메뉴 건너뛰기




Volumn 102, Issue 5, 2006, Pages 375-389

Developments in biotechnological production of sweet proteins

Author keywords

biotechnological production; brazzein; lysozyme; mabinlin; miraculin; monellin; neoculin; sweet tasting proteins; thaumatin

Indexed keywords

BIOMEDICAL ENGINEERING; BIOTECHNOLOGY;

EID: 33845649258     PISSN: 13891723     EISSN: None     Source Type: Journal    
DOI: 10.1263/jbb.102.375     Document Type: Article
Times cited : (80)

References (152)
  • 1
    • 0003876248 scopus 로고
    • O'Brien Nabors L., and Gelardi R.C. (Eds), Marcel Dekker, N.Y.
    • In: O'Brien Nabors L., and Gelardi R.C. (Eds). Alternative sweeteners (1991), Marcel Dekker, N.Y.
    • (1991) Alternative sweeteners
  • 2
    • 0015494327 scopus 로고
    • Isolation and characterization of thaumatin I and II, the sweet-tasting proteins from Thaumatococcus daniellii Benth
    • van der Wel H., and Loeve K. Isolation and characterization of thaumatin I and II, the sweet-tasting proteins from Thaumatococcus daniellii Benth. Eur. J. Biochem. 31 (1972) 221-225
    • (1972) Eur. J. Biochem. , vol.31 , pp. 221-225
    • van der Wel, H.1    Loeve, K.2
  • 3
    • 0003144348 scopus 로고
    • Isolation and characterization of the sweet principal for Dioscoreophyllum cumminsii (Stapf) Diels
    • van der Wel H. Isolation and characterization of the sweet principal for Dioscoreophyllum cumminsii (Stapf) Diels. FEBS Lett. 21 (1972) 88-90
    • (1972) FEBS Lett. , vol.21 , pp. 88-90
    • van der Wel, H.1
  • 4
    • 0015526521 scopus 로고
    • Purification of monellin, the sweet principal for Dioscoreophyllum cumminsii
    • Moris J.A., and Cagan R.H. Purification of monellin, the sweet principal for Dioscoreophyllum cumminsii. Biochim. Biophys. Acta 261 (1972) 114-122
    • (1972) Biochim. Biophys. Acta , vol.261 , pp. 114-122
    • Moris, J.A.1    Cagan, R.H.2
  • 5
    • 0027530456 scopus 로고
    • Purification, complete amino acid sequence and structure characterization of the heat stable sweet protein, mabinlin II
    • Liu X., Hu Z., Maeda S., Aiuchi T., Nakaya K., and Kurihara Y. Purification, complete amino acid sequence and structure characterization of the heat stable sweet protein, mabinlin II. Eur. J. Biochem. 211 (1993) 281-287
    • (1993) Eur. J. Biochem. , vol.211 , pp. 281-287
    • Liu, X.1    Hu, Z.2    Maeda, S.3    Aiuchi, T.4    Nakaya, K.5    Kurihara, Y.6
  • 6
    • 0027959475 scopus 로고
    • Brazzein, a new high-potency thermostable sweet protein from Pentadiplandra brazzeana B
    • Ming D., and Hellekant G. Brazzein, a new high-potency thermostable sweet protein from Pentadiplandra brazzeana B. FEBS Lett. 355 (1994) 106-108
    • (1994) FEBS Lett. , vol.355 , pp. 106-108
    • Ming, D.1    Hellekant, G.2
  • 7
    • 0034769595 scopus 로고    scopus 로고
    • Sweetness and enzymatic activity of lysozyme
    • Masuda T., Ueno Y., and Kitabatake N. Sweetness and enzymatic activity of lysozyme. J. Agric. Food Chem. 49 (2001) 4937-4941
    • (2001) J. Agric. Food Chem. , vol.49 , pp. 4937-4941
    • Masuda, T.1    Ueno, Y.2    Kitabatake, N.3
  • 11
    • 0002885432 scopus 로고
    • Isolation and characterization of pentadin, the sweet principle of Pentadiplandra brazzeana Baillon
    • van der Wel H., Larson G., Hladik A., Hladik C.M., Hellekant G., and Glaser D. Isolation and characterization of pentadin, the sweet principle of Pentadiplandra brazzeana Baillon. Chem. Senses 264 (1989) 6655-6659
    • (1989) Chem. Senses , vol.264 , pp. 6655-6659
    • van der Wel, H.1    Larson, G.2    Hladik, A.3    Hladik, C.M.4    Hellekant, G.5    Glaser, D.6
  • 12
    • 0025126845 scopus 로고
    • Purification and complete amino acid sequence of a new type of sweet protein with taste-modifying activity, curculin
    • Yamashita H., Theeraship A., Nakaya T., Nakamura Y., and Kurihara Y. Purification and complete amino acid sequence of a new type of sweet protein with taste-modifying activity, curculin. J. Biol. Chem. 265 (1990) 15770-15775
