메뉴 건너뛰기




Volumn 23, Issue 11, 2013, Pages 1519-1528

Improving the chitinolytic activity of Bacillus pumilus SG2 by random mutagenesis

Author keywords

AV2 9; Bacillus pumilus; Chitinase; Mutagenesis

Indexed keywords

CHITIN; CHITINASE; MUTANT PROTEIN; NITROUS ACID; RECOMBINANT CHITINASE L; RECOMBINANT CHITINASE S; RECOMBINANT ENZYME; SODIUM CHLORIDE; SPACER DNA; UNCLASSIFIED DRUG;

EID: 84888194453     PISSN: 10177825     EISSN: 17388872     Source Type: Journal    
DOI: 10.4014/jmb.1301.01048     Document Type: Article
Times cited : (28)

References (30)
  • 2
    • 84867644046 scopus 로고    scopus 로고
    • A fundamental protein property, thermodynamic stability, revealed solely from large-scale measurements of protein function
    • Araya CL, Fowler DM, Chenc W, Munieza I, Kelly JW, Fields S. 2012. A fundamental protein property, thermodynamic stability, revealed solely from large-scale measurements of protein function. Proc. Natl. Acad. Sci. USA 109: 16858-16863.
    • (2012) Proc. Natl. Acad. Sci. USA , vol.109 , pp. 16858-16863
    • Araya, C.L.1    Fowler, D.M.2    Chenc, W.3    Munieza, I.4    Kelly, J.W.5    Fields, S.6
  • 3
    • 32144432437 scopus 로고    scopus 로고
    • The SWISSMODEL Workspace: A Web-based environment for protein structure homology modeling
    • Arnold K, Bordoli L, Kopp J, Schwede T. 2006. The SWISSMODEL Workspace: A Web-based environment for protein structure homology modeling. Bioinformatics 22: 195-201.
    • (2006) Bioinformatics , vol.22 , pp. 195-201
    • Arnold, K.1    Bordoli, L.2    Kopp, J.3    Schwede, T.4
  • 4
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72: 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 5
    • 23644462645 scopus 로고    scopus 로고
    • Local stability identification and the role of key acidic amino acid residues in staphylococcal nuclease unfolding
    • Chen HM, Chan SC, Leung KW, Wu JM, Fang HJ, Tsong TY. 2005. Local stability identification and the role of key acidic amino acid residues in staphylococcal nuclease unfolding. FEBS J. 272: 3967-3974.
    • (2005) FEBS J. , vol.272 , pp. 3967-3974
    • Chen, H.M.1    Chan, S.C.2    Leung, K.W.3    Wu, J.M.4    Fang, H.J.5    Tsong, T.Y.6
  • 6
    • 0035023305 scopus 로고    scopus 로고
    • Comparative gene expression profiles following UV exposure in wild type and SOS-deficient Escherichia coli
    • Courcelle J, Khodursky A, Peter B, Brown PO, Hanawalt PC. 2001. Comparative gene expression profiles following UV exposure in wild type and SOS-deficient Escherichia coli. Genetics 158: 41-64.
    • (2001) Genetics , vol.158 , pp. 41-64
    • Courcelle, J.1    Khodursky, A.2    Peter, B.3    Brown, P.O.4    Hanawalt, P.C.5
  • 7
    • 84860894253 scopus 로고    scopus 로고
    • New insights into the role of the glutamic acid of the E-box motif in group B Streptococcus pilus 2a assembly
    • Cozzi R, Nuccitelli A, D'Onofrio M, Necchi F, Rosini R, Zerbini F, et al. 2012. New insights into the role of the glutamic acid of the E-box motif in group B Streptococcus pilus 2a assembly. FASEB J. 26: 1-11.
    • (2012) FASEB J. , vol.26 , pp. 1-11
    • Cozzi, R.1    Nuccitelli, A.2    D'Onofrio, M.3    Necchi, F.4    Rosini, R.5    Zerbini, F.6
  • 9
    • 79955866957 scopus 로고    scopus 로고
    • PoPMuSiC 2.1: A Web server for the estimation of protein stability changes upon mutation and sequence optimality
    • Dehouck Y, Kwasigroch JM, Gilis D, Rooman M. 2011. PoPMuSiC 2.1: a Web server for the estimation of protein stability changes upon mutation and sequence optimality. BMC Bioinformatics 12: 151
    • (2011) BMC Bioinformatics , vol.12 , pp. 151
    • Dehouck, Y.1    Kwasigroch, J.M.2    Gilis, D.3    Rooman, M.4
  • 10
    • 79551499020 scopus 로고    scopus 로고
