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Volumn 146, Issue , 2013, Pages 543-548

High-level extracellular production of alkaline polygalacturonate lyase in Bacillus subtilis with optimized regulatory elements

Author keywords

Alkaline polygalacturonate lyase; Bacillus subtilis; Bpr; Promoter P43; Signal peptide

Indexed keywords

OPTIMIZATION;

EID: 84882962610     PISSN: 09608524     EISSN: 18732976     Source Type: Journal    
DOI: 10.1016/j.biortech.2013.07.129     Document Type: Article
Times cited : (62)

References (35)
  • 2
    • 1642348275 scopus 로고    scopus 로고
    • Effect of signal peptide on the stability and folding kinetics of maltose binding protein
    • Beena K., Udgaonkar J.B., Varadarajan R. Effect of signal peptide on the stability and folding kinetics of maltose binding protein. Biochemistry 2004, 43:3608-3619.
    • (2004) Biochemistry , vol.43 , pp. 3608-3619
    • Beena, K.1    Udgaonkar, J.B.2    Varadarajan, R.3
  • 3
    • 2542478112 scopus 로고    scopus 로고
    • Cloning of the pelA gene from Bacillus licheniformis 14A and biochemical characterization of recombinant, thermostable, high-alkaline pectate lyase
    • Berensmeier S., Singh S.A., Meens J., Buchholz K. Cloning of the pelA gene from Bacillus licheniformis 14A and biochemical characterization of recombinant, thermostable, high-alkaline pectate lyase. Appl. Microbiol. Biotechnol. 2004, 64:560-567.
    • (2004) Appl. Microbiol. Biotechnol. , vol.64 , pp. 560-567
    • Berensmeier, S.1    Singh, S.A.2    Meens, J.3    Buchholz, K.4
  • 4
    • 0035163555 scopus 로고    scopus 로고
    • Development and characterization of a xylose-dependent system for expression of cloned genes in Bacillus subtilis: conditional complementation of a teichoic acid mutant
    • Bhavsar A.P., Zhao X., Brown E.D. Development and characterization of a xylose-dependent system for expression of cloned genes in Bacillus subtilis: conditional complementation of a teichoic acid mutant. Appl. Environ. Microbiol. 2001, 67:403-410.
    • (2001) Appl. Environ. Microbiol. , vol.67 , pp. 403-410
    • Bhavsar, A.P.1    Zhao, X.2    Brown, E.D.3
  • 5
    • 33748101074 scopus 로고    scopus 로고
    • Systematic screening of all signal peptides fromBacillus subtilis: a powerful strategy in optimizing heterologous protein secretion in gram-positive bacteria
    • Brockmeier U., Caspers M., Freudl R., Jockwer A., Noll T., Eggert T. Systematic screening of all signal peptides fromBacillus subtilis: a powerful strategy in optimizing heterologous protein secretion in gram-positive bacteria. J. Mol. Biol. 2006, 362:393-402.
    • (2006) J. Mol. Biol. , vol.362 , pp. 393-402
    • Brockmeier, U.1    Caspers, M.2    Freudl, R.3    Jockwer, A.4    Noll, T.5    Eggert, T.6
  • 6
    • 78049311718 scopus 로고    scopus 로고
    • Optimization of protease secretion in Bacillus subtilis and Bacillus licheniformis by screening of homologous and heterologous signal peptides
    • Degering C., Eggert T., Puls M., Bongaerts J., Evers S., Maurer K.H., Jaeger K.E. Optimization of protease secretion in Bacillus subtilis and Bacillus licheniformis by screening of homologous and heterologous signal peptides. Appl. Environ. Microbiol. 2010, 76:6370-6376.
    • (2010) Appl. Environ. Microbiol. , vol.76 , pp. 6370-6376
    • Degering, C.1    Eggert, T.2    Puls, M.3    Bongaerts, J.4    Evers, S.5    Maurer, K.H.6    Jaeger, K.E.7
  • 7
    • 80054843297 scopus 로고    scopus 로고
    • Overproduction of alkaline polygalacturonate lyase in recombinant Escherichia coli by a two-stage glycerol feeding approach
    • Fang S., 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. Bioresour. Technol. 2011, 102:10671-10678.