    • (1990) J. Biol. Chem. , vol.265 , pp. 15770-15775
    • Yamashita, H.1    Theeraship, A.2    Nakaya, T.3    Nakamura, Y.4    Kurihara, Y.5
  • 13
    • 0014424842 scopus 로고
    • Taste-modifying protein from miracle fruit
    • Kurihara Y., and Beidler L.M. Taste-modifying protein from miracle fruit. Science 161 (1968) 1241-1243
    • (1968) Science , vol.161 , pp. 1241-1243
    • Kurihara, Y.1    Beidler, L.M.2
  • 14
    • 0027096460 scopus 로고
    • Crystal structure of a sweet tasting protein thaumatin I, at 1.65 Å resolution
    • Ogata C.M., Gordon P.F., de Vos A.M., and Kim S.H. Crystal structure of a sweet tasting protein thaumatin I, at 1.65 Å resolution. J. Mol. Biol. 228 (1992) 893-908
    • (1992) J. Mol. Biol. , vol.228 , pp. 893-908
    • Ogata, C.M.1    Gordon, P.F.2    de Vos, A.M.3    Kim, S.H.4
  • 15
    • 0028084264 scopus 로고
    • Structures of three crystal forms of the sweet protein thaumatin
    • Ko T.P., Day J., Greenwood A., and McPherson A. Structures of three crystal forms of the sweet protein thaumatin. Acta. Crystallogr. D 50 (1994) 813-825
    • (1994) Acta. Crystallogr. D , vol.50 , pp. 813-825
    • Ko, T.P.1    Day, J.2    Greenwood, A.3    McPherson, A.4
  • 16
    • 0027527431 scopus 로고
    • Two crystal structures of a potently sweet protein. Natural monellin at 2.75 Å resolution and single-chain monellin at 1.7 Å resolution
    • Somoza J.R., Jiang F., Tong F., Kang S.H., Cho J.M., and Kim S.H. Two crystal structures of a potently sweet protein. Natural monellin at 2.75 Å resolution and single-chain monellin at 1.7 Å resolution. J. Mol. Biol. 234 (1993) 390-404
    • (1993) J. Mol. Biol. , vol.234 , pp. 390-404
    • Somoza, J.R.1    Jiang, F.2    Tong, F.3    Kang, S.H.4    Cho, J.M.5    Kim, S.H.6
  • 17
    • 0033596696 scopus 로고    scopus 로고
    • Solution structure of a sweet protein single-chain monellin determined by nuclear magnetic resonance and dynamical simulated annealing calculations
    • Lee S.Y., Lee J.H., Chang H.J., Cho J.M., Jung J.W., and Lee W. Solution structure of a sweet protein single-chain monellin determined by nuclear magnetic resonance and dynamical simulated annealing calculations. Biochemistry 38 (1999) 2340-2346
    • (1999) Biochemistry , vol.38 , pp. 2340-2346
    • Lee, S.Y.1    Lee, J.H.2    Chang, H.J.3    Cho, J.M.4    Jung, J.W.5    Lee, W.6
  • 21
    • 0000916620 scopus 로고
    • The hen egg white lysozyme molecule
    • Phillips D.C. The hen egg white lysozyme molecule. Proc. Natl. Acad. Sci. USA 57 (1967) 484-495
    • (1967) Proc. Natl. Acad. Sci. USA , vol.57 , pp. 484-495
    • Phillips, D.C.1
  • 24
    • 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., and Verrips C.T. Cloning of cDNA encoding the sweet-tasting plant protein thaumatin and its expression in Escherichia coli. Gene 18 (1982) 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.7    Verrips, C.T.8
  • 25
    • 0033525649 scopus 로고    scopus 로고
    • Crystal structure of tobacco PR-5d protein at 1.8 Å resolution reveals a conserved acidic cleft structure in antifungal thaumatin-like proteins
    • Koiwa H., Kato H., Nakatsu T., Oda J., Yamada Y., and Sato Y. Crystal structure of tobacco PR-5d protein at 1.8 Å resolution reveals a conserved acidic cleft structure in antifungal thaumatin-like proteins. J. Mol. Biol. 286 (1999) 1137-1145
    • (1999) J. Mol. Biol. , vol.286 , pp. 1137-1145
    • Koiwa, H.1    Kato, H.2    Nakatsu, T.3    Oda, J.4    Yamada, Y.5    Sato, Y.6
  • 26
    • 0000047336 scopus 로고
    • Thaumatin-like proteins
    • Witty M., and Higginbotham J.D. (Eds), CRC Press, Boca Raton
    • Dudler R., Mauch F., and Reimmann C. Thaumatin-like proteins. In: Witty M., and Higginbotham J.D. (Eds). Thaumatin (1994), CRC Press, Boca Raton 193-199
    • (1994) Thaumatin , pp. 193-199
    • Dudler, R.1    Mauch, F.2    Reimmann, C.3
  • 27
    • 0000346047 scopus 로고    scopus 로고
