메뉴 건너뛰기




Volumn 15, Issue 1, 2016, Pages

Subtilisin QK-2: Secretory expression in Lactococcus lactis and surface display onto gram-positive enhancer matrix (GEM) particles

Author keywords

Gram positive enhancer matrix; Lactic acid bacteria; Secretory expression; Subtilisin QK 2; Surface display; Thrombus

Indexed keywords

ALKALINE PROTEINASE; BACTERIAL PROTEIN; GRAM POSITIVE ENHANCER MATRIX; SIGNAL PEPTIDE; SUBTILISIN; SUBTILISIN QK 2; UNCLASSIFIED DRUG; CODON; HYBRID PROTEIN;

EID: 85007420531     PISSN: None     EISSN: 14752859     Source Type: Journal    
DOI: 10.1186/s12934-016-0478-7     Document Type: Article
Times cited : (19)

References (37)
  • 2
    • 32644448656 scopus 로고    scopus 로고
    • Subtilisin QK, a fibrinolytic enzyme, inhibits the exogenous nitrite and hydrogen peroxide induced protein nitration, in vitro and in vivo
    • Ko J, Yan J, Zhu L, Qi Y. Subtilisin QK, a fibrinolytic enzyme, inhibits the exogenous nitrite and hydrogen peroxide induced protein nitration, in vitro and in vivo. J Biochem Mol Biol. 2005;38:577-83.
    • (2005) J Biochem Mol Biol , vol.38 , pp. 577-583
    • Ko, J.1    Yan, J.2    Zhu, L.3    Qi, Y.4
  • 3
    • 70350532503 scopus 로고    scopus 로고
    • Thrombolytic effect of subtilisin QK on carrageenan induced thrombosis model in mice
    • Yan F, Yan J, Sun W, Yao L, Wang J, Qi Y, Xu H. Thrombolytic effect of subtilisin QK on carrageenan induced thrombosis model in mice. J Thromb Thrombolysis. 2009;28:444-8.
    • (2009) J Thromb Thrombolysis , vol.28 , pp. 444-448
    • Yan, F.1    Yan, J.2    Sun, W.3    Yao, L.4    Wang, J.5    Qi, Y.6    Xu, H.7
  • 5
    • 80052633525 scopus 로고    scopus 로고
    • Food-grade gene expression in lactic acid bacteria
    • Peterbauer C, Maischberger T, Haltrich D. Food-grade gene expression in lactic acid bacteria. Biotechnol J. 2011;6:1147-61.
    • (2011) Biotechnol J , vol.6 , pp. 1147-1161
    • Peterbauer, C.1    Maischberger, T.2    Haltrich, D.3
  • 7
    • 0030956641 scopus 로고    scopus 로고
    • Cell wall anchoring of the Streptococcus pyogenes M6 protein in various lactic acid bacteria
    • Piard JC, Hautefort I, Fischetti VA, Ehrlich SD, Fons M, Gruss A. Cell wall anchoring of the Streptococcus pyogenes M6 protein in various lactic acid bacteria. J Bacteriol. 1997;179:3068-72.
    • (1997) J Bacteriol , vol.179 , pp. 3068-3072
    • Piard, J.C.1    Hautefort, I.2    Fischetti, V.A.3    Ehrlich, S.D.4    Fons, M.5    Gruss, A.6
  • 9
    • 33646153514 scopus 로고    scopus 로고
    • Immunogenicity of a malaria parasite antigen displayed by Lactococcus lactis in oral immunisations
    • Ramasamy R, Yasawardena S, Zomer A, Venema G, Kok J, Leenhouts K. Immunogenicity of a malaria parasite antigen displayed by Lactococcus lactis in oral immunisations. Vaccine. 2006;24:3900-8.
    • (2006) Vaccine , vol.24 , pp. 3900-3908
    • Ramasamy, R.1    Yasawardena, S.2    Zomer, A.3    Venema, G.4    Kok, J.5    Leenhouts, K.6
  • 11
    • 23944501101 scopus 로고    scopus 로고
    • Cell surface display system for Lactococcus lactis: a novel development for oral vaccine
    • Raha AR, Varma NR, Yusoff K, Ross E, Foo HL. Cell surface display system for Lactococcus lactis: a novel development for oral vaccine. Appl Microbiol Biotechnol. 2005;68:75-81.
    • (2005) Appl Microbiol Biotechnol , vol.68 , pp. 75-81
