메뉴 건너뛰기




Volumn 89, Issue 12, 2014, Pages 1825-1832

Enhanced expression of pgdS gene for high production of poly-γ-glutamic aicd with lower molecular weight in Bacillus licheniformis WX-02

Author keywords

Bacillus licheniformis; Depolymerase; Molecular weight; Poly glutamic acid; Yield

Indexed keywords

AMINO ACIDS; BACTERIOLOGY; ENZYME ACTIVITY; ESCHERICHIA COLI; TRANSCRIPTION;

EID: 84911438143     PISSN: 02682575     EISSN: 10974660     Source Type: Journal    
DOI: 10.1002/jctb.4261     Document Type: Article
Times cited : (41)

References (41)
  • 2
    • 79955019471 scopus 로고    scopus 로고
    • Poly (glutamic acid) - an emerging biopolymer of commercial interest
    • Bajaj I and Singhal R, Poly (glutamic acid) - an emerging biopolymer of commercial interest. Bioresource Technol 102:5551-5561 (2011).
    • (2011) Bioresource Technol , vol.102 , pp. 5551-5561
    • Bajaj, I.1    Singhal, R.2
  • 3
    • 84901693696 scopus 로고    scopus 로고
    • Adsorption of rare earths (III) by calcium alginate-poly glutamic acid hybrid gels
    • Wang F, Zhao J, Wei X, Huo F, Li W, Hu Q and Liu H, Adsorption of rare earths (III) by calcium alginate-poly glutamic acid hybrid gels. J Chem Technol Biotechnol. DOI 10.1002/jctb.4186 (2013).
    • (2013) J Chem Technol Biotechnol
    • Wang, F.1    Zhao, J.2    Wei, X.3    Huo, F.4    Li, W.5    Hu, Q.6    Liu, H.7
  • 4
    • 0028215850 scopus 로고
    • Biosynthesis of poly (γ-glutamic acid) from L-glutamic acid, citric acid, and ammonium sulfate in Bacillus subtilis IFO3335
    • Kunioka M and Goto A, Biosynthesis of poly (γ-glutamic acid) from L-glutamic acid, citric acid, and ammonium sulfate in Bacillus subtilis IFO3335. Appl Microbiol Biotechnol 40:867-872 (1994).
    • (1994) Appl Microbiol Biotechnol , vol.40 , pp. 867-872
    • Kunioka, M.1    Goto, A.2
  • 5
    • 80051469978 scopus 로고    scopus 로고
    • Expression of glr gene encoding glutamate racemase in Bacillus licheniformis WX-02 and its regulatory effects on synthesis of poly-γ-glutamic acid
    • Jiang F, Qi GF, Ji ZX, Zhang SL, Liu J, Ma X and Chen SW, Expression of glr gene encoding glutamate racemase in Bacillus licheniformis WX-02 and its regulatory effects on synthesis of poly-γ-glutamic acid. Biotechnol Lett 33:1837-1840 (2011).
    • (2011) Biotechnol Lett , vol.33 , pp. 1837-1840
    • Jiang, F.1    Qi, G.F.2    Ji, Z.X.3    Zhang, S.L.4    Liu, J.5    Ma, X.6    Chen, S.W.7
  • 6
    • 0030150505 scopus 로고    scopus 로고
    • Alkaline hydrolysis of poly (γ-glutamic acid) produced by microorganism
    • Kubota H, Nambu Y and Endo T, Alkaline hydrolysis of poly (γ-glutamic acid) produced by microorganism. J Polym Sci Part A: Polym Chem 34:1347-1351 (1996).
    • (1996) J Polym Sci Part A: Polym Chem , vol.34 , pp. 1347-1351
    • Kubota, H.1    Nambu, Y.2    Endo, T.3
  • 7
    • 0031240577 scopus 로고    scopus 로고
    • Purification and properties of two isozymes of γ-glutamyltranspeptidase from Bacillus subtilis TAM-4
    • Abe K, Ito Y, Ohmachi T and Asada Y, Purification and properties of two isozymes of γ-glutamyltranspeptidase from Bacillus subtilis TAM-4. Biosci Biotechnol Biochem 61:1621-1625 (1997).