    • Taste properties of grape (Vitis vinifera) pathogenesis-related proteins isolated from wine
    • Peng Z., Pocock K.F., Waters E.J., Francis I.L., and Williams P.J. Taste properties of grape (Vitis vinifera) pathogenesis-related proteins isolated from wine. J. Agric. Food Chem. 45 (1997) 4639-4643
    • (1997) J. Agric. Food Chem. , vol.45 , pp. 4639-4643
    • Peng, Z.1    Pocock, K.F.2    Waters, E.J.3    Francis, I.L.4    Williams, P.J.5
  • 29
    • 0011796549 scopus 로고
    • The sales and marketing of talin
    • Witty M., and Higginbotham J.D. (Eds), CRC Press, Boca Raton, FL
    • Etheridge K. The sales and marketing of talin. In: Witty M., and Higginbotham J.D. (Eds). Thaumatin (1994), CRC Press, Boca Raton, FL 47-59
    • (1994) Thaumatin , pp. 47-59
    • Etheridge, K.1
  • 30
    • 0029828233 scopus 로고    scopus 로고
    • Strategies for achieving high-level expression of genes in Escherichia coli
    • Makrides S.C. Strategies for achieving high-level expression of genes in Escherichia coli. Microbiol. Rev. 60 (1996) 512-538
    • (1996) Microbiol. Rev. , vol.60 , pp. 512-538
    • Makrides, S.C.1
  • 31
    • 0032007853 scopus 로고    scopus 로고
    • Strategies for optimizing heterologous protein expression in Escherichia coli
    • Hannig G., and Makrides S.C. Strategies for optimizing heterologous protein expression in Escherichia coli. Trends Biotechnol. 16 (1998) 54-60
    • (1998) Trends Biotechnol. , vol.16 , pp. 54-60
    • Hannig, G.1    Makrides, S.C.2
  • 32
    • 0032884573 scopus 로고    scopus 로고
    • Recombinant protein expression in Escherichia coli
    • Baneyx F. Recombinant protein expression in Escherichia coli. Curr. Opin. Biotechnol. 10 (1999) 411-421
    • (1999) Curr. Opin. Biotechnol. , vol.10 , pp. 411-421
    • Baneyx, F.1
  • 34
    • 0033897334 scopus 로고    scopus 로고
    • Refolding the sweet-tasting protein thaumatin II from insoluble inclusion bodies synthesised in Escherichia coli
    • Daniell S., Mellits K.H., Faus I., and Connerton I. Refolding the sweet-tasting protein thaumatin II from insoluble inclusion bodies synthesised in Escherichia coli. Food Chem. 71 (2000) 105-110
    • (2000) Food Chem. , vol.71 , pp. 105-110
    • Daniell, S.1    Mellits, K.H.2    Faus, I.3    Connerton, I.4
  • 35
    • 0000634855 scopus 로고
    • Secretion of the sweet-tasting plant protein thaumatin by Bacillus subtilis
    • Illingworth C., Larson G., and Hellekant G. Secretion of the sweet-tasting plant protein thaumatin by Bacillus subtilis. Biotechnol. Lett. 10 (1988) 587-592
    • (1988) Biotechnol. Lett. , vol.10 , pp. 587-592
    • Illingworth, C.1    Larson, G.2    Hellekant, G.3
  • 36
    • 0002337293 scopus 로고
    • Secretion of the sweet-tasting plant protein thaumatin by Streptomyces lividans
    • Illingworth C., Larson G., and Hellekant G. Secretion of the sweet-tasting plant protein thaumatin by Streptomyces lividans. J. Ind. Microbiol. 4 (1989) 37-42
    • (1989) J. Ind. Microbiol. , vol.4 , pp. 37-42
    • Illingworth, C.1    Larson, G.2    Hellekant, G.3
  • 37
    • 15444377148 scopus 로고
    • Yeast systems for the commercial production of heterologous proteins
    • Buckholz R.G., and Gleeson M.A.G. Yeast systems for the commercial production of heterologous proteins. Bio/Technology 9 (1991) 1067-1072
    • (1991) Bio/Technology , vol.9 , pp. 1067-1072
    • Buckholz, R.G.1    Gleeson, M.A.G.2
  • 38
    • 0030272554 scopus 로고    scopus 로고
    • The expression of recombinant proteins in yeasts
    • Sudbery P.E. The expression of recombinant proteins in yeasts. Curr. Opin. Biotechnol. 7 (1996) 517-524
    • (1996) Curr. Opin. Biotechnol. , vol.7 , pp. 517-524
    • Sudbery, P.E.1
  • 39
    • 0030725815 scopus 로고    scopus 로고
    • Production of recombinant proteins by methylotrophic yeasts
    • Hollenberg C.P., and Gellissen G. Production of recombinant proteins by methylotrophic yeasts. Curr. Opin. Biotechnol. 8 (1997) 554-560
