메뉴 건너뛰기




Volumn 41, Issue 9, 2006, Pages 2002-2009

Purification and characterization of alkaline protease from a newly isolated haloalkaliphilic Bacillus sp.

Author keywords

Alkaline protease; Bacillus sp.; Haloalkaliphiles; Protein denaturation; Protein folding; Salt tolerance

Indexed keywords

BACTERIOLOGY; CATALYST ACTIVITY; MOLECULAR WEIGHT; PH EFFECTS; SODIUM CHLORIDE; THERMAL EFFECTS;

EID: 33746375656     PISSN: 13595113     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.procbio.2006.04.016     Document Type: Article
Times cited : (81)

References (48)
  • 1
    • 0000491381 scopus 로고
    • Natronobacterium gen. nov. and Natronococcus gen. nov., to new genera of haloalkalophilic archaebacteria
    • Tindall B.J., Ross H.N.M., and Grant W.D. Natronobacterium gen. nov. and Natronococcus gen. nov., to new genera of haloalkalophilic archaebacteria. Syst Appl Micobial 5 (1984) 41-57
    • (1984) Syst Appl Micobial , vol.5 , pp. 41-57
    • Tindall, B.J.1    Ross, H.N.M.2    Grant, W.D.3
  • 2
    • 0035222885 scopus 로고    scopus 로고
    • Halonatronum saccharophilum gen. nov. sp. nov-a new haloalkalophilic bacteria from the order haloanaerobiales from Lake Magadi
    • Zhilina T.N., Garnova E.S., Turova T.P., Kostrikina N.A., and Zavarzin G. Halonatronum saccharophilum gen. nov. sp. nov-a new haloalkalophilic bacteria from the order haloanaerobiales from Lake Magadi. Mikrobiologiia 70 (2001) 77-85
    • (2001) Mikrobiologiia , vol.70 , pp. 77-85
    • Zhilina, T.N.1    Garnova, E.S.2    Turova, T.P.3    Kostrikina, N.A.4    Zavarzin, G.5
  • 3
    • 0034807809 scopus 로고    scopus 로고
    • Natrialba hulunbeirensis sp. nov. and Natrialba chahannaoensis sp. nov., novel haloalkaliphilic archaea from soda lakes in Inner Mongolia Autonomous Region, China
    • Xu Y., Wang Z., Xue Y., Zhou P., Ma Y., Ventosa A., et al. Natrialba hulunbeirensis sp. nov. and Natrialba chahannaoensis sp. nov., novel haloalkaliphilic archaea from soda lakes in Inner Mongolia Autonomous Region, China. Int J Syst Evol Microbiol 51 (2001) 1693-1698
    • (2001) Int J Syst Evol Microbiol , vol.51 , pp. 1693-1698
    • Xu, Y.1    Wang, Z.2    Xue, Y.3    Zhou, P.4    Ma, Y.5    Ventosa, A.6
  • 4
    • 0034802314 scopus 로고    scopus 로고
    • Natronobacterium nitratireducens sp. nov., a haloalkaliphilic archaean isolated from a soda lake in China
    • Xin H., Itoh T., Zhou P., Suzuki K., and Nakase T. Natronobacterium nitratireducens sp. nov., a haloalkaliphilic archaean isolated from a soda lake in China. Int J Syst Evol Microbiol 51 (2001) 1825-1829
    • (2001) Int J Syst Evol Microbiol , vol.51 , pp. 1825-1829
    • Xin, H.1    Itoh, T.2    Zhou, P.3    Suzuki, K.4    Nakase, T.5
  • 5
    • 0037978083 scopus 로고    scopus 로고
    • Spirochaeta americana sp. nov., a new haloalkaliphilic, obligately anaerobic spirochaete isolated from soda Mono Lake in California
    • Hoover R.B., Pikuta E.V., Bej A.K., Marsic D., Whitman W.B., Tang J., et al. Spirochaeta americana sp. nov., a new haloalkaliphilic, obligately anaerobic spirochaete isolated from soda Mono Lake in California. Int J Syst Evol Microbiol 53 (2003) 815-821
    • (2003) Int J Syst Evol Microbiol , vol.53 , pp. 815-821
    • Hoover, R.B.1    Pikuta, E.V.2    Bej, A.K.3    Marsic, D.4    Whitman, W.B.5    Tang, J.6
  • 6
    • 24944433802 scopus 로고    scopus 로고
    • Growth physiology and competitive interaction of obligately chemolithoautotrophic, haloalkaliphilic, sulfur-oxidizing bacteria from soda lakes