    • (1997) Biosci Biotechnol Biochem , vol.61 , pp. 1621-1625
    • Abe, K.1    Ito, Y.2    Ohmachi, T.3    Asada, Y.4
  • 8
    • 0028172511 scopus 로고
    • Cromwick A-M and Gross RA, γ-Poly (glutamic acid) formation by Bacillus licheniformis 9945a: physiological and biochemical studies
    • Birrer GA, Cromwick A-M and Gross RA, γ-Poly (glutamic acid) formation by Bacillus licheniformis 9945a: physiological and biochemical studies. Int J Biologic Macromol 16:265-275 (1994).
    • (1994) Int J Biologic Macromol , vol.16 , pp. 265-275
    • Birrer, G.A.1
  • 9
    • 0034158180 scopus 로고    scopus 로고
    • Enzymatic breakdown of poly-γ-D-glutamic acid in Bacillus licheniformis: identification of a polyglutamyl γ-hydrolase enzyme
    • King EC, Blacker AJ and Bugg TDH, Enzymatic breakdown of poly-γ-D-glutamic acid in Bacillus licheniformis: identification of a polyglutamyl γ-hydrolase enzyme. Biomacromolecules 1:75-83 (2000).
    • (2000) Biomacromolecules , vol.1 , pp. 75-83
    • King, E.C.1    Blacker, A.J.2    Bugg, T.D.H.3
  • 10
    • 33749030166 scopus 로고    scopus 로고
    • Structure of the hydrolyzed product (F-2) released from γ-polyglutamic acid by γ-glutamyl hydrolase YwtD of Bacillus subtilis
    • Chunhachart O, Hanayama T, Hidesaki M, Tanimoto H and Tahara Y, Structure of the hydrolyzed product (F-2) released from γ-polyglutamic acid by γ-glutamyl hydrolase YwtD of Bacillus subtilis. Biosci Biotechnol Biochem 70:2289-2291 (2006).
    • (2006) Biosci Biotechnol Biochem , vol.70 , pp. 2289-2291
    • Chunhachart, O.1    Hanayama, T.2    Hidesaki, M.3    Tanimoto, H.4    Tahara, Y.5
  • 11
    • 57449105176 scopus 로고    scopus 로고
    • Q, Feng XH and Ouyang PK, Investigation on enzymatic degradation of γ-polyglutamic acid from Bacillus subtilis NX-2
    • Wu
    • Yao J, Jing J, Xu H, Liang JF, Wu Q, Feng XH and Ouyang PK, Investigation on enzymatic degradation of γ-polyglutamic acid from Bacillus subtilis NX-2. J Molec Catal B: Enzyme 56:158-164 (2009).
    • (2009) J Molec Catal B: Enzyme , vol.56 , pp. 158-164
    • Yao, J.1    Jing, J.2    Xu, H.3    Liang, J.F.4
  • 12
    • 0037379280 scopus 로고    scopus 로고
    • Characterization of the Bacillus subtilis ywtD gene, whose product is involved in γ-polyglutamic acid degradation
    • Suzuki T and Tahara Y, Characterization of the Bacillus subtilis ywtD gene, whose product is involved in γ-polyglutamic acid degradation. J Bacteriol 185:2379-2382 (2003).
    • (2003) J Bacteriol , vol.185 , pp. 2379-2382
    • Suzuki, T.1    Tahara, Y.2
  • 14
    • 33748459631 scopus 로고    scopus 로고
    • Novel poly-γ-glutamate-processing enzyme catalyzing γ-glutamyl DD-amidohydrolysis
    • Ashiuchi M, Nakamura H, Yamamoto M and Misono H, Novel poly-γ-glutamate-processing enzyme catalyzing γ-glutamyl DD-amidohydrolysis. J Biosci Bioeng 102:60-65 (2006).
    • (2006) J Biosci Bioeng , vol.102 , pp. 60-65
    • Ashiuchi, M.1    Nakamura, H.2    Yamamoto, M.3    Misono, H.4
  • 15
  • 16
    • 84856796707 scopus 로고    scopus 로고
    • Enzymatic degradation of poly-γ-glutamic acid
    • ed by Hamano Y. Springer, New York
    • Kimura K and Fujimoto Z, Enzymatic degradation of poly-γ-glutamic acid, in Amino-Acid Homopolymers Occurring in Nature, ed by Hamano Y. Springer, New York, 95-117 (2010).