    • (2011) Bioresour. Technol. , vol.102 , pp. 10671-10678
    • Fang, S.1    Li, J.H.2    Liu, L.3    Du, G.C.4    Chen, J.5
  • 8
    • 33845946823 scopus 로고    scopus 로고
    • Protein secretion pathways in Bacillus subtilis: implication for optimization of heterologous protein secretion
    • Fu L.L., Xu Z.R., Li W.F., Shuai J.B., Lu P., Hu C.X. Protein secretion pathways in Bacillus subtilis: implication for optimization of heterologous protein secretion. Biotechnol. Adv. 2007, 25:1-12.
    • (2007) Biotechnol. Adv. , vol.25 , pp. 1-12
    • Fu, L.L.1    Xu, Z.R.2    Li, W.F.3    Shuai, J.B.4    Lu, P.5    Hu, C.X.6
  • 9
    • 39049125071 scopus 로고    scopus 로고
    • Bacillus protein secretion: an unfolding story
    • Harwood C.R., Cranenburgh R. Bacillus protein secretion: an unfolding story. Trends Microbiol. 2008, 16:73-79.
    • (2008) Trends Microbiol. , vol.16 , pp. 73-79
    • Harwood, C.R.1    Cranenburgh, R.2
  • 11
    • 22544467018 scopus 로고    scopus 로고
    • Microbial pectinolytic enzymes: a review
    • Jayani R.S., Saxena S., Gupta R. Microbial pectinolytic enzymes: a review. Process Biochem. 2005, 40:2931-2944.
    • (2005) Process Biochem. , vol.40 , pp. 2931-2944
    • Jayani, R.S.1    Saxena, S.2    Gupta, R.3
  • 12
    • 47749104151 scopus 로고    scopus 로고
    • Effect of pectate lyase bioscouring on physical, chemical and low-stress mechanical properties of cotton fabrics
    • Kalantzi S., Mamma D., Christakopoulos P., Kekos D. Effect of pectate lyase bioscouring on physical, chemical and low-stress mechanical properties of cotton fabrics. Bioresour. Technol. 2008, 99:8185-8192.
    • (2008) Bioresour. Technol. , vol.99 , pp. 8185-8192
    • Kalantzi, S.1    Mamma, D.2    Christakopoulos, P.3    Kekos, D.4
  • 13
    • 0035191237 scopus 로고    scopus 로고
    • Applications of pectinases in the commercial sector: a review
    • Kashyap D.R., Vohra P.K., Chopra S., Tewari R. Applications of pectinases in the commercial sector: a review. Bioresour. Technol. 2001, 77:215-227.
    • (2001) Bioresour. Technol. , vol.77 , pp. 215-227
    • Kashyap, D.R.1    Vohra, P.K.2    Chopra, S.3    Tewari, R.4
  • 14
    • 3442891534 scopus 로고    scopus 로고
    • Enhanced production of an alkaline pectinase from Streptomyces sp RCK-SC by whole-cell immobilization and solid-state cultivation
    • Kuhad R.C., Kapoor M., Rustagi R. Enhanced production of an alkaline pectinase from Streptomyces sp RCK-SC by whole-cell immobilization and solid-state cultivation. World J. Microbiol. Biotechnol. 2004, 20:257-263.
    • (2004) World J. Microbiol. Biotechnol. , vol.20 , pp. 257-263
    • Kuhad, R.C.1    Kapoor, M.2    Rustagi, R.3
  • 15
    • 0034115482 scopus 로고    scopus 로고
    • Production of pectate lyases and cellulases by Chryseomonas luteola strain MFCL0 depends on the growth temperature and the nature of the culture medium: evidence for two critical temperatures
    • Laurent P., Buchon L., Guespin-Michel J.F., Orange N. Production of pectate lyases and cellulases by Chryseomonas luteola strain MFCL0 depends on the growth temperature and the nature of the culture medium: evidence for two critical temperatures. Appl. Environ. Microbiol. 2000, 66:1538-1543.