    • Sorokin D.Y., Banciu H., Loosdrecht M., and Kuenen G. Growth physiology and competitive interaction of obligately chemolithoautotrophic, haloalkaliphilic, sulfur-oxidizing bacteria from soda lakes. Curr Microbiol 4 (2003) 313-314
    • (2003) Curr Microbiol , vol.4 , pp. 313-314
    • Sorokin, D.Y.1    Banciu, H.2    Loosdrecht, M.3    Kuenen, G.4
  • 7
    • 0141482270 scopus 로고    scopus 로고
    • Methylophaga natronica sp. nov., a new alkaliphilic and moderately halophilic, restricted-facultatively methylotrophic bacterium from soda lake of the Southern Transbaikal region
    • Doronina N., Darmaeva T., and Trotsenko Y. Methylophaga natronica sp. nov., a new alkaliphilic and moderately halophilic, restricted-facultatively methylotrophic bacterium from soda lake of the Southern Transbaikal region. Syst Appl Microbiol 26 (2003) 382-389
    • (2003) Syst Appl Microbiol , vol.26 , pp. 382-389
    • Doronina, N.1    Darmaeva, T.2    Trotsenko, Y.3
  • 8
    • 4644309335 scopus 로고    scopus 로고
    • Growth kinetics of haloalkaliphilic, sulfur-oxidizing bacterium thioalkalivibrio versutus strain ALJ 15 in continuous culture
    • Banciu H., Sorokin D.Y., Kleerebezem R., Muyzer G., Galinski E.A., and Kuenen J.G. Growth kinetics of haloalkaliphilic, sulfur-oxidizing bacterium thioalkalivibrio versutus strain ALJ 15 in continuous culture. Extremophiles 8 (2004) 325-334
    • (2004) Extremophiles , vol.8 , pp. 325-334
    • Banciu, H.1    Sorokin, D.Y.2    Kleerebezem, R.3    Muyzer, G.4    Galinski, E.A.5    Kuenen, J.G.6
  • 9
    • 19344365162 scopus 로고    scopus 로고
    • One-step purification and characterization of an alkaline protease from haloalkaliphilic Bacillus sp.
    • Gupta A., Roy I., Patel R.K., Singh S.P., Khare S.K., and Gupta M.N. One-step purification and characterization of an alkaline protease from haloalkaliphilic Bacillus sp. J Chromatogr A 1075 (2005) 103-108
    • (2005) J Chromatogr A , vol.1075 , pp. 103-108
    • Gupta, A.1    Roy, I.2    Patel, R.K.3    Singh, S.P.4    Khare, S.K.5    Gupta, M.N.6
  • 10
    • 24944554850 scopus 로고    scopus 로고
    • Extracellular alkaline protease from a newly isolated haloalkaliphilic Bacillus sp.: production and optimization
    • Patel R.K., Dodia M.S., and Singh S.P. Extracellular alkaline protease from a newly isolated haloalkaliphilic Bacillus sp.: production and optimization. Process Biochem 40 11 (2005) 3569-3575
    • (2005) Process Biochem , vol.40 , Issue.11 , pp. 3569-3575
    • Patel, R.K.1    Dodia, M.S.2    Singh, S.P.3
  • 11
    • 0030730125 scopus 로고    scopus 로고
    • Detection and preliminary characterization of extracellular proteolytic activities of the haloalkaliphilic archaeon Natronococcus occultus
    • Studdert C.A., De Castro R.E., Herrera Seitz K., and Sánchez J.J. Detection and preliminary characterization of extracellular proteolytic activities of the haloalkaliphilic archaeon Natronococcus occultus. Arch Microbiol 168 (1997) 532-535
    • (1997) Arch Microbiol , vol.168 , pp. 532-535
    • Studdert, C.A.1    De Castro, R.E.2    Herrera Seitz, K.3    Sánchez, J.J.4
  • 12
    • 0030696842 scopus 로고    scopus 로고
    • Intracellular proteolytic activity of the haloalkaliphilic archaeon Natronococcus occultus. Effect of starvation
    • Herrera Seitz K., Studdert C., Sanchez J., and De Castro R. Intracellular proteolytic activity of the haloalkaliphilic archaeon Natronococcus occultus. Effect of starvation. J Basic Microbiol 7 (1997) 313-322
    • (1997) J Basic Microbiol , vol.7 , pp. 313-322