    • Raha, A.R.1    Varma, N.R.2    Yusoff, K.3    Ross, E.4    Foo, H.L.5
  • 13
    • 61349192174 scopus 로고    scopus 로고
    • Purification and characterization of a novel fibrinolytic protease from Fusarium s. CPCC 480097
    • Wu B, Wu L, Chen D, Yang Z, Luo M. Purification and characterization of a novel fibrinolytic protease from Fusarium sp. CPCC 480097. J Ind Microbiol Biotechnol. 2009;36:451-9.
    • (2009) J Ind Microbiol Biotechnol , vol.36 , pp. 451-459
    • Wu, B.1    Wu, L.2    Chen, D.3    Yang, Z.4    Luo, M.5
  • 14
    • 84925501860 scopus 로고    scopus 로고
    • Efficient expression of nattokinase in Bacillus licheniformis: host strain construction and signal peptide optimization
    • Wei X, Zhou Y, Chen J, Cai D, Wang D, Qi G, Chen S. Efficient expression of nattokinase in Bacillus licheniformis: host strain construction and signal peptide optimization. J Ind Microbiol Biotechnol. 2015;42:287-95.
    • (2015) J Ind Microbiol Biotechnol , vol.42 , pp. 287-295
    • Wei, X.1    Zhou, Y.2    Chen, J.3    Cai, D.4    Wang, D.5    Qi, G.6    Chen, S.7
  • 15
    • 36949027895 scopus 로고    scopus 로고
    • Secretory expression of nattokinase from Bacillus subtilis YF38 in Escherichia coli
    • Liang X, Jia S, Sun Y, Chen M, Chen X, Zhong J, Huan L. Secretory expression of nattokinase from Bacillus subtilis YF38 in Escherichia coli. Mol Biotechnol. 2007;37:187-94.
    • (2007) Mol Biotechnol , vol.37 , pp. 187-194
    • Liang, X.1    Jia, S.2    Sun, Y.3    Chen, M.4    Chen, X.5    Zhong, J.6    Huan, L.7
  • 16
    • 21644451024 scopus 로고    scopus 로고
    • Efficient system of artificial oil bodies for functional expression and purification of recombinant nattokinase in Escherichia coli
    • Chiang CJ, Chen HC, Chao YP, Tzen JT. Efficient system of artificial oil bodies for functional expression and purification of recombinant nattokinase in Escherichia coli. J Agric Food Chem. 2005;53:4799-804.
    • (2005) J Agric Food Chem , vol.53 , pp. 4799-4804
    • Chiang, C.J.1    Chen, H.C.2    Chao, Y.P.3    Tzen, J.T.4
  • 17
    • 79954987555 scopus 로고    scopus 로고
    • Use of murine models to detect the allergenicity of genetically modified Lactococcus lactis NZ9000/pNZPNK
    • Chiang SS, Liu CF, Ku TW, Mau JL, Lin HT, Pan TM. Use of murine models to detect the allergenicity of genetically modified Lactococcus lactis NZ9000/pNZPNK. J Agric Food Chem. 2011;59:3876-83.
    • (2011) J Agric Food Chem , vol.59 , pp. 3876-3883
    • Chiang, S.S.1    Liu, C.F.2    Ku, T.W.3    Mau, J.L.4    Lin, H.T.5    Pan, T.M.6
  • 18
    • 34247630201 scopus 로고    scopus 로고
    • Secretory expression of a heterologous nattokinase in Lactococcus lactis
    • Liang X, Zhang L, Zhong J, Huan L. Secretory expression of a heterologous nattokinase in Lactococcus lactis. Appl Microbiol Biotechnol. 2007;75:95-101.
    • (2007) Appl Microbiol Biotechnol , vol.75 , pp. 95-101
    • Liang, X.1    Zhang, L.2    Zhong, J.3    Huan, L.4
  • 19
    • 29144455402 scopus 로고    scopus 로고
    • Heterologous leaky production of transglutaminase in Lactococcus lactis significantly enhances the growth performance of the host
    • Fu RY, Chen J, Li Y. Heterologous leaky production of transglutaminase in Lactococcus lactis significantly enhances the growth performance of the host. Appl Environ Microbiol. 2005;71:8911-9.
