • (1988) Appl. Microbiol. Biotechnol. , vol.28 , pp. 409-413
    • Manachini, P.L.1    Fortina, M.G.2    Parmi, C.3
  • 21
    • 0035319086 scopus 로고    scopus 로고
    • Potential of halotolerant and halophilic microorganisms for biotechnology
    • Margesin, R. and F. Schiner. 2001. Potential of halotolerant and halophilic microorganisms for biotechnology. Extremophiles 5: 73-83.
    • (2001) Extremophiles , vol.5 , pp. 73-83
    • Margesin, R.1    Schiner, F.2
  • 22
    • 0034734270 scopus 로고    scopus 로고
    • Halophilic enzymes: Proteins with a grain of salt
    • Mevarech, M., F. Frolow and L.M. Gloss. 2000. Halophilic enzymes: proteins with a grain of salt. Biophys. Chem. 86:155-164.
    • (2000) Biophys. Chem. , vol.86 , pp. 155-164
    • Mevarech, M.1    Frolow, F.2    Gloss, L.M.3
  • 24
    • 0016376184 scopus 로고
    • Comparative specificity of microbial proteinases
    • Morihara, K. 1974. Comparative specificity of microbial proteinases. Adv. Enzymol. 41:179-243.
    • (1974) Adv. Enzymol. , vol.41 , pp. 179-243
    • Morihara, K.1
  • 25
    • 0014470465 scopus 로고
    • Proteolytic enzymes from extremely halophilic bacteria
    • Norberg, P. and B.V. Hofstein. 1969. Proteolytic enzymes from extremely halophilic bacteria. J. Gen. Microbiol. 55:251-256.
    • (1969) J. Gen. Microbiol. , vol.55 , pp. 251-256
    • Norberg, P.1    Hofstein, B.V.2
  • 27
    • 0025115569 scopus 로고
    • Efficient high performance liquid chromatographic system for the purification of a halobacterial serine protease
    • Schmitt, W., U. Rdest and W. Goebel. 1990. Efficient high performance liquid chromatographic system for the purification of a halobacterial serine protease. J. Chromatogr. 521:211-220.
    • (1990) J. Chromatogr. , vol.521 , pp. 211-220
    • Schmitt, W.1    Rdest, U.2    Goebel, W.3
  • 28
    • 2242477886 scopus 로고    scopus 로고
    • Perspectives on biotechnological applications of archaea
    • Schiraldi, C., M. Giuliano and M. De Rosa. 2002. Perspectives on biotechnological applications of archaea. Archaea 1:75-86.
    • (2002) Archaea , vol.1 , pp. 75-86
    • Schiraldi, C.1    Giuliano, M.2    De Rosa, M.3
  • 31
    • 0030730125 scopus 로고    scopus 로고
    • Detection and preliminary characterization of extracellular proteolytic activities of the haloalkaliphilic archaeon Natronococcus occultus
    • Studdert, C.A., R.E De Castro, M.K. Herrera Seitz and J.J. Sanchez. 1997. Detection and preliminary characterization of extracellular proteolytic activities of the haloalkaliphilic archaeon Natronococcus occultus. Arch. Microbiol. 168:532-535.
    • (1997) Arch. Microbiol. , vol.168 , pp. 532-535
    • Studdert, C.A.1    De Castro, R.E.2    Herrera Seitz, M.K.3    Sanchez, J.J.4
  • 32
    • 0035544105 scopus 로고    scopus 로고
    • Purification, biochemical characterization of the haloalkaliphilic archeon Natronococcus occultus extracellular serine protease
    • Studdert, C.A., M.K. Herrera Seitz, M.I. Plasencia Gil, J.J. Sanchez and R.E. De Castro. 2001. Purification, biochemical characterization of the haloalkaliphilic archeon Natronococcus occultus extracellular serine protease. J. Gen. Microbiol. 41:375-383.
    • (2001) J. Gen. Microbiol. , vol.41 , pp. 375-383
    • Studdert, C.A.1    Herrera Seitz, M.K.2    Plasencia Gil, M.I.3    Sanchez, J.J.4    De Castro, R.E.5
  • 34
    • 0037590011 scopus 로고    scopus 로고
    • Extremophiles as a source for novel enzymes
    • van den Berg, B. 2003. Extremophiles as a source for novel enzymes. Curr. Opinion Microbiol. 6:213-218.
    • (2003) Curr. Opinion Microbiol. , vol.6 , pp. 213-218
    • Van Den Berg, B.1
  • 35
    • 0003074147 scopus 로고
    • Proteinases
    • Ed. W.M. Fogarty. Applied Science Publication, New York
    • Ward, O.P. 1983. Proteinases. In Microbial Enzymes and Biotechnology. Ed. W.M. Fogarty. Applied Science Publication, New York, pp 251-317.
    • (1983) Microbial Enzymes and Biotechnology , pp. 251-317
    • Ward, O.P.1
  • 36
    • 0003131953 scopus 로고
    • Protease of haloalkaliphiles
    • Eds. K. Horikoshi and W.D. Grant. Springer-Verlag, New York
    • Yu, X.T. 1991. Protease of haloalkaliphiles. In Superbugs. Eds. K. Horikoshi and W.D. Grant. Springer-Verlag, New York, pp 76-83.
    • (1991) Superbugs , pp. 76-83
    • Yu, X.T.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.