    • First report of a bifunctional chitinase/lysozyme produced by Bacillus pumilus SG2
    • Ghasemi SH, Ahmadian G, Sadeghi M, Zeigler DR. 2011. First report of a bifunctional chitinase/lysozyme produced by Bacillus pumilus SG2. Enzyme Microb. Technol. 48: 225-231.
    • (2011) Enzyme Microb. Technol. , vol.48 , pp. 225-231
    • Ghasemi, S.H.1    Ahmadian, G.2    Sadeghi, M.3    Zeigler, D.R.4
  • 11
    • 3242889460 scopus 로고    scopus 로고
    • Improvement of bioinsecticides production through mutagenesis of Bacillus thuringiensis by U.V. and nitrous acid affecting metabolic pathways and/or delta-endotoxin synthesis
    • Ghribi D, Zouari N, Jaoua S. 2004. Improvement of bioinsecticides production through mutagenesis of Bacillus thuringiensis by U.V. and nitrous acid affecting metabolic pathways and/or delta-endotoxin synthesis. J. Appl. Microbiol. 97: 338-346.
    • (2004) J. Appl. Microbiol. , vol.97 , pp. 338-346
    • Ghribi, D.1    Zouari, N.2    Jaoua, S.3
  • 12
    • 0035073503 scopus 로고    scopus 로고
    • Purification of a thermostable endochitinase from Streptomyces RC1071 isolated from a cerrado soil and its antagonism against phytopathogenic fungi
    • Gomes RC, Semedo LT, Soares RM, Soares RMA, Linhares LF, Ulhoa CJ, et al. 2001. Purification of a thermostable endochitinase from Streptomyces RC1071 isolated from a cerrado soil and its antagonism against phytopathogenic fungi. J. Appl. Microbiol. 90: 653-661.
    • (2001) J. Appl. Microbiol. , vol.90 , pp. 653-661
    • Gomes, R.C.1    Semedo, L.T.2    Soares, R.M.3    Soares, R.M.A.4    Linhares, L.F.5    Ulhoa, C.J.6
  • 13
    • 0026055308 scopus 로고
    • A classification of glycosyl hydrolases based on amino acid sequence similarities
    • Henrissat B. 1991. A classification of glycosyl hydrolases based on amino acid sequence similarities. Biochem. J. 280: 309-316.
    • (1991) Biochem. J. , vol.280 , pp. 309-316
    • Henrissat, B.1
  • 14
    • 0027225980 scopus 로고
    • New families in the classification of glycosyl hydrolases based on amino acid sequence similarities
    • Henrissat B, Bairoch A. 1993. New families in the classification of glycosyl hydrolases based on amino acid sequence similarities. Biochem. J. 29: 781-788.
    • (1993) Biochem. J. , vol.29 , pp. 781-788
    • Henrissat, B.1    Bairoch, A.2
  • 15
    • 0032714186 scopus 로고    scopus 로고
    • Physiological aspects of chitin catabolism in marine bacteria
    • Keyhani NO, Roseman S. 1999. Physiological aspects of chitin catabolism in marine bacteria. Biochim. Biophys. Acta 1473: 108-122.
    • (1999) Biochim. Biophys. Acta , vol.1473 , pp. 108-122
    • Keyhani, N.O.1    Roseman, S.2
  • 16
    • 0037393710 scopus 로고    scopus 로고
    • Molecular cloning, sequencing, and expression of the gene encoding a novel chitinase A from a marine bacterium, Pseudomonas sp
    • Kitamura E, Kamei Y. 2003. Molecular cloning, sequencing, and expression of the gene encoding a novel chitinase A from a marine bacterium, Pseudomonas sp. PE2, and its domain structure. Appl. Microbiol. Biotechnol. 61: 140-149.
    • (2003) PE2, and its domain structure. Appl. Microbiol. Biotechnol. , vol.61 , pp. 140-149
    • Kitamura, E.1    Kamei, Y.2
  • 17
    • 62349120107 scopus 로고    scopus 로고
    • Improving the functional expression of a Bacillus licheniformis laccase by random and site-directed mutagenesis
    • Koschorreck K, Schmid RD, Urlacher VB. 2009. Improving the functional expression of a Bacillus licheniformis laccase by random and site-directed mutagenesis. BMC Biotechnol. 9: 12.
    • (2009) BMC Biotechnol. , vol.9 , pp. 12
    • Koschorreck, K.1    Schmid, R.D.2    Urlacher, V.B.3
  • 18
    • 67949084976 scopus 로고    scopus 로고
