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Volumn 3, Issue 1, 2005, Pages 103-114

Expression of the sweet protein brazzein in maize for production of a new commercial sweetener

Author keywords

Brazzein; Natural sweetener; Sweet protein; Zea mays

Indexed keywords

ZEA MAYS;

EID: 27644494245     PISSN: 14677644     EISSN: 14677652     Source Type: Journal    
DOI: 10.1111/j.1467-7652.2004.00105.x     Document Type: Article
Times cited : (70)

References (35)
  • 1
    • 0034656406 scopus 로고    scopus 로고
    • Efficient production of recombinant brazzein, a small, heat-stable, sweet-tasting protein of plant origin
    • Assadi-Porter, F.M., Aceti, D.J., Cheng, H. and Markley, J.L. (2000a) Efficient production of recombinant brazzein, a small, heat-stable, sweet-tasting protein of plant origin. Arch. Biochem. Biophys. 376, 252-258.
    • (2000) Arch. Biochem. Biophys. , vol.376 , pp. 252-258
    • Assadi-Porter, F.M.1    Aceti, D.J.2    Cheng, H.3    Markley, J.L.4
  • 2
    • 0034656399 scopus 로고    scopus 로고
    • Sweetness determinant sites of brazzein, a small, heat-stable, sweet-tasting protein
    • Assadi-Porter, F.M., Aceti, D.J. and Markley, J.L. (2000b) Sweetness determinant sites of brazzein, a small, heat-stable, sweet-tasting protein. Arch. Biochem. Biophys. 376, 259-265.
    • (2000) Arch. Biochem. Biophys. , vol.376 , pp. 259-265
    • Assadi-Porter, F.M.1    Aceti, D.J.2    Markley, J.L.3
  • 3
    • 0026043040 scopus 로고
    • Molecular basis for allelic polymorphism of the maize Globulin-1 gene
    • Belanger, F.C. and Kriz, A.L. (1991) Molecular basis for allelic polymorphism of the maize Globulin-1 gene. Genetics, 129, 863-872.
    • (1991) Genetics , vol.129 , pp. 863-872
    • Belanger, F.C.1    Kriz, A.L.2
  • 4
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M.M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 5
    • 0042128615 scopus 로고    scopus 로고
    • Long-term stability of transgene expression driven by barley endosperm-specific hordein promoters in transgenic barley
    • Choi, H.W., Lemaux, P.G. and Cho, M.J. (2003) Long-term stability of transgene expression driven by barley endosperm-specific hordein promoters in transgenic barley. Plant Cell Report, 21, 1108-1120.
    • (2003) Plant Cell Report , vol.21 , pp. 1108-1120
    • Choi, H.W.1    Lemaux, P.G.2    Cho, M.J.3
  • 6
    • 0019906163 scopus 로고
    • Cloning of cDNA encoding the sweet tasting plant protein thaumatin and its expression in Escherichia coli
    • Edens, L., Heslinga, L., Klok, R., Ledeboer, A.M., Maat, J., Toonen, M.Y., Visser, C.T. and Varrips, T. (1982) Cloning of cDNA encoding the sweet tasting plant protein thaumatin and its expression in Escherichia coli. Gene, 18, 1-12.
    • (1982) Gene , vol.18 , pp. 1-12
    • Edens, L.1    Heslinga, L.2    Klok, R.3    Ledeboer, A.M.4    Maat, J.5    Toonen, M.Y.6    Visser, C.T.7    Varrips, T.8
  • 7
    • 0021941768 scopus 로고
    • Microbial synthesis of the sweet-tasting protein thaumatin
    • Edens, L. and van der Wel, H. (1985) Microbial synthesis of the sweet-tasting protein thaumatin. Trends Biotechnol. 3, 61-64.
    • (1985) Trends Biotechnol. , vol.3 , pp. 61-64
    • Edens, L.1    Van Der Wel, H.2
  • 8
    • 0034002755 scopus 로고    scopus 로고
    • Recent developments in the characterization and biotechnological production of sweet-tasting proteins
    • Faus, I. (2000) Recent developments in the characterization and biotechnological production of sweet-tasting proteins. Appl. Microbiol. Biotechnol. 53, 145-151.
    • (2000) Appl. Microbiol. Biotechnol. , vol.53 , pp. 145-151
    • Faus, I.1
  • 9
    • 0035078455 scopus 로고    scopus 로고