    • (1997) Curr. Opin. Biotechnol. , vol.8 , pp. 554-560
    • Hollenberg, C.P.1    Gellissen, G.2
  • 40
    • 0000695553 scopus 로고    scopus 로고
    • Applications of yeast in biotechonology: protein production and genetic analysis
    • Cereghino G.P.L., and Cregg J.M. Applications of yeast in biotechonology: protein production and genetic analysis. Curr. Opin. Biotechnol. 10 (1999) 422-427
    • (1999) Curr. Opin. Biotechnol. , vol.10 , pp. 422-427
    • Cereghino, G.P.L.1    Cregg, J.M.2
  • 41
    • 14744282592 scopus 로고    scopus 로고
    • Expressing cloned genes in the yeasts Saccharomyces cerevisiae and Pichia pastoris
    • Higgins S.J., and Hames B.D. (Eds), Oxford University Press, New York
    • Tuite M.F., Clare J.J., and Romanos M.A. Expressing cloned genes in the yeasts Saccharomyces cerevisiae and Pichia pastoris. In: Higgins S.J., and Hames B.D. (Eds). Protein expression (1999), Oxford University Press, New York 61-100
    • (1999) Protein expression , pp. 61-100
    • Tuite, M.F.1    Clare, J.J.2    Romanos, M.A.3
  • 43
    • 0033955337 scopus 로고    scopus 로고
    • Heterologous protein production in the methylotrophic yeast Pichia pastoris
    • Cereghino J.L., and Cregg J.M. Heterologous protein production in the methylotrophic yeast Pichia pastoris. FEMS Microbiol. Rev. 24 (2000) 45-66
    • (2000) FEMS Microbiol. Rev. , vol.24 , pp. 45-66
    • Cereghino, J.L.1    Cregg, J.M.2
  • 44
    • 0034537455 scopus 로고    scopus 로고
    • Heterologous protein production in methylotrophic yeasts
    • Gellissen G. Heterologous protein production in methylotrophic yeasts. Appl. Microbiol. Biotechnol. 54 (2000) 741-750
    • (2000) Appl. Microbiol. Biotechnol. , vol.54 , pp. 741-750
    • Gellissen, G.1
  • 46
    • 0021941768 scopus 로고
    • Microbial synthesis of the sweet-tasting plant protein thaumatin
    • Edens L., and van der Wel H. Microbial synthesis of the sweet-tasting plant protein thaumatin. Trends Biotechnol. 3 (1985) 61-64
    • (1985) Trends Biotechnol. , vol.3 , pp. 61-64
    • Edens, L.1    van der Wel, H.2
  • 47
    • 0011835613 scopus 로고
    • High level expression of thaumatin in Saccharomyces cerevisiae
    • Witty M., and Higginbotham J.D. (Eds), CRC Press, Boca Raton, FL
    • Weickmann J.L., Blair L.C., and Wilcox G.L. High level expression of thaumatin in Saccharomyces cerevisiae. In: Witty M., and Higginbotham J.D. (Eds). Thaumatin (1994), CRC Press, Boca Raton, FL 151-169
    • (1994) Thaumatin , pp. 151-169
    • Weickmann, J.L.1    Blair, L.C.2    Wilcox, G.L.3
  • 48
    • 0036669602 scopus 로고    scopus 로고
    • Production of recombinant proteins in fermenter cultures of the yeast Pichia pastoris
    • Cereghino G.P.L., Cereghino J.L., Ilgen C., and Cregg J.M. Production of recombinant proteins in fermenter cultures of the yeast Pichia pastoris. Curr. Opin. Biotechnol. 13 (2002) 329-332
    • (2002) Curr. Opin. Biotechnol. , vol.13 , pp. 329-332
    • Cereghino, G.P.L.1    Cereghino, J.L.2    Ilgen, C.3    Cregg, J.M.4
  • 49
    • 17244363998 scopus 로고    scopus 로고
    • Heterologous protein production using the Pichia pastoris expression system
    • Macauley-Patrick S., Fazenda M.L., McNeil B., and Harvey L.M. Heterologous protein production using the Pichia pastoris expression system. Yeast 22 (2005) 249-270
    • (2005) Yeast , vol.22 , pp. 249-270
    • Macauley-Patrick, S.1    Fazenda, M.L.2    McNeil, B.3    Harvey, L.M.4
  • 50
    • 14744304041 scopus 로고
    • Rapid selection using G418 of high copy number transformants of Pichia pastoris for high-level foreign gene expression
    • Scorer C.A., Clare J.J., McCombie W.R., Romanos M.A., and Sreekrishna K. Rapid selection using G418 of high copy number transformants of Pichia pastoris for high-level foreign gene expression. Bio/Technology 12 (1994) 181-184
    • (1994) Bio/Technology , vol.12 , pp. 181-184
    • Scorer, C.A.1    Clare, J.J.2    McCombie, W.R.3    Romanos, M.A.4    Sreekrishna, K.5
