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Volumn 115, Issue 6, 2013, Pages 628-632

Purification, characterization, and gene cloning of a cold-adapted thermolysin-like protease from Halobacillus sp. SCSIO 20089

Author keywords

Cold active enzyme; Enzyme purification; Genome walking; Marine sediment; Protease

Indexed keywords

COLD-ACTIVE ENZYMES; ENZYME PURIFICATION; GENOME-WALKING; MARINE SEDIMENTS; PROTEASE;

EID: 84876988510     PISSN: 13891723     EISSN: 13474421     Source Type: Journal    
DOI: 10.1016/j.jbiosc.2012.12.013     Document Type: Article
Times cited : (37)

References (37)
  • 2
    • 1842509102 scopus 로고    scopus 로고
    • Psychrophilic enzymes: hot topics in cold adaptation
    • Feller G., Gerday C. Psychrophilic enzymes: hot topics in cold adaptation. Nat. Rev. Microbiol. 2003, 1:200-208.
    • (2003) Nat. Rev. Microbiol. , vol.1 , pp. 200-208
    • Feller, G.1    Gerday, C.2
  • 4
    • 0036323668 scopus 로고    scopus 로고
    • Bacterial alkaline proteases: molecular approaches and industrial applications
    • Gupta R., Beg Q.K., Lorenz P. Bacterial alkaline proteases: molecular approaches and industrial applications. Appl. Microbiol. Biotechnol. 2002, 59:15-32.
    • (2002) Appl. Microbiol. Biotechnol. , vol.59 , pp. 15-32
    • Gupta, R.1    Beg, Q.K.2    Lorenz, P.3
  • 5
    • 0033572187 scopus 로고    scopus 로고
    • Microbial alkaline proteases: from a bioindustrial viewpoint
    • Kumar C.G., Takagi H. Microbial alkaline proteases: from a bioindustrial viewpoint. Biotechnol. Adv. 1999, 17:561-594.
    • (1999) Biotechnol. Adv. , vol.17 , pp. 561-594
    • Kumar, C.G.1    Takagi, H.2
  • 7
    • 0036868198 scopus 로고    scopus 로고
    • Effects of different buffers on the thermostability and autolysis of a cold-adapted protease MCP-01
    • Chen X.L., Sun C.Y., Zhang Y.Z., Gao P.J. Effects of different buffers on the thermostability and autolysis of a cold-adapted protease MCP-01. J. Protein Chem. 2002, 21:523-527.
    • (2002) J. Protein Chem. , vol.21 , pp. 523-527
    • Chen, X.L.1    Sun, C.Y.2    Zhang, Y.Z.3    Gao, P.J.4
  • 8
    • 77955923960 scopus 로고    scopus 로고
    • Cloning, expression, and identification of a novel extracellular cold-adapted alkaline protease gene of the marine bacterium strain YS-80-122
    • Wang F., Hao J., Yang C., Sun M. Cloning, expression, and identification of a novel extracellular cold-adapted alkaline protease gene of the marine bacterium strain YS-80-122. Appl. Biochem. Biotechnol. 2010, 162:1497-1505.
    • (2010) Appl. Biochem. Biotechnol. , vol.162 , pp. 1497-1505
    • Wang, F.1    Hao, J.2    Yang, C.3    Sun, M.4
  • 9
    • 58149103584 scopus 로고    scopus 로고
    • The thermolysin family (M4) of enzymes: therapeutic and biotechnological potential
    • Adekoya O.A., Sylte I. The thermolysin family (M4) of enzymes: therapeutic and biotechnological potential. Chem. Biol. Drug Des. 2009, 73:7-16.
    • (2009) Chem. Biol. Drug Des. , vol.73 , pp. 7-16
    • Adekoya, O.A.1    Sylte, I.2
  • 10
    • 0034613186 scopus 로고    scopus 로고
    • Substrate specificity in the highly heterogeneous M4 peptidase family is determined by a small subset of amino acids
    • de Kreij A., Venema G., van den Burg B. Substrate specificity in the highly heterogeneous M4 peptidase family is determined by a small subset of amino acids. J. Biol. Chem. 2000, 275:31115-31120.
    • (2000) J. Biol. Chem. , vol.275 , pp. 31115-31120
    • de Kreij, A.1    Venema, G.2    van den Burg, B.3
  • 11