    • Herrera Seitz, K.1    Studdert, C.2    Sanchez, J.3    De Castro, R.4
  • 13
    • 0034663884 scopus 로고    scopus 로고
    • Purification and characterization of a membrane-associated ATPase from Natronococcus occultus, a haloalkaliphilic archaeon
    • Eddy M.L., and Jablonski P.E. Purification and characterization of a membrane-associated ATPase from Natronococcus occultus, a haloalkaliphilic archaeon. FEMS Microbiol Lett 189 (2000) 211-214
    • (2000) FEMS Microbiol Lett , vol.189 , pp. 211-214
    • Eddy, M.L.1    Jablonski, P.E.2
  • 14
    • 0035544105 scopus 로고    scopus 로고
    • Purification and biochemical characterization of the haloalkaliphilic archaeon Natronococcus occultus extracellular serine protease
    • Studdert C.A., Seitz M.K.H., Gilv M.I.P., Sanchez J.J., and De Castro R.E. Purification and biochemical characterization of the haloalkaliphilic archaeon Natronococcus occultus extracellular serine protease. J Basic Microbiol 6 (2001) 375-383
    • (2001) J Basic Microbiol , vol.6 , pp. 375-383
    • Studdert, C.A.1    Seitz, M.K.H.2    Gilv, M.I.P.3    Sanchez, J.J.4    De Castro, R.E.5
  • 15
    • 0026450962 scopus 로고
    • A perspective on the biotechnological potential of extremophiles
    • Herbert R.A. A perspective on the biotechnological potential of extremophiles. Trends Biotechnol 10 (1992) 395-401
    • (1992) Trends Biotechnol , vol.10 , pp. 395-401
    • Herbert, R.A.1
  • 16
    • 0034913744 scopus 로고    scopus 로고
    • Biotechnological uses of archaeal extremozymes
    • Eichler J. Biotechnological uses of archaeal extremozymes. Biotechnol Adv 19 (2001) 261-278
    • (2001) Biotechnol Adv , vol.19 , pp. 261-278
    • Eichler, J.1
  • 18
    • 0041764934 scopus 로고    scopus 로고
    • Applied Biocatalysis: an overview
    • Gupta M.N., and Roy I. Applied Biocatalysis: an overview. Indian J Biochem Biophys 39 (2002) 220-228
    • (2002) Indian J Biochem Biophys , vol.39 , pp. 220-228
    • Gupta, M.N.1    Roy, I.2
  • 19
    • 0035745539 scopus 로고    scopus 로고
    • Enhanced production and characterization of a highly thermostable alkaline protease from Bacillus sp. P-2
    • Kaur S., Vohra R.M., Kapoor M., Khalil Q., and Hoondal G.S. Enhanced production and characterization of a highly thermostable alkaline protease from Bacillus sp. P-2. World J Microbiol Biotechnol 17 (2001) 125-129
    • (2001) World J Microbiol Biotechnol , vol.17 , pp. 125-129
    • Kaur, S.1    Vohra, R.M.2    Kapoor, M.3    Khalil, Q.4    Hoondal, G.S.5
  • 20
    • 0034833840 scopus 로고    scopus 로고
    • Studies on production of thermostable alkaline protease from thermophilic and alkaliphilic Bacillus sp. JB-99 in a chemically defined medium
    • Johnvesly B., and Naik G.R. Studies on production of thermostable alkaline protease from thermophilic and alkaliphilic Bacillus sp. JB-99 in a chemically defined medium. Process Biochem 37 (2001) 139-144
    • (2001) Process Biochem , vol.37 , pp. 139-144
    • Johnvesly, B.1    Naik, G.R.2
  • 21
    • 0037426299 scopus 로고    scopus 로고
    • Stability characteristics of a calcium-independent alkaline protease from Nesterenkonia sp
    • Bakhtiar S., Andersson M., Gessesse A., Mattiasson B., and Kaul R. Stability characteristics of a calcium-independent alkaline protease from Nesterenkonia sp. Enzyme Microb Technol 32 (2002) 525-531
    • (2002) Enzyme Microb Technol , vol.32 , pp. 525-531
    • Bakhtiar, S.1    Andersson, M.2    Gessesse, A.3    Mattiasson, B.4    Kaul, R.5
  • 22
    • 0037426295 scopus 로고    scopus 로고