    • (2010) Amino-Acid Homopolymers Occurring in Nature , pp. 95-117
    • Kimura, K.1    Fujimoto, Z.2
  • 17
    • 11044230062 scopus 로고    scopus 로고
    • Characterization of Bacillus subtilis γ-glutamyltransferase and its involvement in the degradation of capsule poly-γ-glutamate
    • Kimura K, Tran LSP, Uchida I and Itoh Y, Characterization of Bacillus subtilis γ-glutamyltransferase and its involvement in the degradation of capsule poly-γ-glutamate. Microbiology 150:4115-4123 (2004).
    • (2004) Microbiology , vol.150 , pp. 4115-4123
    • Kimura, K.1    Tran, L.S.P.2    Uchida, I.3    Itoh, Y.4
  • 18
    • 79954497873 scopus 로고    scopus 로고
    • Disruption of the cell wall lytic enzyme CwlO affects the amount and molecular size of poly-γ-glutamic acid produced by Bacillus subtilis (natto)
    • Mitsui N, Murasawa H and Sekiguchi J, Disruption of the cell wall lytic enzyme CwlO affects the amount and molecular size of poly-γ-glutamic acid produced by Bacillus subtilis (natto). J Gen Appl Microbiol 57:35-43 (2011).
    • (2011) J Gen Appl Microbiol , vol.57 , pp. 35-43
    • Mitsui, N.1    Murasawa, H.2    Sekiguchi, J.3
  • 20
    • 77949291926 scopus 로고    scopus 로고
    • Isolation of halotolerant Bacillus licheniformis WX-02 and regulatory effects of sodium chloride on yield and molecular sizes of Poly-γ-Glutamic acid
    • Wei XT, Ji ZX and Chen SW, Isolation of halotolerant Bacillus licheniformis WX-02 and regulatory effects of sodium chloride on yield and molecular sizes of Poly-γ-Glutamic acid. Appl Biochem Biotechnol 160:1332-1340 (2010).
    • (2010) Appl Biochem Biotechnol , vol.160 , pp. 1332-1340
    • Wei, X.T.1    Ji, Z.X.2    Chen, S.W.3
  • 22
    • 0003252192 scopus 로고    scopus 로고
    • Plasmids and their usefulness in molecular cloning
    • 3rd edn. Cold Spring Harbor Laboratory Press, New York
    • Sambrook J and Russell DW, Plasmids and their usefulness in molecular cloning, in Molecular Cloning: A Laboratory Manual, 3rd edn. Cold Spring Harbor Laboratory Press, New York, 1803-2500 (2001).
    • (2001) Molecular Cloning: A Laboratory Manual , pp. 1803-2500
    • Sambrook, J.1    Russell, D.W.2
  • 23
    • 0025326334 scopus 로고
    • Gene splicing by overlap extension: tailor-made genes using the polymerase chain reaction
    • Horton RM, Cai ZL, Ho SN and Pease LR, Gene splicing by overlap extension: tailor-made genes using the polymerase chain reaction. BioTechniques 8:528-535 (1990).
    • (1990) BioTechniques , vol.8 , pp. 528-535
    • Horton, R.M.1    Cai, Z.L.2    Ho, S.N.3    Pease, L.R.4
  • 24
    • 0032972099 scopus 로고    scopus 로고
    • High osmolarity improves the electro-transformation efficiency of the gram-positive bacteria Bacillus subtilis and Bacillus licheniformis
    • Xue G-P, Johnson JS and Dalrymple BP, High osmolarity improves the electro-transformation efficiency of the gram-positive bacteria Bacillus subtilis and Bacillus licheniformis. J Microbiol Methods 34:183-191 (1999).
    • (1999) J Microbiol Methods , vol.34 , pp. 183-191
    • Xue, G.-P.1    Johnson, J.S.2    Dalrymple, B.P.3
  • 25
    • 0021355340 scopus 로고
    • A method for the quantitative recovery of protein in dilute solution in the presence of detergents and lipids
    • Wessel D and Flugge UI, A method for the quantitative recovery of protein in dilute solution in the presence of detergents and lipids. Analytic Biochem 138:141-143 (1984).
    • (1984) Analytic Biochem , vol.138 , pp. 141-143
    • Wessel, D.1    Flugge, U.I.2
  • 26
    • 37849010306 scopus 로고    scopus 로고
    • Comparison and validation of methods to quantify Cry1Ab toxin from Bacillus thuringiensis for standardization of insect bioassay
    • Crespo ALB, Spencer TA, Nekl E, Pusztai-Carey M, Moar WJ and Siegfried BD, Comparison and validation of methods to quantify Cry1Ab toxin from Bacillus thuringiensis for standardization of insect bioassay. Appl Environ Microbiol 74:130-135 (2008).