  • 51
    • 1542410210 scopus 로고    scopus 로고
    • Cloning, expression, and characterization of recombinant sweet-protein thaumatin II using the methylotrophic yeast Pichia pastoris
    • Masuda T., Tamaki S., Kaneko R., Wada R., Fujita Y., Mehta A., and Kitabatake N. Cloning, expression, and characterization of recombinant sweet-protein thaumatin II using the methylotrophic yeast Pichia pastoris. Biotechnol. Bioeng. 85 (2004) 761-769
    • (2004) Biotechnol. Bioeng. , vol.85 , pp. 761-769
    • Masuda, T.1    Tamaki, S.2    Kaneko, R.3    Wada, R.4    Fujita, Y.5    Mehta, A.6    Kitabatake, N.7
  • 54
    • 0026098320 scopus 로고
    • Expression of heterologous proteins in Aspergillus
    • Devchand M., and Gwynne D.I. Expression of heterologous proteins in Aspergillus. J Biotechnol. 17 (1991) 3-9
    • (1991) J Biotechnol. , vol.17 , pp. 3-9
    • Devchand, M.1    Gwynne, D.I.2
  • 55
    • 0031054007 scopus 로고    scopus 로고
    • Efficient production of secreted proteins by Aspergillus: progress, limitations and prospects
    • Gouka R.J., Punt P.J., and van den Hondel C.A. Efficient production of secreted proteins by Aspergillus: progress, limitations and prospects. Appl. Microbiol. Biotechnol. 47 (1997) 1-11
    • (1997) Appl. Microbiol. Biotechnol. , vol.47 , pp. 1-11
    • Gouka, R.J.1    Punt, P.J.2    van den Hondel, C.A.3
  • 57
    • 0027411139 scopus 로고
    • A truncated glucoamylase gene fusion for heterologous protein secretion from Aspergillus niger
    • Jeenes D.J., Marczinke B., MacKenzie D.A., and Archer D.B. A truncated glucoamylase gene fusion for heterologous protein secretion from Aspergillus niger. FEMS Microbiol. Lett. 107 (1993) 267-271
    • (1993) FEMS Microbiol. Lett. , vol.107 , pp. 267-271
    • Jeenes, D.J.1    Marczinke, B.2    MacKenzie, D.A.3    Archer, D.B.4
  • 58
    • 0029026622 scopus 로고
    • A system for production of commercial quantities of human lactoferrin: a broad spectrum natural antibiotic
    • Ward P.P., Piddington C.S., Cunningham G.A., Zhou X., Wyatt R.D., and Conneely O.M. A system for production of commercial quantities of human lactoferrin: a broad spectrum natural antibiotic. Biotechnology 13 (1995) 498-503
    • (1995) Biotechnology , vol.13 , pp. 498-503
    • Ward, P.P.1    Piddington, C.S.2    Cunningham, G.A.3    Zhou, X.4    Wyatt, R.D.5    Conneely, O.M.6
  • 60
    • 0001285486 scopus 로고
    • Expression and secretion of thaumatin from Aspergillus oryzae
    • Hahm Y.T., and Batt C.A. Expression and secretion of thaumatin from Aspergillus oryzae. Agric. Biol. Chem. 54 (1990) 2513-2520
    • (1990) Agric. Biol. Chem. , vol.54 , pp. 2513-2520
    • Hahm, Y.T.1    Batt, C.A.2
  • 61
    • 0031434861 scopus 로고    scopus 로고
    • Expression of a synthetic gene encoding the sweet-tasting protein thaumatin in the filamentous fungus Penicillium roquefortii
    • Faus I., Patiño C., del Río J.L., del Moral C., Barroso H.S., Bladé J., and Rubio V. Expression of a synthetic gene encoding the sweet-tasting protein thaumatin in the filamentous fungus Penicillium roquefortii. Biotechnol. Lett. 19 (1997) 1185-1191
    • (1997) Biotechnol. Lett. , vol.19 , pp. 1185-1191
    • Faus, I.1    Patiño, C.2    del Río, J.L.3    del Moral, C.4    Barroso, H.S.5    Bladé, J.6    Rubio, V.7
  • 62
    • 0034002755 scopus 로고    scopus 로고
    • Recent developments in the characterization and biotechnological production of sweet-tasting proteins
    • Faus I. Recent developments in the characterization and biotechnological production of sweet-tasting proteins. Appl. Microbiol. Biotechnol. 53 (2000) 145-151
    • (2000) Appl. Microbiol. Biotechnol. , vol.53 , pp. 145-151
    • Faus, I.1
  • 64
    • 0032985532 scopus 로고    scopus 로고
    • Thaumatin production in Aspergillus awamori by use of expression cassettes with strong fungal promoters and high gene dosage