    • Novel alkaline proteases from alkaliphilic bacteria grown on chicken feather
    • Gessesse A., Kaul R.H., Gashe B.A., and Mattiasson B. Novel alkaline proteases from alkaliphilic bacteria grown on chicken feather. Enzyme Microb Technol 32 (2003) 519-524
    • (2003) Enzyme Microb Technol , vol.32 , pp. 519-524
    • Gessesse, A.1    Kaul, R.H.2    Gashe, B.A.3    Mattiasson, B.4
  • 23
    • 1542649404 scopus 로고    scopus 로고
    • Screening and characterization of the protease CP1 produced by the moderately halophilic bacterium Pseudoalteromonas sp. strain CP76
    • Sánchez-Porro C., Mellado E., Bertoldo C., Antranikian G., and Ventosa A. Screening and characterization of the protease CP1 produced by the moderately halophilic bacterium Pseudoalteromonas sp. strain CP76. Extremophiles 7 (2003) 221-228
    • (2003) Extremophiles , vol.7 , pp. 221-228
    • Sánchez-Porro, C.1    Mellado, E.2    Bertoldo, C.3    Antranikian, G.4    Ventosa, A.5
  • 24
    • 0037507352 scopus 로고    scopus 로고
    • Purification and characterization of an extracellular alkaline serine protease with dehairing function from Bacillus pumilus
    • Huang Q., Peng Y., Li X., Wang Y., and Zhang Y. Purification and characterization of an extracellular alkaline serine protease with dehairing function from Bacillus pumilus. Curr Microbiol 46 (2003) 169-173
    • (2003) Curr Microbiol , vol.46 , pp. 169-173
    • Huang, Q.1    Peng, Y.2    Li, X.3    Wang, Y.4    Zhang, Y.5
  • 25
    • 0034199501 scopus 로고    scopus 로고
    • Extracellular protease of Natrialba magadii: purification and biochemical characterization
    • Gimenez M.I., Studdert C.A., Sanchez J., and De Castro R.E. Extracellular protease of Natrialba magadii: purification and biochemical characterization. Extremophiles 4 (2000) 181-188
    • (2000) Extremophiles , vol.4 , pp. 181-188
    • Gimenez, M.I.1    Studdert, C.A.2    Sanchez, J.3    De Castro, R.E.4
  • 26
    • 0035544097 scopus 로고    scopus 로고
    • Autoproteolytic activation of the haloalkaliphilic archaeon Natronococcus occultus extracellular serine protease
    • Elsztein C., Herrera S.M.K., Sanchez J.J., and de Castro R.E. Autoproteolytic activation of the haloalkaliphilic archaeon Natronococcus occultus extracellular serine protease. J Basic Microbiol 41 (2001) 319-327
    • (2001) J Basic Microbiol , vol.41 , pp. 319-327
    • Elsztein, C.1    Herrera, S.M.K.2    Sanchez, J.J.3    de Castro, R.E.4
  • 27
    • 0030827505 scopus 로고    scopus 로고
    • Alkaline denaturation and partial refolding of pepsin investigated with DAPI as an extrinsic probe
    • Favilla R., Parisoli A., and Mazzini A. Alkaline denaturation and partial refolding of pepsin investigated with DAPI as an extrinsic probe. Biophys Chem 67 (1997) 75-83
    • (1997) Biophys Chem , vol.67 , pp. 75-83
    • Favilla, R.1    Parisoli, A.2    Mazzini, A.3
  • 28
    • 0037378360 scopus 로고    scopus 로고
    • Structural dissection of alkaline denatured pepsin
    • Kamatari Yo., Dobson C.M., and Konno T. Structural dissection of alkaline denatured pepsin. Protein Sci 12 (2003) 717-724
    • (2003) Protein Sci , vol.12 , pp. 717-724
    • Kamatari, Yo.1    Dobson, C.M.2    Konno, T.3
  • 30
    • 33646460646 scopus 로고
    • Academic press Inc., New York
    • Hagihara B. The Enzymes vol. 4 (1958), Academic press Inc., New York
    • (1958) The Enzymes , vol.4
    • Hagihara, B.1
  • 31
    • 8744261915 scopus 로고    scopus 로고
    • Salt-dependent studies of NADP-dependent isocitrate dehydrogense from the halophilic archaeon Haloferax volcanii