    • All-atom model for stabilization of alpha-helical structure in peptides by hydrocarbon staples
    • Kutchukian PS, Yang JS, Verdine GL, Shakhnovich EI. 2009. All-atom model for stabilization of alpha-helical structure in peptides by hydrocarbon staples. J. Am. Chem. Soc. 131: 4622-4627.
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 4622-4627
    • Kutchukian, P.S.1    Yang, J.S.2    Verdine, G.L.3    Shakhnovich, E.I.4
  • 20
    • 33747333106 scopus 로고
    • Use of dinitrosalicylic acid reagent for determination of reducing sugar
    • Miller GL. 1959. Use of dinitrosalicylic acid reagent for determination of reducing sugar. Anal. Chem. 31: 426-428
    • (1959) Anal. Chem. , vol.31 , pp. 426-428
    • Miller, G.L.1
  • 21
    • 0001831324 scopus 로고
    • The role of chitinase of Serratia marcescens in biocontrol of Sclerotium rolfsii
    • Ordentlich A, Elad Y, Chet L. 1988. The role of chitinase of Serratia marcescens in biocontrol of Sclerotium rolfsii. Phytopathology 78: 84-88.
    • (1988) Phytopathology , vol.78 , pp. 84-88
    • Ordentlich, A.1    Elad, Y.2    Chet, L.3
  • 24
    • 0023052559 scopus 로고
    • Isolation and partial characterization of two antifungal proteins from barley
    • Roberts WK, Selitrennikoff CP. 1986. Isolation and partial characterization of two antifungal proteins from barley. Biochim. Biophys. Acta 880: 161-70.
    • (1986) Biochim. Biophys. Acta , vol.880 , pp. 161-170
    • Roberts, W.K.1    Selitrennikoff, C.P.2
  • 25
    • 0026598632 scopus 로고
    • Properties of Bacillus megaterium and Bacillus subtilis mutants which lack the protease that degrades small, acid-soluble proteins during germination
    • Sanchez-Salas JL, Santiago-Lara ML, Setlow B, Sussman MD, Setlow P. 1992. Properties of Bacillus megaterium and Bacillus subtilis mutants which lack the protease that degrades small, acid-soluble proteins during germination. J. Bacteriol. 174: 807-814.
    • (1992) J. Bacteriol. , vol.174 , pp. 807-814
    • Sanchez-Salas, J.L.1    Santiago-Lara, M.L.2    Setlow, B.3    Sussman, M.D.4    Setlow, P.5
  • 27
    • 77954033519 scopus 로고    scopus 로고
    • Bacillus pumilus SG2 chitinases induced and regulated by chitin, show inhibitory activity against Fusarium graminearum and Bipolaris sorokiniana
    • Shali A, Ghasemi SH, Ahmadian G, Ranjbar G, Dehestani A, Khalesi N, et al. 2010. Bacillus pumilus SG2 chitinases induced and regulated by chitin, show inhibitory activity against Fusarium graminearum and Bipolaris sorokiniana. Phytoparasitica 38: 141-147.
    • (2010) Phytoparasitica , vol.38 , pp. 141-147
    • Shali, A.1    Ghasemi, S.H.2    Ahmadian, G.3    Ranjbar, G.4    Dehestani, A.5    Khalesi, N.6
  • 29
    • 0027216435 scopus 로고
    • Identification of glutamic acid 204 and aspartic acid 200 in chitinase A1 of Bacillus circulans WL-12 as essential residues for chitinase activity
    • Watanabe T, Kobori K, Miyashita K, Fujii T, Sakai H, Uchida M, et al. 1993. Identification of glutamic acid 204 and aspartic acid 200 in chitinase A1 of Bacillus circulans WL-12 as essential residues for chitinase activity. J. Biol. Chem. 268: 18567-18572.
    • (1993) J. Biol. Chem. , vol.268 , pp. 18567-18572
    • Watanabe, T.1    Kobori, K.2    Miyashita, K.3    Fujii, T.4    Sakai, H.5    Uchida, M.6
  • 30
    • 79959942908 scopus 로고    scopus 로고
    • A server for predicting effects of mutations on protein stability and malfunction
    • Worth CL, Preissner R, Blundell TL. 2011. A server for predicting effects of mutations on protein stability and malfunction. Nucleic Acids Res. 39: 215-222.
    • (2011) Nucleic Acids Res. , vol.39 , pp. 215-222
    • Worth, C.L.1    Preissner, R.2    Blundell, T.L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.