메뉴 건너뛰기




Volumn 24, Issue 10, 2014, Pages 1405-1412

Cloning, Characterization, And production of a novel lysozyme by different expression hosts

Author keywords

Antimicrobial; Bacillus licheniformis; Bacillus subtilis; Lysozyme; Protein expression system

Indexed keywords

LYSOZYME; PEPSIN A; TRYPSIN; ANTIINFECTIVE AGENT; RECOMBINANT PROTEIN;

EID: 84923462537     PISSN: 10177825     EISSN: 17388872     Source Type: Journal    
DOI: 10.4014/jmb.1404.04039     Document Type: Article
Times cited : (24)

References (36)
  • 2
    • 77951759131 scopus 로고    scopus 로고
    • Lysozymes in the animal kingdom
    • Callewaert L, Michiels CW. 2010. Lysozymes in the animal kingdom. J. Biosci. 35: 127-160.
    • (2010) J. Biosci , vol.35 , pp. 127-160
    • Callewaert, L.1    Michiels, C.W.2
  • 4
    • 77949486278 scopus 로고    scopus 로고
    • Secreted production of Renilla luciferase in Bacillus subtilis
    • Chiang CJ, Chen PT, Chao YP. 2010. Secreted production of Renilla luciferase in Bacillus subtilis. Biotechnol. Prog. 26: 58 9-594.
    • (2010) Biotechnol. Prog , vol.26 , Issue.58 , pp. 9-594
    • Chiang, C.J.1    Chen, P.T.2    Chao, Y.P.3
  • 5
    • 84901459476 scopus 로고    scopus 로고
    • Current development in genetic engineering strategies of Bacillus species
    • Dong H, Zhang D. 2014. Current development in genetic engineering strategies of Bacillus species. Microb. Cell Fact. 13: 63.
    • (2014) Microb. Cell Fact , vol.13 , pp. 63
    • Dong, H.1    Zhang, D.2
  • 6
    • 0027671929 scopus 로고
    • A tightly regulated system for overproduction of bacteriophage T4 lysozyme in Escherichia coli
    • During K. 1993. A tightly regulated system for overproduction of bacteriophage T4 lysozyme in Escherichia coli. Protein Expr. Purif. 4: 412-416.
    • (1993) Protein Expr. Purif , vol.4 , pp. 412-416
    • During, K.1
  • 7
    • 0026095436 scopus 로고
    • Killing of gram-negative bacteria by lactoferrin and lysozyme
    • Ellison RT III, Giehl TJ. 1991. Killing of gram-negative bacteria by lactoferrin and lysozyme. J. Clin. Invest. 88: 1080-1091.
    • (1991) J. Clin. Invest , vol.88 , pp. 1080-1091
    • Ellison, R.T.1    Giehl, T.J.2
  • 8
    • 84879841797 scopus 로고    scopus 로고
    • Production of human lysozyme in biofilm reactor and optimization of growth parameters of Kluyveromyces lactis K7
    • Ercan D, Demirci A. 2013. Production of human lysozyme in biofilm reactor and optimization of growth parameters of Kluyveromyces lactis K7. Appl. Microbiol. Biotechnol. 97: 6211-6221.
    • (2013) Appl. Microbiol. Biotechnol , vol.97 , pp. 6211-6221
    • Ercan, D.1    Demirci, A.2
  • 9
    • 0027259010 scopus 로고
    • Physiological consequence of expression of soluble and active hen egg white lysozyme in Escherichia coli
    • Fischer B, Perry B, Phillips G, Sumner I, Goodenough P. 1993. Physiological consequence of expression of soluble and active hen egg white lysozyme in Escherichia coli. Appl. Microbiol. Biotechnol. 39: 537-540.
    • (1993) Appl. Microbiol. Biotechnol , vol.39 , pp. 537-540
    • Fischer, B.1    Perry, B.2    Phillips, G.3    Sumner, I.4    Goodenough, P.5
  • 10
    • 0026658365 scopus 로고
    • A novel sequential procedure to enhance the renaturation of recombinant protein from Escherichia coli inclusion bodies
