메뉴 건너뛰기




Volumn 168, Issue 4, 2013, Pages 607-615

High-level expression of glutaryl-7-aminocephalosporanic acid acylase from Pseudomonas diminuta NK703 in Escherichia coli by combined optimization strategies

Author keywords

Glutaryl 7 aminocephalosporanic acid acylase (GLA); Lactose induction; Pseudomonas diminuta; Soluble expression

Indexed keywords

GLUTARYL-7-AMINOCEPHALOSPORANIC ACID ACYLASE; HIGH LEVEL EXPRESSION; LACTOSE INDUCTION; OPTIMIZATION STRATEGY; OPTIMIZED CONDITIONS; PSEUDOMONAS DIMINUTA; SOLUBLE EXPRESSION; TOTAL SOLUBLE PROTEIN;

EID: 84888820418     PISSN: 01681656     EISSN: 18734863     Source Type: Journal    
DOI: 10.1016/j.jbiotec.2013.08.024     Document Type: Article
Times cited : (15)

References (22)
  • 2
    • 0017184389 scopus 로고
    • A rapid and sensitive method for quantitation of microgram amounts of protein using the principal of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for quantitation of microgram amounts of protein using the principal of protein-dye binding. Analytical Biochemistry 1976, 72:248-254.
    • (1976) Analytical Biochemistry , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 3
    • 0029892121 scopus 로고    scopus 로고
    • Review: Optimizing inducer and culture conditions for expression of foreign proteins under the control of the lac promoter
    • Donovan R.S., Robinson C.W., Glick B.R. Review: Optimizing inducer and culture conditions for expression of foreign proteins under the control of the lac promoter. Journal of Industrial Microbiology 1996, 16:145-154.
    • (1996) Journal of Industrial Microbiology , vol.16 , pp. 145-154
    • Donovan, R.S.1    Robinson, C.W.2    Glick, B.R.3
  • 4
    • 80054843297 scopus 로고    scopus 로고
    • Overproduction of alkaline polygalacturonate lyase in recombinant Escherichia coli by a two-stage glycerol feeding approach
    • Fang S.Y., Li J.H., Liu L., Du G.C., Chen J. Overproduction of alkaline polygalacturonate lyase in recombinant Escherichia coli by a two-stage glycerol feeding approach. Bioresource Technology 2011, 102:10671-10678.
    • (2011) Bioresource Technology , vol.102 , pp. 10671-10678
    • Fang, S.Y.1    Li, J.H.2    Liu, L.3    Du, G.C.4    Chen, J.5
  • 5
    • 36049000963 scopus 로고    scopus 로고
    • Purification and immobilization of recombinant variants of Brevundimonas diminuta glutaryl-7-aminocephalosporanic acid acylase expressed in Escherichia coli cells
    • Khatuntseva S.A., El'darov M.A., Redo V.A., Skryabin K.G. Purification and immobilization of recombinant variants of Brevundimonas diminuta glutaryl-7-aminocephalosporanic acid acylase expressed in Escherichia coli cells. Journal of Biotechnology 2008, 133:123-126.
    • (2008) Journal of Biotechnology , vol.133 , pp. 123-126
    • Khatuntseva, S.A.1    El'darov, M.A.2    Redo, V.A.3    Skryabin, K.G.4
  • 6
    • 0034903834 scopus 로고    scopus 로고
    • Cloning and high expression of glutaryl 7-aminocephalosporanic acid acylase gene from Pseudomonas diminuta
    • Kim D.W., Yoon K.H. Cloning and high expression of glutaryl 7-aminocephalosporanic acid acylase gene from Pseudomonas diminuta. Biotechnology Letters 2001, 23:1067-1071.
    • (2001) Biotechnology Letters , vol.23 , pp. 1067-1071
    • Kim, D.W.1    Yoon, K.H.2
  • 8
    • 0034435442 scopus 로고    scopus 로고
    • The 2.0Å crystal structure of cephalosporin acylase
    • Kim Y., Yoon K., Khang Y., Turley S., Hol W.G.J. The 2.0Å crystal structure of cephalosporin acylase. Structure 2000, 8:1059-1068.
    • (2000) Structure , vol.8 , pp. 1059-1068
    • Kim, Y.1    Yoon, K.2    Khang, Y.3    Turley, S.4    Hol, W.G.J.5
  • 10
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970, 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 11
    • 0033564384 scopus 로고    scopus 로고
    • In vivo post-translational processing and subunit reconstitution of cephalosporin acylase from Pseudomonas sp
    • Li Y., Chen J.F., Jiang W.H., Mao X., Zhao G.P., Wang E.D. In vivo post-translational processing and subunit reconstitution of cephalosporin acylase from Pseudomonas sp. European Journal of Biochemistry 1999, 130(262):713-719.