    • (2000) Appl. Environ. Microbiol. , vol.66 , pp. 1538-1543
    • Laurent, P.1    Buchon, L.2    Guespin-Michel, J.F.3    Orange, N.4
  • 16
    • 77954994527 scopus 로고    scopus 로고
    • Cloning, expression, and characterization of a highly active alkaline pectate lyase from alkaliphilic Bacillus sp. N16-5
    • Li G., Rao L., Xue Y., Zhou C., Zhang Y., Ma Y.H. Cloning, expression, and characterization of a highly active alkaline pectate lyase from alkaliphilic Bacillus sp. N16-5. J. Microbiol. Biotechnol. 2010, 20:670-677.
    • (2010) J. Microbiol. Biotechnol. , vol.20 , pp. 670-677
    • Li, G.1    Rao, L.2    Xue, Y.3    Zhou, C.4    Zhang, Y.5    Ma, Y.H.6
  • 17
    • 0036883453 scopus 로고    scopus 로고
    • Efficient secretory overexpression of Bacillus subtilis pectate lyase in Escherichia coli and single-step purification
    • Matsumoto T., Katsura D., Kondo A., Fukuda H. Efficient secretory overexpression of Bacillus subtilis pectate lyase in Escherichia coli and single-step purification. Biochem. Eng. J. 2002, 12:175-179.
    • (2002) Biochem. Eng. J. , vol.12 , pp. 175-179
    • Matsumoto, T.1    Katsura, D.2    Kondo, A.3    Fukuda, H.4
  • 18
    • 0034200611 scopus 로고    scopus 로고
    • A new high-alkaline and high-molecular-weight pectate lyase from a Bacillus isolate: enzymatic properties and cloning of the gene for the enzyme
    • Ogawa A., Sawada K., Saito K., Hakamada Y., Sumitomo N., Hatada Y., Kobayashi T., Ito S. A new high-alkaline and high-molecular-weight pectate lyase from a Bacillus isolate: enzymatic properties and cloning of the gene for the enzyme. Biosci. Biotechnol. Biochem. 2000, 64:1133-1141.
    • (2000) Biosci. Biotechnol. Biochem. , vol.64 , pp. 1133-1141
    • Ogawa, A.1    Sawada, K.2    Saito, K.3    Hakamada, Y.4    Sumitomo, N.5    Hatada, Y.6    Kobayashi, T.7    Ito, S.8
  • 19
    • 77956107104 scopus 로고    scopus 로고
    • Heterologous protein secretion by Bacillus species from the cradle to the grave
    • Pohl S., Harwood C.R. Heterologous protein secretion by Bacillus species from the cradle to the grave. Adv. Appl. Microbiol. 2010, 73:1-25.
    • (2010) Adv. Appl. Microbiol. , vol.73 , pp. 1-25
    • Pohl, S.1    Harwood, C.R.2
  • 20
    • 0023652058 scopus 로고
    • Synonymous codon usage in Bacillus subtilis reflects both translational selection and mutational biases
    • Shields D.C., Sharp P.M. Synonymous codon usage in Bacillus subtilis reflects both translational selection and mutational biases. Nucleic Acids Res. 1987, 15:8023-8040.
    • (1987) Nucleic Acids Res. , vol.15 , pp. 8023-8040
    • Shields, D.C.1    Sharp, P.M.2
  • 21
    • 0033818171 scopus 로고    scopus 로고
    • Signal peptide-dependent protein transport in Bacillus subtilis: a genome-based survey of the secretome
    • Tjalsma H., Bolhuis A., Jongbloed J.D., Bron S., van Dijl J.M. Signal peptide-dependent protein transport in Bacillus subtilis: a genome-based survey of the secretome. Microbiol. Mol. Biol. Rev. 2000, 64:515-547.