    • (2005) Appl Environ Microbiol , vol.71 , pp. 8911-8919
    • Fu, R.Y.1    Chen, J.2    Li, Y.3
  • 20
    • 77249111221 scopus 로고    scopus 로고
    • Highlevel expression of Lactobacillus beta-galactosidases in Lactococcus lactis using the food-grade, nisin-controlled expression system NICE
    • Maischberger T, Mierau I, Peterbauer CK, Hugenholtz J, Haltrich D. Highlevel expression of Lactobacillus beta-galactosidases in Lactococcus lactis using the food-grade, nisin-controlled expression system NICE. J Agric Food Chem. 2010;58:2279-87.
    • (2010) J Agric Food Chem , vol.58 , pp. 2279-2287
    • Maischberger, T.1    Mierau, I.2    Peterbauer, C.K.3    Hugenholtz, J.4    Haltrich, D.5
  • 21
    • 79959257699 scopus 로고    scopus 로고
    • Nisin-inducible secretion of a biologically active singlechain insulin analog by Lactococcus lactis NZ9000
    • Ng DT, Sarkar CA. Nisin-inducible secretion of a biologically active singlechain insulin analog by Lactococcus lactis NZ9000. Biotechnol Bioeng. 2011;108:1987-96.
    • (2011) Biotechnol Bioeng , vol.108 , pp. 1987-1996
    • Ng, D.T.1    Sarkar, C.A.2
  • 22
    • 0345276496 scopus 로고    scopus 로고
    • Lactic acid bacteria as prime candidates for codon optimization
    • Fuglsang A. Lactic acid bacteria as prime candidates for codon optimization. Biochem Biophys Res Commun. 2003;312:285-91.
    • (2003) Biochem Biophys Res Commun , vol.312 , pp. 285-291
    • Fuglsang, A.1
  • 23
    • 0037459069 scopus 로고    scopus 로고
    • General function of N-terminal propeptide on assisting protein folding and inhibiting catalytic activity based on observations with a chimeric thermolysin-like protease
    • Tang B, Nirasawa S, Kitaoka M, Marie-Claire C, Hayashi K. General function of N-terminal propeptide on assisting protein folding and inhibiting catalytic activity based on observations with a chimeric thermolysin-like protease. Biochem Biophys Res Commun. 2003;301:1093-8.
    • (2003) Biochem Biophys Res Commun , vol.301 , pp. 1093-1098
    • Tang, B.1    Nirasawa, S.2    Kitaoka, M.3    Marie-Claire, C.4    Hayashi, K.5
  • 25
    • 0034108191 scopus 로고    scopus 로고
    • HtrA is the unique surface housekeeping protease in Lactococcus lactis and is required for natural protein processing
    • Poquet I, Saint V, Seznec E, Simoes N, Bolotin A, Gruss A. HtrA is the unique surface housekeeping protease in Lactococcus lactis and is required for natural protein processing. Mol Microbiol. 2000;35:1042-51.
    • (2000) Mol Microbiol , vol.35 , pp. 1042-1051
    • Poquet, I.1    Saint, V.2    Seznec, E.3    Simoes, N.4    Bolotin, A.5    Gruss, A.6
  • 26
    • 0031854230 scopus 로고    scopus 로고
    • Formulation-related problems associated with intravenous drug delivery
    • Yalkowsky SH, Krzyzaniak JF, Ward GH. Formulation-related problems associated with intravenous drug delivery. J Pharm Sci. 1998;87:787-96.
    • (1998) J Pharm Sci , vol.87 , pp. 787-796
    • Yalkowsky, S.H.1    Krzyzaniak, J.F.2    Ward, G.H.3
  • 29
    • 50849091252 scopus 로고    scopus 로고
    • Lactococcus lactisexpressing listeriolysin O (LLO) provides protection and specific CD8(+) T cells against Listeria monocytogenes in the murine infection model
    • Bahey-El-Din M, Casey PG, Griffin BT, Gahan CG. Lactococcus lactisexpressing listeriolysin O (LLO) provides protection and specific CD8(+) T cells against Listeria monocytogenes in the murine infection model. Vaccine. 2008;26:5304-14.