    • (1999) European Journal of Biochemistry , vol.130 , Issue.262 , pp. 713-719
    • Li, Y.1    Chen, J.F.2    Jiang, W.H.3    Mao, X.4    Zhao, G.P.5    Wang, E.D.6
  • 12
    • 3042655014 scopus 로고    scopus 로고
    • Optimization of an industrial biocatalyst of glutaryl acylase: stabilization of the enzyme by multipoint covalent attachment onto new amino-epoxy sepabeads
    • López-Gallego F., Betancor L., Hidalgo A., Mateo C., Guisán J.M., Fernández-Lafuente R. Optimization of an industrial biocatalyst of glutaryl acylase: stabilization of the enzyme by multipoint covalent attachment onto new amino-epoxy sepabeads. Journal of Biotechnology 2004, 111:219-227.
    • (2004) Journal of Biotechnology , vol.111 , pp. 219-227
    • López-Gallego, F.1    Betancor, L.2    Hidalgo, A.3    Mateo, C.4    Guisán, J.M.5    Fernández-Lafuente, R.6
  • 14
    • 0141514470 scopus 로고    scopus 로고
    • Deacylation activity of cephalosporin acylase to cephalosporin C is improved by changing the side-chain conformations of active-site residues
    • Oh B., Kim M., Yoon J., Chung K., Shin Y., Lee D. Deacylation activity of cephalosporin acylase to cephalosporin C is improved by changing the side-chain conformations of active-site residues. Biochemical and Biophysical Research Communications 2003, 310:19-27.
    • (2003) Biochemical and Biophysical Research Communications , vol.310 , pp. 19-27
    • Oh, B.1    Kim, M.2    Yoon, J.3    Chung, K.4    Shin, Y.5    Lee, D.6
  • 17
    • 38549143777 scopus 로고    scopus 로고
    • Production of active eukaryotic proteins through bacterial expression systems: a review of the existing biotechnology strategies
    • Sahdev S., Khattar S.K., Saini K.S. Production of active eukaryotic proteins through bacterial expression systems: a review of the existing biotechnology strategies. Molecular and Cellular Biochemistry 2008, 307:249-264.
    • (2008) Molecular and Cellular Biochemistry , vol.307 , pp. 249-264
    • Sahdev, S.1    Khattar, S.K.2    Saini, K.S.3
  • 18
    • 33745727403 scopus 로고    scopus 로고
    • Enzymatic modifications of cephalosporins by cephalosporin acylase and other enzymes
    • Sonawane V.C. Enzymatic modifications of cephalosporins by cephalosporin acylase and other enzymes. Critical Reviews in Biotechnology 2006, 26:95-120.
    • (2006) Critical Reviews in Biotechnology , vol.26 , pp. 95-120
    • Sonawane, V.C.1
  • 19
    • 0033898359 scopus 로고    scopus 로고
    • Environmentally safe production of 7-aminodeacetoxycephalosporanic acid (7-ADCA) using recombinant strains of Acremonium chrysogenum
    • Velasco J., Adrio J.L., Moreno M.Á., Diez B., Soler G., Barredo J.L. Environmentally safe production of 7-aminodeacetoxycephalosporanic acid (7-ADCA) using recombinant strains of Acremonium chrysogenum. Nature Biotechnology 2000, 18:857-861.
    • (2000) Nature Biotechnology , vol.18 , pp. 857-861
    • Velasco, J.1    Adrio, J.L.2    Moreno, M.Á.3    Diez, B.4    Soler, G.5    Barredo, J.L.6
  • 21
    • 0035181565 scopus 로고    scopus 로고
    • Two novel engineered bacteria for secretory expression of glutaryl 7-amino-cephalosporanic acid acylase
    • Zheng Y.G., Li Y., Chen J.F., Jiang W.H., Zhao G.P., Wang E.D. Two novel engineered bacteria for secretory expression of glutaryl 7-amino-cephalosporanic acid acylase. Biotechnology Letters 2001, 23:1781-1787.
    • (2001) Biotechnology Letters , vol.23 , pp. 1781-1787
    • Zheng, Y.G.1    Li, Y.2    Chen, J.F.3    Jiang, W.H.4    Zhao, G.P.5    Wang, E.D.6
  • 22
    • 33847337324 scopus 로고    scopus 로고
    • Inducible and constitutive expression of glutaryl-7-aminocephalosporanic acid acylase by fusion to maltose-binding protein
    • Zhou H., Yu H.M., Luo H., Shi Y.Y., Ma X.F., Shen Z.Y. Inducible and constitutive expression of glutaryl-7-aminocephalosporanic acid acylase by fusion to maltose-binding protein. Enzyme and Microbial Technology 2007, 40:555-562.
    • (2007) Enzyme and Microbial Technology , vol.40 , pp. 555-562
    • Zhou, H.1    Yu, H.M.2    Luo, H.3    Shi, Y.Y.4    Ma, X.F.5    Shen, Z.Y.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.