    • (2000) Microbiol. Mol. Biol. Rev. , vol.64 , pp. 515-547
    • Tjalsma, H.1    Bolhuis, A.2    Jongbloed, J.D.3    Bron, S.4    van Dijl, J.M.5
  • 22
    • 38849120689 scopus 로고    scopus 로고
    • Characterization of DegU-dependent expression of bpr in Bacillus subtilis
    • Tsukahara K., Ogura M. Characterization of DegU-dependent expression of bpr in Bacillus subtilis. FEMS Microbiol. Lett. 2008, 280:8-13.
    • (2008) FEMS Microbiol. Lett. , vol.280 , pp. 8-13
    • Tsukahara, K.1    Ogura, M.2
  • 23
    • 84872143710 scopus 로고    scopus 로고
    • Bacillus subtilis: from soil bacterium to super-secreting cell factory
    • van Dijl J.M., Hecker M. Bacillus subtilis: from soil bacterium to super-secreting cell factory. Microb. Cell Fact. 2013, 12:3.
    • (2013) Microb. Cell Fact. , vol.12 , pp. 3
    • van Dijl, J.M.1    Hecker, M.2
  • 24
    • 0021243550 scopus 로고
    • Overlapping promoters transcribed by Bacillus subtilis sigma 55 and sigma 37 RNA polymerase holoenzymes during growth and stationary phases
    • Wang P.Z., Doi R.H. Overlapping promoters transcribed by Bacillus subtilis sigma 55 and sigma 37 RNA polymerase holoenzymes during growth and stationary phases. J. Biol. Chem. 1984, 259:8619-8625.
    • (1984) J. Biol. Chem. , vol.259 , pp. 8619-8625
    • Wang, P.Z.1    Doi, R.H.2
  • 25
    • 55549131481 scopus 로고    scopus 로고
    • Enhancement of alkaline polygalacturonate lyase production in recombinant Pichia pastoris according to the ratio of methanol to cell concentration
    • Wang Y., Wang Z.H., Du G.C., Hua Z.Z., Liu L.M., Li J.H., Chen J. Enhancement of alkaline polygalacturonate lyase production in recombinant Pichia pastoris according to the ratio of methanol to cell concentration. Bioresour. Technol. 2009, 100:1343-1349.
    • (2009) Bioresour. Technol. , vol.100 , pp. 1343-1349
    • Wang, Y.1    Wang, Z.H.2    Du, G.C.3    Hua, Z.Z.4    Liu, L.M.5    Li, J.H.6    Chen, J.7
  • 26
    • 71549114849 scopus 로고    scopus 로고
    • Enhancement of cell viability and alkaline polygalacturonate lyase production by sorbitol co-feeding with methanol in Pichia pastoris fermentation
    • Wang Z.H., Wang Y., Zhang D.X., Li J.H., Hua Z.Z., Do G.C., Chen J. Enhancement of cell viability and alkaline polygalacturonate lyase production by sorbitol co-feeding with methanol in Pichia pastoris fermentation. Bioresour. Technol. 2010, 101:1318-1323.
    • (2010) Bioresour. Technol. , vol.101 , pp. 1318-1323
    • Wang, Z.H.1    Wang, Y.2    Zhang, D.X.3    Li, J.H.4    Hua, Z.Z.5    Do, G.C.6    Chen, J.7
  • 27
    • 84866163996 scopus 로고    scopus 로고
    • Increased production of alkaline polygalacturonate lyase in the recombinant Pichia pastoris by controlling cell concentration during continuous culture
    • Wang H.L., Li J.H., Liu L., Li X.M., Jia D.X., Du G.C., Chen J., Song J.N. Increased production of alkaline polygalacturonate lyase in the recombinant Pichia pastoris by controlling cell concentration during continuous culture. Bioresour. Technol. 2012, 124:338-346.