    • 30144439453 scopus 로고    scopus 로고
    • Comparative sequence and structure analysis reveal features of cold adaptation of an enzyme in the thermolysin family
    • Adekoya O.A., Helland R., Willassen N.P., Sylte I. Comparative sequence and structure analysis reveal features of cold adaptation of an enzyme in the thermolysin family. Proteins 2006, 62:435-449.
    • (2006) Proteins , vol.62 , pp. 435-449
    • Adekoya, O.A.1    Helland, R.2    Willassen, N.P.3    Sylte, I.4
  • 13
    • 0017184389 scopus 로고
    • Rapid and sensitive method for quantitation of microgram quantities of protein utilizing principle of protein-dye binding
    • Bradford M.M. Rapid and sensitive method for quantitation of microgram quantities of protein utilizing principle of protein-dye binding. Anal. Biochem. 1976, 72:248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 14
    • 0000795704 scopus 로고
    • Crystalline soybean trypsin inhibitor. 2. General properties
    • Kunitz M. Crystalline soybean trypsin inhibitor. 2. General properties. J. Gen. Physiol. 1947, 30:291-310.
    • (1947) J. Gen. Physiol. , vol.30 , pp. 291-310
    • Kunitz, M.1
  • 15
    • 0014431088 scopus 로고
    • A spectrophotometric assay for neutral protease
    • Feder J. A spectrophotometric assay for neutral protease. Biochem. Biophys. Res. Commun. 1968, 32:326-332.
    • (1968) Biochem. Biophys. Res. Commun. , vol.32 , pp. 326-332
    • Feder, J.1
  • 16
    • 0023664635 scopus 로고
    • Sequence from picomole quantities of proteins electroblotted onto polyvinylidene difluoride membranes
    • Matsudaira P. Sequence from picomole quantities of proteins electroblotted onto polyvinylidene difluoride membranes. J. Biol. Chem. 1987, 262:10035-10038.
    • (1987) J. Biol. Chem. , vol.262 , pp. 10035-10038
    • Matsudaira, P.1
  • 17
    • 0043122986 scopus 로고    scopus 로고
    • CODEHOP (COnsensus-DEgenerate Hybrid Oligonucleotide Primer) PCR primer design
    • Rose T.M., Henikoff J.G., Henikoff S. CODEHOP (COnsensus-DEgenerate Hybrid Oligonucleotide Primer) PCR primer design. Nucleic Acids Res. 2003, 31:3763-3766.
    • (2003) Nucleic Acids Res. , vol.31 , pp. 3763-3766
    • Rose, T.M.1    Henikoff, J.G.2    Henikoff, S.3
  • 18
    • 36448931584 scopus 로고    scopus 로고
    • High-efficiency thermal asymmetric interlaced PCR for amplification of unknown flanking sequences
    • Liu Y.G., Chen Y. High-efficiency thermal asymmetric interlaced PCR for amplification of unknown flanking sequences. Biotechniques 2007, 43:649-656.
    • (2007) Biotechniques , vol.43 , pp. 649-656
    • Liu, Y.G.1    Chen, Y.2
  • 19
    • 0038655233 scopus 로고    scopus 로고
    • Halobacillus salinus sp. nov., isolated from a salt lake on the coast of the East Sea in Korea
    • Yoon J.H., Kook H.K.G., Park Y.H. Halobacillus salinus sp. nov., isolated from a salt lake on the coast of the East Sea in Korea. Int. J. Syst. Evol. Microbiol. 2003, 53:687-693.
    • (2003) Int. J. Syst. Evol. Microbiol. , vol.53 , pp. 687-693
    • Yoon, J.H.1    Kook, H.K.G.2    Park, Y.H.3
  • 20
    • 33745514465 scopus 로고    scopus 로고
    • A halophilic serine proteinase from Halobacillus sp. SR5-3 isolated from fish sauce: purification and characterization
    • Namwong S., Hiraga K., Takada K., Tsunemi M., Tanasupawat S., Oda K. A halophilic serine proteinase from Halobacillus sp. SR5-3 isolated from fish sauce: purification and characterization. Biosci. Biotechnol. Biochem. 2006, 70:1395-1401.
    • (2006) Biosci. Biotechnol. Biochem. , vol.70 , pp. 1395-1401