    • Moralejo F.J., Cardoza R.E., Gutierrez S., and Martin J.F. Thaumatin production in Aspergillus awamori by use of expression cassettes with strong fungal promoters and high gene dosage. Appl. Environ. Microbiol. 65 (1999) 1168-1174
    • (1999) Appl. Environ. Microbiol. , vol.65 , pp. 1168-1174
    • Moralejo, F.J.1    Cardoza, R.E.2    Gutierrez, S.3    Martin, J.F.4
  • 65
    • 0036304602 scopus 로고    scopus 로고
    • Silencing of the Aspergillopepsin B (pepB) gene of Aspergillus awamori by antisense RNA expression or protease removal by gene disruption results in a large increase in thaumatin production
    • Moralejo F.J., Cardoza R.E., Gutierrez S., Lombraña M., Fierro F., and Martín J.F. Silencing of the Aspergillopepsin B (pepB) gene of Aspergillus awamori by antisense RNA expression or protease removal by gene disruption results in a large increase in thaumatin production. Appl. Environ. Microbiol. 68 (2002) 3550-3559
    • (2002) Appl. Environ. Microbiol. , vol.68 , pp. 3550-3559
    • Moralejo, F.J.1    Cardoza, R.E.2    Gutierrez, S.3    Lombraña, M.4    Fierro, F.5    Martín, J.F.6
  • 66
    • 0034530437 scopus 로고    scopus 로고
    • Overexpression and lack of degradation of thaumatin in an aspergillopepsin A-defective mutant of Aspergillus awamori containing an insertion in the pepA gene
    • Moralejo F.J., Cardoza R.E., Gutiérrez S., Sisniega H., Faus I., and Martín J.F. Overexpression and lack of degradation of thaumatin in an aspergillopepsin A-defective mutant of Aspergillus awamori containing an insertion in the pepA gene. Appl. Microbiol. Biotechnol. 54 (2000) 772-777
    • (2000) Appl. Microbiol. Biotechnol. , vol.54 , pp. 772-777
    • Moralejo, F.J.1    Cardoza, R.E.2    Gutiérrez, S.3    Sisniega, H.4    Faus, I.5    Martín, J.F.6
  • 67
    • 0034795111 scopus 로고    scopus 로고
    • A defined level of protein disulfide isomerase expression is required for optimal secretion of thaumatin by Aspergillus awamori
    • Moralejo F.J., Watson A.J., Jeenes D.J., Archer D.B., and Martín J.F. A defined level of protein disulfide isomerase expression is required for optimal secretion of thaumatin by Aspergillus awamori. Mol. Genet. Genomics 266 (2001) 246-253
    • (2001) Mol. Genet. Genomics , vol.266 , pp. 246-253
    • Moralejo, F.J.1    Watson, A.J.2    Jeenes, D.J.3    Archer, D.B.4    Martín, J.F.5
  • 68
    • 4644290897 scopus 로고    scopus 로고
    • Modulation of Aspergillus awamori thaumatin secretion by modification of bipA gene expression
    • Lombraña M., Moralejo F.J., Pinto R., and Martín J.F. Modulation of Aspergillus awamori thaumatin secretion by modification of bipA gene expression. Appl. Environ. Microbiol. 70 (2004) 5145-5152
    • (2004) Appl. Environ. Microbiol. , vol.70 , pp. 5145-5152
    • Lombraña, M.1    Moralejo, F.J.2    Pinto, R.3    Martín, J.F.4
  • 69
    • 0025255488 scopus 로고
    • Preprothaumatin II is processed to biological activity in Solanum tuberosum
    • Witty M. Preprothaumatin II is processed to biological activity in Solanum tuberosum. Biotechnol. Lett. 12 (1990) 131-136
    • (1990) Biotechnol. Lett. , vol.12 , pp. 131-136
    • Witty, M.1
  • 70
    • 0036067395 scopus 로고    scopus 로고
    • Variable properties of transgenic cucumber plants containing the thaumatin II gene from Thaumatococcus daniellii
    • Szwacka M., Kryzymowska M., Osuch A., Kowalczyk M.E., and Malepszy S. Variable properties of transgenic cucumber plants containing the thaumatin II gene from Thaumatococcus daniellii. Acta Physiol. Plant. 24 (2002) 173-185
    • (2002) Acta Physiol. Plant. , vol.24 , pp. 173-185
    • Szwacka, M.1    Kryzymowska, M.2    Osuch, A.3    Kowalczyk, M.E.4    Malepszy, S.5
  • 71
    • 33845630402 scopus 로고    scopus 로고
    • Pear transformation with the gene for supersweet protein thaumatin II
    • Lebedev V.G., Taran S.A., Shmatchenko V.V., and Dolgov S.V. Pear transformation with the gene for supersweet protein thaumatin II. Acta Hortic. 596 (2002) 199-202