    • (2012) Bioresour. Technol. , vol.124 , pp. 338-346
    • Wang, H.L.1    Li, J.H.2    Liu, L.3    Li, X.M.4    Jia, D.X.5    Du, G.C.6    Chen, J.7    Song, J.N.8
  • 28
    • 8844278305 scopus 로고    scopus 로고
    • Bacillus subtilis as cell factory for pharmaceutical proteins: a biotechnological approach to optimize the host organism
    • Westers L., Westers H., Quax W.J. Bacillus subtilis as cell factory for pharmaceutical proteins: a biotechnological approach to optimize the host organism. Biochim. Biophys. Acta 2004, 1694:299-310.
    • (2004) Biochim. Biophys. Acta , vol.1694 , pp. 299-310
    • Westers, L.1    Westers, H.2    Quax, W.J.3
  • 30
    • 22144475150 scopus 로고    scopus 로고
    • High-level expression and secretion of methyl parathion hydrolase in Bacillus subtilis WB800
    • Zhang X.Z., Cui Z.L., Hong Q., Li S.P. High-level expression and secretion of methyl parathion hydrolase in Bacillus subtilis WB800. Appl. Environ. Microbiol. 2005, 71:4101-4103.
    • (2005) Appl. Environ. Microbiol. , vol.71 , pp. 4101-4103
    • Zhang, X.Z.1    Cui, Z.L.2    Hong, Q.3    Li, S.P.4
  • 31
    • 79958703776 scopus 로고    scopus 로고
    • One-step production of lactate from cellulose as the sole carbon source without any other organic nutrient by recombinant cellulolytic Bacillus subtilis
    • Zhang X.Z., Sathitsuksanoh N., Zhu Z., Percival Zhang Y.H. One-step production of lactate from cellulose as the sole carbon source without any other organic nutrient by recombinant cellulolytic Bacillus subtilis. Metab. Eng. 2011, 13:364-372.
    • (2011) Metab. Eng. , vol.13 , pp. 364-372
    • Zhang, X.Z.1    Sathitsuksanoh, N.2    Zhu, Z.3    Percival Zhang, Y.H.4
  • 32
    • 84875036107 scopus 로고    scopus 로고
    • The alkaline pectate lyase PEL168 of Bacillus subtilis heterologously expressed in Pichia pastoris is more stable and efficient for degumming ramie fiber
    • Zhang C., Yao J., Zhou C., Mao L., Zhang G., Ma Y. The alkaline pectate lyase PEL168 of Bacillus subtilis heterologously expressed in Pichia pastoris is more stable and efficient for degumming ramie fiber. BMC Biotechnol. 2013, 13:26.
    • (2013) BMC Biotechnol. , vol.13 , pp. 26
    • Zhang, C.1    Yao, J.2    Zhou, C.3    Mao, L.4    Zhang, G.5    Ma, Y.6
  • 33
    • 33847256067 scopus 로고    scopus 로고
    • Efficient secretory expression of an alkaline pectate lyase gene from Bacillus subtilis in E. coli and the purification and characterization of the protein
    • Zhuge B., Du G.C., Shen W., Zhuge J., Chen J. Efficient secretory expression of an alkaline pectate lyase gene from Bacillus subtilis in E. coli and the purification and characterization of the protein. Biotechnol. Lett. 2007, 29:405-410.
    • (2007) Biotechnol. Lett. , vol.29 , pp. 405-410
    • Zhuge, B.1    Du, G.C.2    Shen, W.3    Zhuge, J.4    Chen, J.5
  • 34
    • 42949179630 scopus 로고    scopus 로고
    • Expression of a Bacillus subtilis pectate lyase gene in Pichia pastoris
    • Zhuge B., Du G.C., Shen W., Zhuge J., Chen J. Expression of a Bacillus subtilis pectate lyase gene in Pichia pastoris. Biochem. Eng. J. 2008, 40:92-98.
    • (2008) Biochem. Eng. J. , vol.40 , pp. 92-98
    • Zhuge, B.1    Du, G.C.2    Shen, W.3    Zhuge, J.4    Chen, J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.