    • Namwong, S.1    Hiraga, K.2    Takada, K.3    Tsunemi, M.4    Tanasupawat, S.5    Oda, K.6
  • 21
    • 57649225420 scopus 로고    scopus 로고
    • Production, optimization and purification of a novel extracellular protease from the moderately halophilic bacterium Halobacillus karajensis
    • Karbalaei-Heidari H.R., Amoozegar M.A., Hajighasemi M., Ziaee A.A., Ventosa A. Production, optimization and purification of a novel extracellular protease from the moderately halophilic bacterium Halobacillus karajensis. J. Ind. Microbiol. Biotechnol. 2009, 36:21-27.
    • (2009) J. Ind. Microbiol. Biotechnol. , vol.36 , pp. 21-27
    • Karbalaei-Heidari, H.R.1    Amoozegar, M.A.2    Hajighasemi, M.3    Ziaee, A.A.4    Ventosa, A.5
  • 22
    • 0028292010 scopus 로고
    • Cold adaptation of proteins - purification, characterization, and sequence of the heat-labile subtilisin from the Antarctic psychrophile Bacillus Ta41
    • Davail S., Feller G., Narinx E., Gerday C. Cold adaptation of proteins - purification, characterization, and sequence of the heat-labile subtilisin from the Antarctic psychrophile Bacillus Ta41. J. Biol. Chem. 1994, 269:17448-17453.
    • (1994) J. Biol. Chem. , vol.269 , pp. 17448-17453
    • Davail, S.1    Feller, G.2    Narinx, E.3    Gerday, C.4
  • 24
    • 38849104810 scopus 로고    scopus 로고
    • Purification and characterization of a cold-adapted alpha-amylase produced by Nocardiopsis sp. 7326 isolated from Prydz Bay, Antarctic
    • Zhang J.W., Zeng R.Y. Purification and characterization of a cold-adapted alpha-amylase produced by Nocardiopsis sp. 7326 isolated from Prydz Bay, Antarctic. Mar. Biotechnol. 2008, 10:75-82.
    • (2008) Mar. Biotechnol. , vol.10 , pp. 75-82
    • Zhang, J.W.1    Zeng, R.Y.2
  • 25
    • 0032975313 scopus 로고    scopus 로고
    • Cold-active serine alkaline protease from the psychrotrophic bacterium Shewanella strain Ac10: gene cloning and enzyme purification and characterization
    • Kulakova L., Galkin A., Kurihara T., Yoshimura T., Esaki N. Cold-active serine alkaline protease from the psychrotrophic bacterium Shewanella strain Ac10: gene cloning and enzyme purification and characterization. Appl. Environ. Microbiol. 1999, 65:611-617.
    • (1999) Appl. Environ. Microbiol. , vol.65 , pp. 611-617
    • Kulakova, L.1    Galkin, A.2    Kurihara, T.3    Yoshimura, T.4    Esaki, N.5
  • 26
    • 44349188528 scopus 로고    scopus 로고
    • Extracellular proteases from the Antarctic marine Pseudoalteromonas sp. P96-47 strain
    • Vazquez S.C., Hernandez E., Cormack W.P.M. Extracellular proteases from the Antarctic marine Pseudoalteromonas sp. P96-47 strain. Rev. Argent. Microbiol. 2008, 40:63-71.
    • (2008) Rev. Argent. Microbiol. , vol.40 , pp. 63-71
    • Vazquez, S.C.1    Hernandez, E.2    Cormack, W.P.M.3
  • 27
    • 0001621050 scopus 로고
    • Bacillus stearothermophilus Kp-1236 neutral protease with strong thermostability comparable to thermolysin
    • Takii Y., Taguchi H., Shimoto H., Suzuki Y. Bacillus stearothermophilus Kp-1236 neutral protease with strong thermostability comparable to thermolysin. Appl. Microbiol. Biotechnol. 1987, 27:186-191.
    • (1987) Appl. Microbiol. Biotechnol. , vol.27 , pp. 186-191
    • Takii, Y.1    Taguchi, H.2    Shimoto, H.3    Suzuki, Y.4
  • 28
    • 0025909433 scopus 로고
    • Characterization of an inhibitory metal-binding site in carboxypeptidase-A
    • Larsen K.S., Auld D.S. Characterization of an inhibitory metal-binding site in carboxypeptidase-A. Biochemistry 1991, 30:2613-2618.