    • (2002) Acta Hortic. , vol.596 , pp. 199-202
    • Lebedev, V.G.1    Taran, S.A.2    Shmatchenko, V.V.3    Dolgov, S.V.4
  • 72
    • 0041851337 scopus 로고    scopus 로고
    • Modification of tomato taste in transgenic plants carrying a thaumatin gene from Thaumatococcus daniellii Benth
    • Bartoszewski G., Niedziela A., Szwacka M., and Niemirowicz-Szczytt K. Modification of tomato taste in transgenic plants carrying a thaumatin gene from Thaumatococcus daniellii Benth. Plant Breeding 122 (2003) 347-351
    • (2003) Plant Breeding , vol.122 , pp. 347-351
    • Bartoszewski, G.1    Niedziela, A.2    Szwacka, M.3    Niemirowicz-Szczytt, K.4
  • 73
    • 22144479397 scopus 로고    scopus 로고
    • Transgenic strawberry plants expressing a thaumatin II gene demonstrate enhanced resistance to Botrytis cinerea
    • Schestibratov K.A., and Dolgov S.V. Transgenic strawberry plants expressing a thaumatin II gene demonstrate enhanced resistance to Botrytis cinerea. Sci. Hortic. 106 (2005) 177-189
    • (2005) Sci. Hortic. , vol.106 , pp. 177-189
    • Schestibratov, K.A.1    Dolgov, S.V.2
  • 74
    • 0015783386 scopus 로고
    • Chemostimulatory protein: a new type of taste stimulus
    • Morris J.A., and Cagan R.H. Chemostimulatory protein: a new type of taste stimulus. Science 181 (1973) 32-35
    • (1973) Science , vol.181 , pp. 32-35
    • Morris, J.A.1    Cagan, R.H.2
  • 75
    • 0024338385 scopus 로고
    • Redesigning a sweet protein: increased stability and renaturability
    • Kim S.H., Kang C.H., Kim R., Cho J.M., Lee Y.B., and Lee T.K. Redesigning a sweet protein: increased stability and renaturability. Protein Eng. 2 (1989) 571-575
    • (1989) Protein Eng. , vol.2 , pp. 571-575
    • Kim, S.H.1    Kang, C.H.2    Kim, R.3    Cho, J.M.4    Lee, Y.B.5    Lee, T.K.6
  • 76
    • 0023660834 scopus 로고
    • Crystal structure of the intensely sweet protein monellin
    • Ogata C., Hatada M., Tomlinson G., Shin W.C., and Kim S.H. Crystal structure of the intensely sweet protein monellin. Nature 328 (1987) 739-742
    • (1987) Nature , vol.328 , pp. 739-742
    • Ogata, C.1    Hatada, M.2    Tomlinson, G.3    Shin, W.C.4    Kim, S.H.5
  • 78
    • 0035375110 scopus 로고    scopus 로고
    • Solution structure, backbone dynamics, and stability of a double mutant single-chain monellin. Structural origin of sweetness
    • Sung Y.H., Shin J., Chang H.J., Cho J.M., and Lee W. Solution structure, backbone dynamics, and stability of a double mutant single-chain monellin. Structural origin of sweetness. J. Biol. Chem. 276 (2001) 19624-19630
    • (2001) J. Biol. Chem. , vol.276 , pp. 19624-19630
    • Sung, Y.H.1    Shin, J.2    Chang, H.J.3    Cho, J.M.4    Lee, W.5
  • 79
    • 28344440151 scopus 로고    scopus 로고
    • High-level expression of a synthetic gene encoding a sweet protein, monellin, in Escherichia coli
    • Chen Z., Cai H., Lu F., and Du L. High-level expression of a synthetic gene encoding a sweet protein, monellin, in Escherichia coli. Biotechnol. Lett. 27 (2005) 1745-1749
    • (2005) Biotechnol. Lett. , vol.27 , pp. 1745-1749
    • Chen, Z.1    Cai, H.2    Lu, F.3    Du, L.4
  • 80
    • 0028966667 scopus 로고
    • The taste-active regions of monellin, a potently sweet protein
    • Somoza J.R., Cho J.M., and Kim S.H. The taste-active regions of monellin, a potently sweet protein. Chem. Senses 20 (1995) 61-68
    • (1995) Chem. Senses , vol.20 , pp. 61-68
    • Somoza, J.R.1    Cho, J.M.2    Kim, S.H.3
  • 81
    • 10144231476 scopus 로고    scopus 로고
    • Large-scale purification of recombinant monellin from yeast
    • Kim I.H., and Lim K.J. Large-scale purification of recombinant monellin from yeast. J. Ferment. Bioeng. 82 (1996) 180-182
    • (1996) J. Ferment. Bioeng. , vol.82 , pp. 180-182
    • Kim, I.H.1    Lim, K.J.2
  • 82
    • 0030903928 scopus 로고    scopus 로고
    • High-level expression of a sweet protein, monellin, in the food yeast Candida utilis