    • (2008) Vaccine , vol.26 , pp. 5304-5314
    • Bahey-El-Din, M.1    Casey, P.G.2    Griffin, B.T.3    Gahan, C.G.4
  • 30
    • 0029757175 scopus 로고    scopus 로고
    • Controlled gene expression systems for Lactococcus lactis with the food-grade inducer nisin
    • De Ruyter P, Kuipers OP, De Vos WM. Controlled gene expression systems for Lactococcus lactis with the food-grade inducer nisin. Appl Environ Microbiol. 1996;62:3662-7.
    • (1996) Appl Environ Microbiol , vol.62 , pp. 3662-3667
    • De Ruyter, P.1    Kuipers, O.P.2    De Vos, W.M.3
  • 31
    • 84952053948 scopus 로고    scopus 로고
    • Novel method based on chromogenic media for discrimination and selective enumeration of lactic acid bacteria in fermented milk products
    • Galat A, Dufresne J, Combrisson J, Thépaut J, Boumghar-Bourtchai L, Boyer M, Fourmestraux C. Novel method based on chromogenic media for discrimination and selective enumeration of lactic acid bacteria in fermented milk products. Food Microbiol. 2015;55:86-94.
    • (2015) Food Microbiol , vol.55 , pp. 86-94
    • Galat, A.1    Dufresne, J.2    Combrisson, J.3    Thépaut, J.4    Boumghar-Bourtchai, L.5    Boyer, M.6    Fourmestraux, C.7
  • 32
    • 84925486339 scopus 로고    scopus 로고
    • Constructing a recombinant hyaluronic acid biosynthesis operon and producing food-grade hyaluronic acid in Lactococcus lactis
    • Sheng J, Ling P, Wang F. Constructing a recombinant hyaluronic acid biosynthesis operon and producing food-grade hyaluronic acid in Lactococcus lactis. J Ind Microbiol Biotechnol. 2015;42:197-206.
    • (2015) J Ind Microbiol Biotechnol , vol.42 , pp. 197-206
    • Sheng, J.1    Ling, P.2    Wang, F.3
  • 35
    • 50449151040 scopus 로고
    • The fibrin plate method for estimating fibrinolytic activity
    • Astrup T, Mullertz S. The fibrin plate method for estimating fibrinolytic activity. Arch Biochem Biophys. 1952;40:346-51.
    • (1952) Arch Biochem Biophys , vol.40 , pp. 346-351
    • Astrup, T.1    Mullertz, S.2
  • 36
    • 0031800841 scopus 로고    scopus 로고
    • Development and application of an in vitro methodology to determine the transit tolerance of potentially probiotic Lactobacillus and Bifidobacterium species in the upper human gastrointestinal tract
    • Charteris WP, Kelly PM, Morelli L, Collins JK. Development and application of an in vitro methodology to determine the transit tolerance of potentially probiotic Lactobacillus and Bifidobacterium species in the upper human gastrointestinal tract. J Appl Microbiol. 1998;84:759-68.
    • (1998) J Appl Microbiol , vol.84 , pp. 759-768
    • Charteris, W.P.1    Kelly, P.M.2    Morelli, L.3    Collins, J.K.4
  • 37
    • 14644445240 scopus 로고    scopus 로고
    • Monitoring dynamic expression of nuclear genes in Chlamydomonas reinhardtii by using a synthetic luciferase reporter gene
    • Fuhrmann M, Hausherr A, Ferbitz L, Schodl T, Heitzer M, Hegemann P. Monitoring dynamic expression of nuclear genes in Chlamydomonas reinhardtii by using a synthetic luciferase reporter gene. Plant Mol Biol. 2004;55:869-81.
    • (2004) Plant Mol Biol , vol.55 , pp. 869-881
    • Fuhrmann, M.1    Hausherr, A.2    Ferbitz, L.3    Schodl, T.4    Heitzer, M.5    Hegemann, P.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.