    • (1991) Biochemistry , vol.30 , pp. 2613-2618
    • Larsen, K.S.1    Auld, D.S.2
  • 29
    • 11244249563 scopus 로고    scopus 로고
    • Gene cloning and characterization of a Bacillus vietnamensis metalloprotease
    • Kim M., Nishiyama Y., Mura K., Tokue C., Arai S. Gene cloning and characterization of a Bacillus vietnamensis metalloprotease. Biosci. Biotechnol. Biochem. 2004, 68:1533-1540.
    • (2004) Biosci. Biotechnol. Biochem. , vol.68 , pp. 1533-1540
    • Kim, M.1    Nishiyama, Y.2    Mura, K.3    Tokue, C.4    Arai, S.5
  • 30
    • 66149140273 scopus 로고    scopus 로고
    • Cloning, expression, and purification of Pseudomonas aeruginosa keratinase in Escherichia coli AD494(DE3)pLysS expression system
    • Lin H.H., Yin L.J., Jiang S.T. Cloning, expression, and purification of Pseudomonas aeruginosa keratinase in Escherichia coli AD494(DE3)pLysS expression system. J. Agric. Food Chem. 2009, 57:3506-3511.
    • (2009) J. Agric. Food Chem. , vol.57 , pp. 3506-3511
    • Lin, H.H.1    Yin, L.J.2    Jiang, S.T.3
  • 31
    • 80053345905 scopus 로고    scopus 로고
    • SignalP 4.0: discriminating signal peptides from transmembrane regions
    • Petersen T.N., Brunak S., von Heijne G., Nielsen H. SignalP 4.0: discriminating signal peptides from transmembrane regions. Nat. Methods 2011, 8:785-786.
    • (2011) Nat. Methods , vol.8 , pp. 785-786
    • Petersen, T.N.1    Brunak, S.2    von Heijne, G.3    Nielsen, H.4
  • 33
    • 0029036451 scopus 로고
    • Evolutionary families of metallopeptidases
    • Rawlings N.D., Barrett A.J. Evolutionary families of metallopeptidases. Methods Enzymol. 1995, 248:183-228.
    • (1995) Methods Enzymol. , vol.248 , pp. 183-228
    • Rawlings, N.D.1    Barrett, A.J.2
  • 34
    • 0037688133 scopus 로고    scopus 로고
    • Molecular adaptations to cold in psychrophilic enzymes
    • Feller G. Molecular adaptations to cold in psychrophilic enzymes. Cell. Mol. Life Sci. 2003, 60:648-662.
    • (2003) Cell. Mol. Life Sci. , vol.60 , pp. 648-662
    • Feller, G.1
  • 35
    • 0028289989 scopus 로고
    • Stability and structural-analysis of alpha-amylase from the Antarctic psychrophile Alteromonas haloplanctis-A23
    • Feller G., Payan F., Theys F., Qian M.X., Haser R., Gerday C. Stability and structural-analysis of alpha-amylase from the Antarctic psychrophile Alteromonas haloplanctis-A23. Eur. J. Biochem. 1994, 222:441-447.
    • (1994) Eur. J. Biochem. , vol.222 , pp. 441-447
    • Feller, G.1    Payan, F.2    Theys, F.3    Qian, M.X.4    Haser, R.5    Gerday, C.6
  • 36
    • 0342981073 scopus 로고    scopus 로고
    • Molecular adaptation to cold of an Antarctic bacterial lipase
    • Arpigny J.L., Lamotte J., Gerday C. Molecular adaptation to cold of an Antarctic bacterial lipase. J. Mol. Catal. B Enzym. 1997, 3:29-35.
    • (1997) J. Mol. Catal. B Enzym. , vol.3 , pp. 29-35
    • Arpigny, J.L.1    Lamotte, J.2    Gerday, C.3
  • 37
    • 46749089070 scopus 로고    scopus 로고
    • Structural insights into cold inactivation of tryptophanase and cold adaptation of subtilisin S41
    • Almog O., Kogan A., de Leeuw M., Gdalevsky G.Y., Cohen-Luria R., Parola A.H. Structural insights into cold inactivation of tryptophanase and cold adaptation of subtilisin S41. Biopolymers 2008, 89:354-359.
    • (2008) Biopolymers , vol.89 , pp. 354-359
    • Almog, O.1    Kogan, A.2    de Leeuw, M.3    Gdalevsky, G.Y.4    Cohen-Luria, R.5    Parola, A.H.6


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