    • Fischer B, Perry B, Sumner I, Goodenough P. 1992. A novel sequential procedure to enhance the renaturation of recombinant protein from Escherichia coli inclusion bodies. Protein Eng. 5: 593-596.
    • (1992) Protein Eng , vol.5 , pp. 593-596
    • Fischer, B.1    Perry, B.2    Sumner, I.3    Goodenough, P.4
  • 11
    • 34848901438 scopus 로고    scopus 로고
    • Crystal structure of Tapes japonica lysozyme with substrate analogue: Structural basis of the catalytic mechanism and manifestation of its chitinase activity accompanied by quaternary structural change
    • Goto T, Abe Y, Kakuta Y, Takeshita K, Imoto T, Ueda T. 2007. Crystal structure of Tapes japonica lysozyme with substrate analogue: structural basis of the catalytic mechanism and manifestation of its chitinase activity accompanied by quaternary structural change. J. Biol. Chem. 282: 27459-27467.
    • (2007) J. Biol. Chem , vol.282 , pp. 27459-27467
    • Goto, T.1    Abe, Y.2    Kakuta, Y.3    Takeshita, K.4    Imoto, T.5    Ueda, T.6
  • 12
    • 0029620311 scopus 로고
    • Protein disulfide isomerase mutant lacking its isomerase activity accelerates protein folding in the cell
    • Hayano T, Hirose M, Kikuchi M. 1995. Protein disulfide isomerase mutant lacking its isomerase activity accelerates protein folding in the cell. FEBS Lett. 377: 505-511.
    • (1995) FEBS Lett , vol.377 , pp. 505-511
    • Hayano, T.1    Hirose, M.2    Kikuchi, M.3
  • 13
    • 0018820115 scopus 로고
    • Insect immunity. Purification and properties of three inducible bactericidal proteins from hemolymph of immunized pupae of Hyalophora cecropia
    • Hultmark D, Steiner H, Rasmuson T, Boman HG. 1980. Insect immunity. Purification and properties of three inducible bactericidal proteins from hemolymph of immunized pupae of Hyalophora cecropia. Eur. J. Biochem. 106: 7-16.
    • (1980) Eur. J. Biochem , vol.106 , pp. 7-16
    • Hultmark, D.1    Steiner, H.2    Rasmuson, T.3    Boman, H.G.4
  • 14
    • 0021490172 scopus 로고
    • What’s new in lysozyme research? Always a model system, today as yesterday
    • Jolles P, Jolles J. 1984. What’s new in lysozyme research? Always a model system, today as yesterday. Mol. Cell. Biochem. 63: 165-189.
    • (1984) Mol. Cell. Biochem , vol.63 , pp. 165-189
    • Jolles, P.1    Jolles, J.2
  • 15
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK. 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
  • 16
    • 84875088103 scopus 로고    scopus 로고
    • Engineering Escherichia coli for soluble expression and single step purification of active human lysozyme
    • Lamppa JW, Tanyos SA, Griswold KE. 2013. Engineering Escherichia coli for soluble expression and single step purification of active human lysozyme. J. Biotechnol. 164: 1-8.
    • (2013) J. Biotechnol , vol.164 , pp. 1-8
    • Lamppa, J.W.1    Tanyos, S.A.2    Griswold, K.E.3
  • 17
    • 15944375504 scopus 로고    scopus 로고
    • Antibacterial properties of aged dental cements evaluated by direct-contact and agar diffusion tests
    • Lewinstein I, Matalon S, Slutzkey S, Weiss EI. 2005. Antibacterial properties of aged dental cements evaluated by direct-contact and agar diffusion tests. J. Prosthet. Dent. 93: 364-371.
    • (2005) J. Prosthet. Dent , vol.93 , pp. 364-371
    • Lewinstein, I.1    Matalon, S.2    Slutzkey, S.3    Weiss, E.I.4
  • 19
    • 0035947615 scopus 로고    scopus 로고
