메뉴 건너뛰기




Volumn 177, Issue 4, 2015, Pages 909-922

Cloning and Expression of Plantaricin W Produced by Lactobacillus plantarum U10 Isolate from “Tempoyak” Indonesian Fermented Food as Immunity Protein in Lactococcus lactis

Author keywords

Immunity; L. lactis; Plantaricin; PlnW; pNZ8148

Indexed keywords

ANTIBIOTICS; BACILLI; BACTERIA; CLONING;

EID: 84942818281     PISSN: 02732289     EISSN: 15590291     Source Type: Journal    
DOI: 10.1007/s12010-015-1786-9     Document Type: Article
Times cited : (12)

References (42)
  • 1
    • 84964294747 scopus 로고    scopus 로고
    • Fermentation of tempoyak using isolated tempoyak culture
    • Amiza, M. A., Zakiah, J., Ng, L. K., & Lai, K. W. (2006). Fermentation of tempoyak using isolated tempoyak culture. Res. J. Mirobiol., 1, 243–254.
    • (2006) Res. J. Mirobiol. , vol.1 , pp. 243-254
    • Amiza, M.A.1    Zakiah, J.2    Ng, L.K.3    Lai, K.W.4
  • 2
    • 70349326643 scopus 로고    scopus 로고
    • Influence of Pediococcus acidilactici as a starter on the flavor of tempoyak (fermented durian)
    • COI: 1:CAS:528:DC%2BD1MXht1WisbzP
    • Yuliana, N., & Garcia, V. V. (2009). Influence of Pediococcus acidilactici as a starter on the flavor of tempoyak (fermented durian). Indian Journal of Biotechnology, 8, 304–310.
    • (2009) Indian Journal of Biotechnology , vol.8 , pp. 304-310
    • Yuliana, N.1    Garcia, V.V.2
  • 3
    • 23044477877 scopus 로고    scopus 로고
    • Evidence on correlation between number of disulfide bridge and toxicity of class IIa bacteriocins
    • COI: 1:CAS:528:DC%2BD2MXntVGju7g%3D
    • Richard, C., Canon, R., Naghmouchi, K., Bertrand, D., Prevost, H., & Drider, D. (2006). Evidence on correlation between number of disulfide bridge and toxicity of class IIa bacteriocins. Food Microbiology, 23, 175–183.
    • (2006) Food Microbiology , vol.23 , pp. 175-183
    • Richard, C.1    Canon, R.2    Naghmouchi, K.3    Bertrand, D.4    Prevost, H.5    Drider, D.6
  • 4
    • 84961291389 scopus 로고    scopus 로고
    • Purification and characterization of bacteriocin produced by Lactobacillus brevis UN isolated dhulliachar: a traditional food product of Northeast India
    • COI: 1:CAS:528:DC%2BC2cXmvVWitLg%3D
    • Gautam, N., Sharma, N., & Ahlawat, O. P. (2014). Purification and characterization of bacteriocin produced by Lactobacillus brevis UN isolated dhulliachar: a traditional food product of Northeast India. Indian Journal of Microbiology, 54, 185–189.
    • (2014) Indian Journal of Microbiology , vol.54 , pp. 185-189
    • Gautam, N.1    Sharma, N.2    Ahlawat, O.P.3
  • 5
    • 84977509141 scopus 로고    scopus 로고
    • Partial characterization of bacteriocins from two Pediococcus acidilactici strains isolated during traditional sorghum beer processing in Côte d’Ivoire
    • Aka-Gbezo, S., N’Guessan, F. K., N’Dédé Djeni, T., Djè, M. K., & Bonfoh, B. (2014). Partial characterization of bacteriocins from two Pediococcus acidilactici strains isolated during traditional sorghum beer processing in Côte d’Ivoire. Adv Microbiol., 4, 1250–1259.