    • (2008) Appl Environ Microbiol , vol.74 , pp. 130-135
    • Crespo, A.L.B.1    Spencer, T.A.2    Nekl, E.3    Pusztai-Carey, M.4    Moar, W.J.5    Siegfried, B.D.6
  • 27
    • 0035151837 scopus 로고    scopus 로고
    • Efficient recovery of γ-poly (glutamic acid) from highly viscous culture broth
    • Do JH, Chang HN and Lee SY, Efficient recovery of γ-poly (glutamic acid) from highly viscous culture broth. Biotechnol Bioeng 76:219-223 (2001).
    • (2001) Biotechnol Bioeng , vol.76 , pp. 219-223
    • Do, J.H.1    Chang, H.N.2    Lee, S.Y.3
  • 28
    • 33845870649 scopus 로고    scopus 로고
    • Removal of Cr(III), Ni(II) and Cu(II) by poly(γ-glutamic acid) from Bacillus subtilis NX-2
    • Yao J, Xu H, Wang J, Jiang M and Ouyang PK, Removal of Cr(III), Ni(II) and Cu(II) by poly(γ-glutamic acid) from Bacillus subtilis NX-2. J Biomater Sci - Polym Ed 18:193-204 (2007).
    • (2007) J Biomater Sci - Polym Ed , vol.18 , pp. 193-204
    • Yao, J.1    Xu, H.2    Wang, J.3    Jiang, M.4    Ouyang, P.K.5
  • 29
    • 34247476128 scopus 로고    scopus 로고
    • Salt-inducible bionylon polymer from Bacillus megaterium
    • Shimizu K, Nakamura H and Ashiuchi M, Salt-inducible bionylon polymer from Bacillus megaterium. Appl Environ Microbiol 73:2378-2379 (2007).
    • (2007) Appl Environ Microbiol , vol.73 , pp. 2378-2379
    • Shimizu, K.1    Nakamura, H.2    Ashiuchi, M.3
  • 30
    • 0033802118 scopus 로고    scopus 로고
    • Polymer production by two newly isolated extremely halophilic archaea: application of a novel corrosion-resistant bioreactor
    • Hezayen F, Rehm B, Eberhardt R and Steinbüchel A, Polymer production by two newly isolated extremely halophilic archaea: application of a novel corrosion-resistant bioreactor. Appl Microbiol Biotechnol 54:319-325 (2000).
    • (2000) Appl Microbiol Biotechnol , vol.54 , pp. 319-325
    • Hezayen, F.1    Rehm, B.2    Eberhardt, R.3    Steinbüchel, A.4
  • 31
    • 0037545836 scopus 로고    scopus 로고
    • Characterization of poly-γ-glutamate hydrolase encoded by a bacteriophage genome: possible role in phage infection of Bacillus subtilis encapsulated with poly-γ-glutamate
    • Kimura K and Itoh Y, Characterization of poly-γ-glutamate hydrolase encoded by a bacteriophage genome: possible role in phage infection of Bacillus subtilis encapsulated with poly-γ-glutamate. Appl Environ Microbiol 69:2491-2497 (2003).
    • (2003) Appl Environ Microbiol , vol.69 , pp. 2491-2497
    • Kimura, K.1    Itoh, Y.2
  • 32
    • 0642374442 scopus 로고
    • A modified ninhydrin reagent for the photometric determination of amino acids and related compounds
    • Moore S and Stein WH, A modified ninhydrin reagent for the photometric determination of amino acids and related compounds. J Biological Chem 211:907-913 (1954).
    • (1954) J Biological Chem , vol.211 , pp. 907-913
    • Moore, S.1    Stein, W.H.2
  • 33
    • 43549124764 scopus 로고    scopus 로고
    • Selection of the internal control gene for real-time quantitative RT-PCR assays in temperature treated Leptospira
    • Carrillo-Casas EM, Hernández-Castro R, Suárez-Güemes F and de la Pena-Moctezuma A, Selection of the internal control gene for real-time quantitative RT-PCR assays in temperature treated Leptospira. Curr Microbiol 56:539-546 (2008).