    • Escherichia coli ykfE ORFan gene encodes a potent inhibitor of C-type lysozyme
    • Monchois V, Abergel C, Sturgis J, Jeudy S, Claverie JM. 2001. Escherichia coli ykfE ORFan gene encodes a potent inhibitor of C-type lysozyme. J. Biol. Chem. 276: 18437-18441.
    • (2001) J. Biol. Chem , vol.276 , pp. 18437-18441
    • Monchois, V.1    Abergel, C.2    Sturgis, J.3    Jeudy, S.4    Claverie, J.M.5
  • 20
    • 0033991321 scopus 로고    scopus 로고
    • Endotoxin removal from protein solutions
    • Petsch D, Anspach FB. 2000. Endotoxin removal from protein solutions. J. Biotechnol. 76: 97-119.
    • (2000) J. Biotechnol , vol.76 , pp. 97-119
    • Petsch, D.1    Anspach, F.B.2
  • 21
    • 0030800608 scopus 로고    scopus 로고
    • Molecular divergence of lysozymes and alpha-lactalbumin
    • Qasba PK, Kumar S. 1997. Molecular divergence of lysozymes and alpha-lactalbumin. Crit. Rev. Biochem. Mol. Biol. 32: 255-306.
    • (1997) Crit. Rev. Biochem. Mol. Biol , vol.32 , pp. 255-306
    • Qasba, P.K.1    Kumar, S.2
  • 22
    • 0026534357 scopus 로고
    • Efficient in vitro folding of the three-disulfide derivatives of hen lysozyme in the presence of glycerol
    • Sawano H, Koumoto Y, Ohta K, Sasaki Y, Segawa S, Tachibana H. 1992. Efficient in vitro folding of the three-disulfide derivatives of hen lysozyme in the presence of glycerol. FEBS Lett. 303: 11-14.
    • (1992) FEBS Lett , vol.303 , pp. 11-14
    • Sawano, H.1    Koumoto, Y.2    Ohta, K.3    Sasaki, Y.4    Segawa, S.5    Tachibana, H.6
  • 23
    • 27944471040 scopus 로고    scopus 로고
    • Heterologous expression of hen egg white lysozyme and resonance assignment of tryptophan side chains in its non-native states
    • Schlorb C, Ackermann K, Richter C, Wirmer J, Schwalbe H. 2005. Heterologous expression of hen egg white lysozyme and resonance assignment of tryptophan side chains in its non-native states. J. Biomol. NMR 33: 95-104.
    • (2005) J. Biomol. NMR , vol.33 , pp. 95-104
    • Schlorb, C.1    Ackermann, K.2    Richter, C.3    Wirmer, J.4    Schwalbe, H.5
  • 25
    • 0027401020 scopus 로고
    • Protein secretion in Bacillus species
    • Simonen M, Palva I. 1993. Protein secretion in Bacillus species. Microbiol. Rev. 57: 109-137.
    • (1993) Microbiol. Rev , vol.57 , pp. 109-137
    • Simonen, M.1    Palva, I.2
  • 26
    • 84872143710 scopus 로고    scopus 로고
    • Bacillus subtilis: From soil bacterium to super-secreting cell factory
    • van Dijl JM, Hecker M. 2013. Bacillus subtilis: from soil bacterium to super-secreting cell factory. Microb. Cell Fact. 12: 3.
    • (2013) Microb. Cell Fact , vol.12 , pp. 3
    • Van Dijl, J.M.1    Hecker, M.2
  • 27
    • 36249005511 scopus 로고    scopus 로고
    • Production of 1,3-propanediol from glycerol by recombinant E. coli using incompatible plasmids system
    • Wang F, Qu H, Zhang D, Tian P, Tan T. 2007. Production of 1,3-propanediol from glycerol by recombinant E. coli using incompatible plasmids system. Mol. Biotechnol. 37: 112-119.
    • (2007) Mol. Biotechnol , vol.37 , pp. 112-119
    • Wang, F.1    Qu, H.2    Zhang, D.3    Tian, P.4    Tan, T.5
  • 28
    • 84861588029 scopus 로고    scopus 로고
    • Cloning and functional expression of a human lysozyme gene (hly) from human leukocytes in Pichia pastoris
    • Wei JT, Tang CD, Wu MC, Liu GL, Shi HL, Li JF. 2012. Cloning and functional expression of a human lysozyme gene (hly) from human leukocytes in Pichia pastoris. Mol. Med. Rep. 6: 173-178.