    • (2014) Adv Microbiol. , vol.4 , pp. 1250-1259
    • Aka-Gbezo, S.1    N’Guessan, F.K.2    N’Dédé Djeni, T.3    Djè, M.K.4    Bonfoh, B.5
  • 6
    • 84942826451 scopus 로고    scopus 로고
    • Isolation and characterization of Lactobacillus plantarum S34 from Indonesian traditional food. PhD thesis
    • Seoul: KR
    • Mustopa, A. Z. (2010). Isolation and characterization of Lactobacillus plantarum S34 from Indonesian traditional food. PhD thesis, Dankook University, Seoul, KR.
    • (2010) Dankook University
    • Mustopa, A.Z.1
  • 7
    • 84876496320 scopus 로고    scopus 로고
    • Isolation of bacteriocin-producing lactic acid bacteria from ‘ugba’ and ‘okpiye’, two locally fermented Nigerian food condiments
    • COI: 1:CAS:528:DC%2BC3sXpt1Onsb0%3D
    • Nwuche, C. O. (2013). Isolation of bacteriocin-producing lactic acid bacteria from ‘ugba’ and ‘okpiye’, two locally fermented Nigerian food condiments. Brazilian Archives of Biology and Technology, 56, 101–106.
    • (2013) Brazilian Archives of Biology and Technology , vol.56 , pp. 101-106
    • Nwuche, C.O.1
  • 8
    • 84977512359 scopus 로고    scopus 로고
    • Diversity of lactic acid bacteria isolated from Indonesian traditional fermented foods
    • Mustopa, A. Z., & Fatimah. (2014). Diversity of lactic acid bacteria isolated from Indonesian traditional fermented foods. Microbiol. Indones., 8, 48–57.
    • (2014) Microbiol. Indones. , vol.8 , pp. 48-57
    • Mustopa, A.Z.1
  • 9
    • 0029772572 scopus 로고    scopus 로고
    • Characterization of the locus responsible for the bacteriocin production in Lactobacillus plantarum C11
    • COI: 1:CAS:528:DyaK28Xks1Sks70%3D
    • Diep, D. B., Havarstein, L. S., & Nes, I. F. (1996). Characterization of the locus responsible for the bacteriocin production in Lactobacillus plantarum C11. Journal of Bacteriology, 178, 4472–4483.
    • (1996) Journal of Bacteriology , vol.178 , pp. 4472-4483
    • Diep, D.B.1    Havarstein, L.S.2    Nes, I.F.3
  • 10
    • 84858592725 scopus 로고    scopus 로고
    • Structure of plantaricin locus of Lactobacillus plantarum 8P-A3
    • COI: 1:CAS:528:DC%2BC38XitValur0%3D
    • Tsapieva, A., Duplik, N., & Suvorov, A. (2011). Structure of plantaricin locus of Lactobacillus plantarum 8P-A3. Benef. Microbes., 2, 255–261.
    • (2011) Benef. Microbes. , vol.2 , pp. 255-261
    • Tsapieva, A.1    Duplik, N.2    Suvorov, A.3
  • 11
    • 77950652492 scopus 로고    scopus 로고
    • The Abi proteins and their involvement in bacteriocin self-immunity
    • Kjos, M., Snipen, L., Salchian, Z., Nes, I. F., & Diep, D. B. (2010). The Abi proteins and their involvement in bacteriocin self-immunity. Journal of Bacteriology, 8, 2068–2076.
    • (2010) Journal of Bacteriology , vol.8 , pp. 2068-2076
    • Kjos, M.1    Snipen, L.2    Salchian, Z.3    Nes, I.F.4    Diep, D.B.5
  • 14
    • 84954358663 scopus 로고    scopus 로고
    • Therapeutic potential of type a (I) lantibiotics, a group of cationic peptide antibiotics
    • Smith, L., & Hillman, J. D. (2008). Therapeutic potential of type a (I) lantibiotics, a group of cationic peptide antibiotics. Current Opinion in Microbiology, 11, 401–408.