    • (2008) Curr Microbiol , vol.56 , pp. 539-546
    • Carrillo-Casas, E.M.1    Hernández-Castro, R.2    Suárez-Güemes, F.3    de la Pena-Moctezuma, A.4
  • 34
    • 33947626585 scopus 로고    scopus 로고
    • Calcium-dependent conformational changes in guanylate cyclase-activating protein 2 monitored by cysteine accessibility
    • Helten A and Koch KW, Calcium-dependent conformational changes in guanylate cyclase-activating protein 2 monitored by cysteine accessibility. Biochem Biophys Res Commun 356:687-692 (2007).
    • (2007) Biochem Biophys Res Commun , vol.356 , pp. 687-692
    • Helten, A.1    Koch, K.W.2
  • 35
    • 0036097461 scopus 로고    scopus 로고
    • Cloning and molecular characterization of a SDS-activated tyrosinase from Marinomonas mediterranea
    • Lopez-Serrano D, Sanchez-Amat A and Solano F, Cloning and molecular characterization of a SDS-activated tyrosinase from Marinomonas mediterranea. Pigment Cell Res 15:104-111 (2002).
    • (2002) Pigment Cell Res , vol.15 , pp. 104-111
    • Lopez-Serrano, D.1    Sanchez-Amat, A.2    Solano, F.3
  • 36
    • 85007856438 scopus 로고
    • Purification and characterization of poly (γ-glutamic acid) hydrolase from a filamentous fungus, Myrothecium sp. TM-4222
    • Tanaka T, Hiruta O, Futamura T, UoTAN K and Satoh A, Purification and characterization of poly (γ-glutamic acid) hydrolase from a filamentous fungus, Myrothecium sp. TM-4222. Biosci Biotechnol Biochem 57:2148-2153 (1993).
    • (1993) Biosci Biotechnol Biochem , vol.57 , pp. 2148-2153
    • Tanaka, T.1    Hiruta, O.2    Futamura, T.3    Uotan, K.4    Satoh, A.5
  • 37
    • 0142152598 scopus 로고    scopus 로고
    • Antifreeze activities of poly(γ-glutamic acid) produced by Bacillus licheniformis
    • Shih IL, Van YT and Sau YY, Antifreeze activities of poly(γ-glutamic acid) produced by Bacillus licheniformis. Biotechnol Lett 25:1709-1712 (2003).
    • (2003) Biotechnol Lett , vol.25 , pp. 1709-1712
    • Shih, I.L.1    Van, Y.T.2    Sau, Y.Y.3
  • 38
    • 0034946131 scopus 로고    scopus 로고
    • The production of poly-(γ-glutamic acid) from microorganisms and its various applications
    • Shih I-L and Van Y-T, The production of poly-(γ-glutamic acid) from microorganisms and its various applications. Bioresource Technol 79:207-225 (2001).
    • (2001) Bioresource Technol , vol.79 , pp. 207-225
    • Shih, I.-L.1    Van, Y.-T.2
  • 39
    • 33745289074 scopus 로고    scopus 로고
    • Poly-gamma-glutamate in bacteria
    • Candela T and Fouet A, Poly-gamma-glutamate in bacteria. Molecul Microbiol 60:1091-1098 (2006).
    • (2006) Molecul Microbiol , vol.60 , pp. 1091-1098
    • Candela, T.1    Fouet, A.2
  • 40
    • 0242424106 scopus 로고    scopus 로고
    • Trimeric subunit stoichiometry of the glutamate transporters from Bacillus caldotenax and Bacillus stearothermophilus
    • Yernool D, Boudker O, Folta-Stogniew E and Gouaux E, Trimeric subunit stoichiometry of the glutamate transporters from Bacillus caldotenax and Bacillus stearothermophilus. Biochemistry 42:12981-12988 (2003).
    • (2003) Biochemistry , vol.42 , pp. 12981-12988
    • Yernool, D.1    Boudker, O.2    Folta-Stogniew, E.3    Gouaux, E.4
  • 41
    • 0036323007 scopus 로고    scopus 로고
    • Biochemistry and molecular genetics of poly-γ-glutamate synthesis
    • Ashiuchi M and Misono H, Biochemistry and molecular genetics of poly-γ-glutamate synthesis. Appl Microbiol Biotechnol 59:9-14 (2002).
    • (2002) Appl Microbiol Biotechnol , vol.59 , pp. 9-14
    • Ashiuchi, M.1    Misono, H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.