    • Efficiency and stability of high molecular weight DNA transformation: An analysis in tomato
    • Frary, A. and Hamilton, C.M. (2001) Efficiency and stability of high molecular weight DNA transformation: an analysis in tomato. Transgenic Res. 10, 121-132.
    • (2001) Transgenic Res. , vol.10 , pp. 121-132
    • Frary, A.1    Hamilton, C.M.2
  • 10
    • 0002643896 scopus 로고
    • Fruits of the rainforest and taste perception as a result of evolutionary interactions
    • (Hladik, C.M., Hladik, A., Linares, O.P., Pagezy, H., Semple, A. and Hadley, M., eds), Paris and Carnforth, Lancashire: UNESCO and The Parthenon Publishing Group
    • Hladick, C.M. (1993) Fruits of the rainforest and taste perception as a result of evolutionary interactions. In Tropical Forests, People and Food: Biocultural Interactions and Applications to Development. (Hladik, C.M., Hladik, A., Linares, O.P., Pagezy, H., Semple, A. and Hadley, M., eds), pp. 73-82. Paris and Carnforth, Lancashire: UNESCO and The Parthenon Publishing Group.
    • (1993) Tropical Forests, People and Food: Biocultural Interactions and Applications to Development , pp. 73-82
    • Hladick, C.M.1
  • 11
    • 0036864268 scopus 로고    scopus 로고
    • Pathogenisis-related (PR)-proteins identified as allergens
    • Hoffman-Sommerguber, K. (2002) Pathogenisis-related (PR)-proteins identified as allergens. Biochem. Soc. Trans. 30, 930-935.
    • (2002) Biochem. Soc. Trans. , vol.30 , pp. 930-935
    • Hoffman-Sommerguber, K.1
  • 13
    • 0033179650 scopus 로고    scopus 로고
    • Plant-based production of xenogenic proteins
    • Hood, E.E. and Jilka, J.M. (1999) Plant-based production of xenogenic proteins. Curr. Opin. Biotechnol. 4, 382-386.
    • (1999) Curr. Opin. Biotechnol. , vol.4 , pp. 382-386
    • Hood, E.E.1    Jilka, J.M.2
  • 14
    • 0033280755 scopus 로고    scopus 로고
    • Molecular farming of industrial proteins from transgenic maize
    • Hood, E.E., Kusnadi, A., Nikolov, Z. and Howard, J.A. (1999) Molecular farming of industrial proteins from transgenic maize. Adv. Exp. Med. Biol. 464, 127-147.
    • (1999) Adv. Exp. Med. Biol. , vol.464 , pp. 127-147
    • Hood, E.E.1    Kusnadi, A.2    Nikolov, Z.3    Howard, J.A.4
  • 16
    • 2442590941 scopus 로고    scopus 로고
    • Plant molecular farming: Systems and products
    • Horn, M.E., Woodard, S.L and Howard, J.A. (2004) Plant molecular farming: systems and products. Plant Cell Rep. 22, 711-720.
    • (2004) Plant Cell Rep. , vol.22 , pp. 711-720
    • Horn, M.E.1    Woodard, S.L.2    Howard, J.A.3
  • 17
    • 0030199663 scopus 로고    scopus 로고
    • Synthesis and characterization of the sweet protein brazzein
    • Izawa, H., Ota, M., Kohmura, M. and Ariyoshi, Y. (1996) Synthesis and characterization of the sweet protein brazzein. Biopolymers, 39, 95-101.
    • (1996) Biopolymers , vol.39 , pp. 95-101
    • Izawa, H.1    Ota, M.2    Kohmura, M.3    Ariyoshi, Y.4
  • 18
  • 20
    • 0025387556 scopus 로고
    • Synthesis and accumulation of pea plastocyanin in transgenic tobacco plants
    • Last, D.I. and Gray, J.C. (1990) Synthesis and accumulation of pea plastocyanin in transgenic tobacco plants. Plant Mol. Biol. 14, 229-238.
    • (1990) Plant Mol. Biol. , vol.14 , pp. 229-238
    • Last, D.I.1    Gray, J.C.2
  • 22
    • 0023664635 scopus 로고
    • Sequence from picomole quantities of proteins electroblotted onto polyvinylidene difluoride membranes
    • Matsudaira, P. (1987) Sequence from picomole quantities of proteins electroblotted onto polyvinylidene difluoride membranes. J. Biol. Chem. 262, 10 035-10 038.
    • (1987) J. Biol. Chem. , vol.262 , pp. 10035-10038
    • Matsudaira, P.1
  • 23
    • 0027959475 scopus 로고