    • (2008) Current Opinion in Microbiology , vol.11 , pp. 401-408
    • Smith, L.1    Hillman, J.D.2
  • 16
    • 84898886958 scopus 로고    scopus 로고
    • Cloning and heterologous expression of plnE, -F, -J and –K genes derived from soil metagenome and purification of active plantaricin peptides
    • Pal, G., & Sheela, S. (2014). Cloning and heterologous expression of plnE, -F, -J and –K genes derived from soil metagenome and purification of active plantaricin peptides. Applied Microbiology and Biotechnology, 98, 1441–1447.
    • (2014) Applied Microbiology and Biotechnology , vol.98 , pp. 1441-1447
    • Pal, G.1    Sheela, S.2
  • 17
    • 84977469410 scopus 로고    scopus 로고
    • Construction, expression and purification of recombinant pre-mature peptide of plantaricin f from Lactobacillus plantarum S34 in Escherichia coli
    • Kusdianawati., Mustopa, A. Z., Suharsono., Budiarto, B. R., Fatimah., & Danuri, H. (2015). Construction, expression and purification of recombinant pre-mature peptide of plantaricin f from Lactobacillus plantarum S34 in Escherichia coli. IJAS, 16, 31–38.
    • (2015) IJAS , vol.16 , pp. 31-38
  • 18
    • 33748741796 scopus 로고    scopus 로고
    • Improved expression and purification of the correctly folded response regulator PlnC from lactobacilli
    • Straume, D., Axelsson, L., Nes, I. F., & Diep, D. B. (2006). Improved expression and purification of the correctly folded response regulator PlnC from lactobacilli. Journal of Microbiological Methods, 67, 193–201.
    • (2006) Journal of Microbiological Methods , vol.67 , pp. 193-201
    • Straume, D.1    Axelsson, L.2    Nes, I.F.3    Diep, D.B.4
  • 19
    • 84977534462 scopus 로고    scopus 로고
    • Expression of the immunity protein of plantaricin 423, produced by Lactobacillus plantarum 423, and analysis of the plasmid encoding the bacteriocin
    • Van Reenen, C. A., Chikindas, M. L., Van Zyl, W. H., & Dicks, L. M. T. (2002). Expression of the immunity protein of plantaricin 423, produced by Lactobacillus plantarum 423, and analysis of the plasmid encoding the bacteriocin. International Journal of Food Microbiology, 81, 29–40.
    • (2002) International Journal of Food Microbiology , vol.81 , pp. 29-40
    • Van Reenen, C.A.1    Chikindas, M.L.2    Van Zyl, W.H.3    Dicks, L.M.T.4
  • 21
    • 0004136246 scopus 로고    scopus 로고
    • Molecular Cloning: a laboratory manual (vol
    • Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press
    • Sambrook, J., & Russell, D. W. (2001). Molecular Cloning: a laboratory manual (vol. 3). Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press.
    • (2001) 3)
    • Sambrook, J.1    Russell, D.W.2
  • 22
    • 0032884466 scopus 로고    scopus 로고
    • Rapid plasmid DNA isolation from Lactococcus lactis using overnight cultures
    • Duan, K., Dunn, N. W., & Kim, W. S. (1999). Rapid plasmid DNA isolation from Lactococcus lactis using overnight cultures. Biotechnol. Techniques. 13, 519–521.
    • (1999) Biotechnol. Techniques , vol.13 , pp. 519-521
    • Duan, K.1    Dunn, N.W.2    Kim, W.S.3
  • 23
    • 84894258646 scopus 로고    scopus 로고
    • Protter: interactive protein feature visualization and integration with experimental proteomic data
    • Omasits, U., Ahrens, C. H., Muller, S., & Wollscheid, B. (2013). Protter: interactive protein feature visualization and integration with experimental proteomic data. Bioinformatics, 30, 844–846.