    • (2012) Mol. Med. Rep , vol.6 , pp. 173-178
    • Wei, J.T.1    Tang, C.D.2    Wu, M.C.3    Liu, G.L.4    Shi, H.L.5    Li, J.F.6
  • 29
    • 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 WJ. 2004. Bacillus subtilis as cell factory for pharmaceutical proteins: a biotechnological approach to optimize the host organism. Biochim. Biophys. Acta 1694: 299-310.
    • (2004) Biochim. Biophys. Acta , vol.1694 , pp. 299-310
    • Westers, L.1    Westers, H.2    Quax, W.J.3
  • 31
    • 79958280761 scopus 로고    scopus 로고
    • Process evaluations and economic analyses of recombinant human lysozyme and hen egg-white lysozyme purifications
    • Wilken LR, Nikolov ZL. 2011. Process evaluations and economic analyses of recombinant human lysozyme and hen egg-white lysozyme purifications. Biotechnol. Prog. 27: 733-743.
    • (2011) Biotechnol. Prog , vol.27 , pp. 733-743
    • Wilken, L.R.1    Nikolov, Z.L.2
  • 32
    • 39649125420 scopus 로고    scopus 로고
    • Extracellular expression of a functional recombinant Ganoderma lucidium immunomodulatory protein by Bacillus subtilis and Lactococcus lactis
    • Yeh CM, Yeh CK, Hsu XY, Luo QM, Lin MY. 2008. Extracellular expression of a functional recombinant Ganoderma lucidium immunomodulatory protein by Bacillus subtilis and Lactococcus lactis. Appl. Environ. Microbiol. 74: 1039-1049.
    • (2008) Appl. Environ. Microbiol , vol.74 , pp. 1039-1049
    • Yeh, C.M.1    Yeh, C.K.2    Hsu, X.Y.3    Luo, Q.M.4    Lin, M.Y.5
  • 33
    • 84863288448 scopus 로고    scopus 로고
    • Translation elongation regulates substrate selection by the signal recognition particle
    • Zhang D, Shan SO. 2012. Translation elongation regulates substrate selection by the signal recognition particle. J. Biol. Chem. 287: 7652-7660.
    • (2012) J. Biol. Chem , vol.287 , pp. 7652-7660
    • Zhang, D.1    Shan, S.O.2
  • 34
    • 34147157290 scopus 로고    scopus 로고
    • Ubiquinone-10 production using Agrobacterium tumefaciens dps gene in Escherichia coli by coexpression system
    • Zhang D, Shrestha B, Li Z, Tan T. 2007. Ubiquinone-10 production using Agrobacterium tumefaciens dps gene in Escherichia coli by coexpression system. Mol. Biotechnol. 35: 1-14.
    • (2007) Mol. Biotechnol , vol.35 , pp. 1-14
    • Zhang, D.1    Shrestha, B.2    Li, Z.3    Tan, T.4
  • 35
    • 84863039852 scopus 로고    scopus 로고
    • Novel proteomic tools reveal essential roles of SRP and importance of proper membrane protein biogenesis
    • M111011585
    • Zhang D, Sweredoski MJ, Graham RL, Hess S, Shan SO. 2012. Novel proteomic tools reveal essential roles of SRP and importance of proper membrane protein biogenesis. Mol. Cell. Proteomics 11: M111011585.
    • (2012) Mol. Cell. Proteomics , vol.11
    • Zhang, D.1    Sweredoski, M.J.2    Graham, R.L.3    Hess, S.4    Shan, S.O.5
  • 36
    • 0021256398 scopus 로고
    • Glucosamine substitution and muramidase susceptibility in Bacillus anthracis
    • Zipperle GF Jr, Ezzell JW Jr, Doyle RJ. 1984. Glucosamine substitution and muramidase susceptibility in Bacillus anthracis. Can. J. Microbiol. 30: 553-559.
    • (1984) Can. J. Microbiol , vol.30 , pp. 553-559
    • Zipperle, G.F.1    Ezzell, J.W.2    Doyle, R.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.