    • Madern D., Camacho M., Rodriguez-Arnedo A., Bonete M.J., and Zaccai G. Salt-dependent studies of NADP-dependent isocitrate dehydrogense from the halophilic archaeon Haloferax volcanii. Extremophiles 8 (2004) 377-384
    • (2004) Extremophiles , vol.8 , pp. 377-384
    • Madern, D.1    Camacho, M.2    Rodriguez-Arnedo, A.3    Bonete, M.J.4    Zaccai, G.5
  • 32
    • 0036598907 scopus 로고    scopus 로고
    • Molecular identification of alkaliphilic and halotolerant strain Bacillus sp. FTU as Bacillus pseudofirmus FTU
    • Muntyan M.S., Tourova T.P., Lysenko A.M., Kolganova T.V., Fritze D., and Skulachev V.P. Molecular identification of alkaliphilic and halotolerant strain Bacillus sp. FTU as Bacillus pseudofirmus FTU. Extremophiles 6 (2002) 195-199
    • (2002) Extremophiles , vol.6 , pp. 195-199
    • Muntyan, M.S.1    Tourova, T.P.2    Lysenko, A.M.3    Kolganova, T.V.4    Fritze, D.5    Skulachev, V.P.6
  • 33
    • 0025112926 scopus 로고
    • Halophilic extracellur protease from a halophilic archebacterium strain 172 P1
    • Kamekura M., and Seno Y. Halophilic extracellur protease from a halophilic archebacterium strain 172 P1. Biochem Cell Biol 68 (1990) 352-359
    • (1990) Biochem Cell Biol , vol.68 , pp. 352-359
    • Kamekura, M.1    Seno, Y.2
  • 34
    • 0025115569 scopus 로고
    • Efficient high-performance liquid chromatographic system for the purification of a halobacterial serine protease
    • Schmitt W., Rdest U., and Goebel W. Efficient high-performance liquid chromatographic system for the purification of a halobacterial serine protease. J Chromatogr 521 (1990) 211-220
    • (1990) J Chromatogr , vol.521 , pp. 211-220
    • Schmitt, W.1    Rdest, U.2    Goebel, W.3
  • 36
    • 0031979332 scopus 로고    scopus 로고
    • Effect of salts on the solubility of thermolysin: a remarkable increase in the solubility as well as the activity by the addition of salts without aggregation or dispersion of thermolysin
    • Inouye K., Kuzuyz K., and Tonomura B. Effect of salts on the solubility of thermolysin: a remarkable increase in the solubility as well as the activity by the addition of salts without aggregation or dispersion of thermolysin. J Biochem 123 (1998) 847-852
    • (1998) J Biochem , vol.123 , pp. 847-852
    • Inouye, K.1    Kuzuyz, K.2    Tonomura, B.3
  • 37
    • 0036014891 scopus 로고    scopus 로고
    • Optimization of protease activity of alkaliphilic bacteria isolated from an alkaline lake in India
    • Kanekar P.P., Nilegaonkar S.S., Sarnaik S.S., and Kelkar A.S. Optimization of protease activity of alkaliphilic bacteria isolated from an alkaline lake in India. Bioresour Technol 85 (2002) 87-93
    • (2002) Bioresour Technol , vol.85 , pp. 87-93
    • Kanekar, P.P.1    Nilegaonkar, S.S.2    Sarnaik, S.S.3    Kelkar, A.S.4
  • 38
    • 0034983826 scopus 로고    scopus 로고
    • A study of extracellular alkaline protease from Bacillus subtilis NCIM 2713
    • Mane R.R., and Bapat M. A study of extracellular alkaline protease from Bacillus subtilis NCIM 2713. Indian J Exp Biol 39 (2001) 578-583
    • (2001) Indian J Exp Biol , vol.39 , pp. 578-583
    • Mane, R.R.1    Bapat, M.2
  • 39
    • 3042745637 scopus 로고    scopus 로고
    • A novel extracellular subtilisin-like protease from the hyperthermophile Aeropyrum pernix K1: biochemical properties, cloning, and expression
    • Catara G., Ruggiero G., La Cara F., Digilio F.A., Capasso A., and Rossi M. A novel extracellular subtilisin-like protease from the hyperthermophile Aeropyrum pernix K1: biochemical properties, cloning, and expression. Extremophiles 7 (2003) 391-399