    • (2013) Bioinformatics , vol.30 , pp. 844-846
    • Omasits, U.1    Ahrens, C.H.2    Muller, S.3    Wollscheid, B.4
  • 24
    • 0029177438 scopus 로고
    • Transformation of Lactococcus by electroporation
    • Holo, H., & Nes, I. F. (1995). Transformation of Lactococcus by electroporation. Methods in Molecular Biology, 47, 195–199.
    • (1995) Methods in Molecular Biology , vol.47 , pp. 195-199
    • Holo, H.1    Nes, I.F.2
  • 25
    • 84879578911 scopus 로고    scopus 로고
    • Heterologous expression of Lactobacillus casei RecO improved the multiple-stress tolerance and lactic acid production in Lactococcus lactis NZ9000 during salt stress
    • Wu, C., Zhang, J., Du, G, & Chen, J. (2013). Heterologous expression of Lactobacillus casei RecO improved the multiple-stress tolerance and lactic acid production in Lactococcus lactis NZ9000 during salt stress. Bioresource Technology, 143, 238–241.
    • (2013) Bioresource Technology , vol.143 , pp. 238-241
    • Wu, C.1    Zhang, J.2    Du, G.3    Chen, J.4
  • 26
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227, 680–685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 27
    • 0028345645 scopus 로고
    • Quantitative zymography: detection of picogram quantities of gelatinases
    • Kleiner, D. E., & Stevenson, W. G. S. (1994). Quantitative zymography: detection of picogram quantities of gelatinases. Analytical Chemistry, 218, 325–329.
    • (1994) Analytical Chemistry , vol.218 , pp. 325-329
    • Kleiner, D.E.1    Stevenson, W.G.S.2
  • 28
    • 80055116983 scopus 로고    scopus 로고
    • Sigma's non-specific protease activity assay - casein as a substrate
    • Enyard, C. C. (2009). Sigma's non-specific protease activity assay - casein as a substrate. Journal of Visualized Experiments, 17, 899.
    • (2009) Journal of Visualized Experiments , vol.17 , pp. 899
    • Enyard, C.C.1
  • 29
    • 0029757175 scopus 로고    scopus 로고
    • Controlled gene expression system for Lactococcus lactis with the food-grade inducer nisin
    • de Ruyter, P. G., Kuipers, O. P., & de Vos, W. M. (1996). Controlled gene expression system for Lactococcus lactis with the food-grade inducer nisin. Applied and Environmental Microbiology, 62, 3662–3667.
    • (1996) Applied and Environmental Microbiology , vol.62 , pp. 3662-3667
    • de Ruyter, P.G.1    Kuipers, O.P.2    de Vos, W.M.3
  • 30
    • 27544451339 scopus 로고    scopus 로고
    • M. (2005). 10 years of the nisin-controlled gene expression system (NICE) in Lactococcus lactis
    • Mierau, I., & Kleerebezem, M. (2005). 10 years of the nisin-controlled gene expression system (NICE) in Lactococcus lactis. Applied Microbiology and Biotechnology, 68, 705–717.
    • Applied Microbiology and Biotechnology , vol.68 , pp. 705-717
    • Mierau, I.1
  • 33
    • 79958720098 scopus 로고    scopus 로고
    • Expansion of type II CAAX protease reveals evolutionary origin of γ-secretase subunit APH-1
    • Pei, J., Mitchell, D. A., Dixon, J. E., & Grishin, N. V. (2011). Expansion of type II CAAX protease reveals evolutionary origin of γ-secretase subunit APH-1. Journal of Molecular Biology, 410, 18–26.
    • (2011) Journal of Molecular Biology , vol.410 , pp. 18-26
    • Pei, J.1    Mitchell, D.A.2    Dixon, J.E.3    Grishin, N.V.4
  • 34
    • 84883303937 scopus 로고    scopus 로고
    • Production of the Bacillus licheniformis SubC protease using Lactococcus lactis NICE expression system
    • Mironczuk, A. M., Krasowka, A., Murzyn, A., Plachetka, M., & Lukaszewicz, M. (2012). Production of the Bacillus licheniformis SubC protease using Lactococcus lactis NICE expression system. SpringerPlus., 1, 54.