    • Brazzein, a new high-potency thermostable sweet protein from Pentadiplandra brazzeana B
    • Ming, D. and Hellenkant, G. (1994) Brazzein, a new high-potency thermostable sweet protein from Pentadiplandra brazzeana B. FEBS Lett. 355, 106-108.
    • (1994) FEBS Lett. , vol.355 , pp. 106-108
    • Ming, D.1    Hellenkant, G.2
  • 24
    • 0029257252 scopus 로고
    • Quantification of cysteinyl sulfhydryl residues in peptides and proteins by ESI-MS or MALDI-MS
    • Ming, D., Markley, J.L. and Hellekant, G. (1995) Quantification of cysteinyl sulfhydryl residues in peptides and proteins by ESI-MS or MALDI-MS. Pept. Res. 8, 113-114.
    • (1995) Pept. Res. , vol.8 , pp. 113-114
    • Ming, D.1    Markley, J.L.2    Hellekant, G.3
  • 25
    • 0023324061 scopus 로고
    • High meiotic stability of a foreign gene introduced into tobacco by Agrobacterium-mediated transformation
    • Muller, A.J., Mendel, R.R., Schiemnann, J., Simoens, C. and Inze, D. (1987) High meiotic stability of a foreign gene introduced into tobacco by Agrobacterium-mediated transformation. Mol. Gen. Genet. 207, 171-175.
    • (1987) Mol. Gen. Genet. , vol.207 , pp. 171-175
    • Muller, A.J.1    Mendel, R.R.2    Schiemnann, J.3    Simoens, C.4    Inze, D.5
  • 26
    • 14744294442 scopus 로고
    • Production of the sweet protein monellin in transgenic plants
    • Penarrubia, L., Kim, R., Giovannoni, J., Kim, S.H. and Fisher, R. (1992) Production of the sweet protein monellin in transgenic plants. Biotechnology, 10, 561-564.
    • (1992) Biotechnology , vol.10 , pp. 561-564
    • Penarrubia, L.1    Kim, R.2    Giovannoni, J.3    Kim, S.H.4    Fisher, R.5
  • 27
    • 0022431982 scopus 로고
    • Two barley alpha-amylase gene families are regulated differently in aleurone cells
    • Rogers, J.C. (1985) Two barley alpha-amylase gene families are regulated differently in aleurone cells. J. Biol. Chem. 260, 3731-3738.
    • (1985) J. Biol. Chem. , vol.260 , pp. 3731-3738
    • Rogers, J.C.1
  • 30
    • 0025355051 scopus 로고
    • A cassette containing the bar gene of Streptomyces hygroscopicus: Selectable marker for plant transformation
    • White, J., Chang, S.-Y., Bibb, M.J. and Bibb, J.M. (1992) A cassette containing the bar gene of Streptomyces hygroscopicus: selectable marker for plant transformation. Nucleic Acids Res. 18, 1062.
    • (1992) Nucleic Acids Res. , vol.18 , pp. 1062
    • White, J.1    Chang, S.-Y.2    Bibb, M.J.3    Bibb, J.M.4
  • 31
    • 0025255488 scopus 로고
    • Preprothaumatin II is processed to biological activity in Solanum tuberosum
    • Witty, M. (1990) Preprothaumatin II is processed to biological activity in Solanum tuberosum. Biotechnol. Lett. 12, 131-136.
    • (1990) Biotechnol. Lett. , vol.12 , pp. 131-136
    • Witty, M.1
  • 34
    • 0013619412 scopus 로고    scopus 로고
    • Molecular cloning and transgenic expression of the sweet protein mabinlin in potato tubers
    • Xiong, L. and Sun, S. (1996) Molecular cloning and transgenic expression of the sweet protein mabinlin in potato tubers. Plant Physiol. 111, 57.
    • (1996) Plant Physiol. , vol.111 , pp. 57
    • Xiong, L.1    Sun, S.2
  • 35
    • 0029360358 scopus 로고
    • Issues and advances in the use of transgenic organisms for the production of thaumatin, the intensely sweet protein from Thaumatococcus daniellii
    • Zemanek, E. and Wasserman, B.P. (1995) Issues and advances in the use of transgenic organisms for the production of thaumatin, the intensely sweet protein from Thaumatococcus daniellii. Crit. Rev. Food Sci. Nutr. 35, 455-466.
    • (1995) Crit. Rev. Food Sci. Nutr. , vol.35 , pp. 455-466
    • Zemanek, E.1    Wasserman, B.P.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.