    • (2003) Extremophiles , vol.7 , pp. 391-399
    • Catara, G.1    Ruggiero, G.2    La Cara, F.3    Digilio, F.A.4    Capasso, A.5    Rossi, M.6
  • 40
    • 0027281639 scopus 로고
    • Purification and properties of the highly thermostable alkaline protease from an alkaliphilic and thermophilic Bacillus sp
    • Fujiwara N., Masui A., and Imanaka T. Purification and properties of the highly thermostable alkaline protease from an alkaliphilic and thermophilic Bacillus sp. J Biotechnol 30 (1993) 245-256
    • (1993) J Biotechnol , vol.30 , pp. 245-256
    • Fujiwara, N.1    Masui, A.2    Imanaka, T.3
  • 41
    • 23144431945 scopus 로고    scopus 로고
    • Purification and partial characterization of thermostable serine alkaline protease from a newly isolated Bacillus subtilis PE-11
    • Adinarayana K., Ellaiah P., and Prasad D.S. Purification and partial characterization of thermostable serine alkaline protease from a newly isolated Bacillus subtilis PE-11. AAPS Pharm Sci Tech 4 (2003) 1-9
    • (2003) AAPS Pharm Sci Tech , vol.4 , pp. 1-9
    • Adinarayana, K.1    Ellaiah, P.2    Prasad, D.S.3
  • 42
    • 1942502760 scopus 로고    scopus 로고
    • Enhanced production of alkaline proteases by Bacillus sphaericus using fed-batch culture
    • Singh J., Vohra R.M., and Sahoo D.K. Enhanced production of alkaline proteases by Bacillus sphaericus using fed-batch culture. Process Biochem 39 (2004) 1093-1101
    • (2004) Process Biochem , vol.39 , pp. 1093-1101
    • Singh, J.1    Vohra, R.M.2    Sahoo, D.K.3
  • 43
    • 33645893233 scopus 로고
    • Characteristics of the alkaline protease from the moderate halophile, Halomonas sp. ES 10
    • Kim C., Oh M., and Choi D. Characteristics of the alkaline protease from the moderate halophile, Halomonas sp. ES 10. J Korean Agric Chem Soc 35 (1992) 237-241
    • (1992) J Korean Agric Chem Soc , vol.35 , pp. 237-241
    • Kim, C.1    Oh, M.2    Choi, D.3
  • 44
    • 0035515015 scopus 로고    scopus 로고
    • Purification and characteristics of alkaline proteinase from alkalophlic Bacillus
    • Muderrizade A., Ensari N.Y., Aguloglu S., and Otludil B. Purification and characteristics of alkaline proteinase from alkalophlic Bacillus. Prikl Biokhim Mikrobiol 37 (2001) 674-677
    • (2001) Prikl Biokhim Mikrobiol , vol.37 , pp. 674-677
    • Muderrizade, A.1    Ensari, N.Y.2    Aguloglu, S.3    Otludil, B.4
  • 45
    • 33746331442 scopus 로고    scopus 로고
    • Dodia, MS. Stability and folding of extracelluler enzymes from haloalkaliphilic bacteria. Ph.D. thesis. Saurashtra University, Rajkot, India, 2005.
  • 47
    • 0028917544 scopus 로고
    • Effective renaturation of reduced lysozyme by gentle removal of urea
    • Maeda Y., Koga H., Yamada H., and Imoto T. Effective renaturation of reduced lysozyme by gentle removal of urea. Protein Eng 8 (1995) 201-205
    • (1995) Protein Eng , vol.8 , pp. 201-205
    • Maeda, Y.1    Koga, H.2    Yamada, H.3    Imoto, T.4
  • 48
    • 2942674796 scopus 로고    scopus 로고
    • Molecular adaptations: the malate dehydrogenase from the extreme halophilic bacterium Salinibacter rubber behaves like a non-halophilic protein
    • Madern D., and Zaccai G. Molecular adaptations: the malate dehydrogenase from the extreme halophilic bacterium Salinibacter rubber behaves like a non-halophilic protein. Biochemie 86 (2004) 295-303
    • (2004) Biochemie , vol.86 , pp. 295-303
    • Madern, D.1    Zaccai, G.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.