    • (2012) SpringerPlus. , vol.1 , pp. 54
    • Mironczuk, A.M.1    Krasowka, A.2    Murzyn, A.3    Plachetka, M.4    Lukaszewicz, M.5
  • 35
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of protein
    • Kyte, J., & Doolittle, R. F. (1982). A simple method for displaying the hydropathic character of protein. Journal of Molecular Biology, 157, 105–132.
    • (1982) Journal of Molecular Biology , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 36
    • 84941992384 scopus 로고    scopus 로고
    • Bioinformatics for beginners: genes, genomes, molecular evolution
    • UK: Elsevier
    • Choudhuri, S. (2014). Bioinformatics for beginners: genes, genomes, molecular evolution, database and analytical tools. UK: Elsevier.
    • (2014) database and analytical tools
    • Choudhuri, S.1
  • 37
    • 0032897165 scopus 로고    scopus 로고
    • Effects of gene disruptions in the nisin gene cluster of Lactococcus lactis on nisin production and producer immunity
    • Ra, R., Beerthuyzen, M. M., de Vos, W. M., Saris, P. E., & Kuipers, O. P. (1999). Effects of gene disruptions in the nisin gene cluster of Lactococcus lactis on nisin production and producer immunity. Microbiol., 145, 1227–1233.
    • (1999) Microbiol. , vol.145 , pp. 1227-1233
    • Ra, R.1    Beerthuyzen, M.M.2    de Vos, W.M.3    Saris, P.E.4    Kuipers, O.P.5
  • 38
    • 0037414778 scopus 로고    scopus 로고
    • Function of Lactococcus lactis nisin immunity genes nisI and nis FEG after coordinated expression in the surrogate host Bacillus subtilis
    • Stein, T., Heinzmann, S., Solovieva, I., & Entian, K. D. (2003). Function of Lactococcus lactis nisin immunity genes nisI and nis FEG after coordinated expression in the surrogate host Bacillus subtilis. The Journal of Biological Chemistry, 278, 89–94.
    • (2003) The Journal of Biological Chemistry , vol.278 , pp. 89-94
    • Stein, T.1    Heinzmann, S.2    Solovieva, I.3    Entian, K.D.4
  • 40
    • 65549126460 scopus 로고    scopus 로고
    • Plasmid pAMS1-encoded, bacteriocin-related “Siblicide” in Enterococcus faecalis
    • Sedgley, C. M., Clewell, D. B., & Flannagan, S. E. (2009). Plasmid pAMS1-encoded, bacteriocin-related “Siblicide” in Enterococcus faecalis. Journal of Bacteriology, 191, 3183–3188.
    • (2009) Journal of Bacteriology , vol.191 , pp. 3183-3188
    • Sedgley, C.M.1    Clewell, D.B.2    Flannagan, S.E.3
  • 41
    • 33645803827 scopus 로고    scopus 로고
    • Identification of Bacillus subtilis σW-dependent genes that provide intrinsic resistance to antimicrobial compounds produced by Bacili
    • Butcher, B. G., & Helmann, J. D. (2006). Identification of Bacillus subtilis σW-dependent genes that provide intrinsic resistance to antimicrobial compounds produced by Bacili. Molecular Microbiology, 60, 765–782.
    • (2006) Molecular Microbiology , vol.60 , pp. 765-782
    • Butcher, B.G.1    Helmann, J.D.2
  • 42
    • 33746088411 scopus 로고    scopus 로고
    • Evidence for a novel protease governing regulated intramembrane proteolysis and resistance to antimicrobial peptides in Bacillus subtilis
    • Ellermeier, C. D., & Losick, R. (2006). Evidence for a novel protease governing regulated intramembrane proteolysis and resistance to antimicrobial peptides in Bacillus subtilis. Genes & Development, 20, 1911–1922.
    • (2006) Genes & Development , vol.20 , pp. 1911-1922
    • Ellermeier, C.D.1    Losick, R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.