    • Kondo K., Miura Y., Sone H., Kobayashi K., and Iijima H. High-level expression of a sweet protein, monellin, in the food yeast Candida utilis. Nat. Biotechnol. 15 (1997) 453-457
    • (1997) Nat. Biotechnol. , vol.15 , pp. 453-457
    • Kondo, K.1    Miura, Y.2    Sone, H.3    Kobayashi, K.4    Iijima, H.5
  • 84
    • 0025445835 scopus 로고
    • Solid-phase synthesis and crystallization of monellin, an intensely sweet protein
    • Kohmura M., Nio N., and Ariyoshi Y. Solid-phase synthesis and crystallization of monellin, an intensely sweet protein. Agric. Biol. Chem. 54 (1990) 1521-1530
    • (1990) Agric. Biol. Chem. , vol.54 , pp. 1521-1530
    • Kohmura, M.1    Nio, N.2    Ariyoshi, Y.3
  • 85
    • 85007661605 scopus 로고
    • Solid-phase synthesis of crystalline monellin, a sweet protein
    • Kohmura M., Nio N., and Ariyoshi Y. Solid-phase synthesis of crystalline monellin, a sweet protein. Agric. Biol. Chem. 55 (1991) 539-545
    • (1991) Agric. Biol. Chem. , vol.55 , pp. 539-545
    • Kohmura, M.1    Nio, N.2    Ariyoshi, Y.3
  • 86
    • 0025622898 scopus 로고
    • Solid-phase synthesis and crystallization of [Asn22, Gln25, Asn26]-A-chain-[Asn49, Glu50]-B-chain-monellin, an analogue of the sweet protein monellin
    • Kohmura M., Nio N., and Ariyoshi Y. Solid-phase synthesis and crystallization of [Asn22, Gln25, Asn26]-A-chain-[Asn49, Glu50]-B-chain-monellin, an analogue of the sweet protein monellin. Agric. Biol. Chem. 54 (1990) 3157-3162
    • (1990) Agric. Biol. Chem. , vol.54 , pp. 3157-3162
    • Kohmura, M.1    Nio, N.2    Ariyoshi, Y.3
  • 87
    • 0026182184 scopus 로고
    • Solid-phase synthesis of crystalline [Ser41] B-chain monellin, an analogue of the sweet protein monellin
    • Kohmura M., Nio N., and Ariyoshi Y. Solid-phase synthesis of crystalline [Ser41] B-chain monellin, an analogue of the sweet protein monellin. Agric. Biol. Chem. 55 (1991) 1831-1838
    • (1991) Agric. Biol. Chem. , vol.55 , pp. 1831-1838
    • Kohmura, M.1    Nio, N.2    Ariyoshi, Y.3
  • 88
    • 0026824282 scopus 로고
    • Solid-phase synthesis of [AsnA16]-, [AsnA22]-, [GlnA25]-, and [AsnA26] monellin, analogues of the sweet protein monellin
    • Kohmura M., Nio N., and Ariyoshi Y. Solid-phase synthesis of [AsnA16]-, [AsnA22]-, [GlnA25]-, and [AsnA26] monellin, analogues of the sweet protein monellin. Biosci. Biotechnol. Biochem. 56 (1992) 472-476
    • (1992) Biosci. Biotechnol. Biochem. , vol.56 , pp. 472-476
    • Kohmura, M.1    Nio, N.2    Ariyoshi, Y.3
  • 89
    • 0027022363 scopus 로고
    • Highly probable active site of the sweet protein monellin
    • Kohmura M., Nio N., and Ariyoshi Y. Highly probable active site of the sweet protein monellin. Biosci. Biotechnol. Biochem. 56 (1992) 1937-1942
    • (1992) Biosci. Biotechnol. Biochem. , vol.56 , pp. 1937-1942
    • Kohmura, M.1    Nio, N.2    Ariyoshi, Y.3
  • 90
    • 0012414166 scopus 로고
    • Solid-phase synthesis and structure-taste relationships of anlogs of the sweet protein monellin
    • Kohmura M., Nio N., and Ariyoshi Y. Solid-phase synthesis and structure-taste relationships of anlogs of the sweet protein monellin. Biosci. Biotechnol. Biochem. 58 (1994) 1522-1524
    • (1994) Biosci. Biotechnol. Biochem. , vol.58 , pp. 1522-1524
    • Kohmura, M.1    Nio, N.2    Ariyoshi, Y.3
  • 91
    • 0034656399 scopus 로고    scopus 로고
    • Sweetness determinant sites of brazzein, a small, heat-stable, sweet-tasting protein
    • Assadi-Porter F.M., Aceti D., and Markley J.L. Sweetness determinant sites of brazzein, a small, heat-stable, sweet-tasting protein. Arch. Biochem. Biophys. 376 (2000) 259-265
    • (2000) Arch. Biochem. Biophys. , vol.376 , pp. 259-265
    • Assadi-Porter, F.M.1    Aceti, D.2    Markley, J.L.3
  • 92
    • 33644539544 scopus 로고    scopus 로고
    • Brazzein a small, sweet protein: discovery and physiological overview
    • Hellekant G., and Danilova V. Brazzein a small, sweet protein: discovery and physiological overview. Chem Senses 30 suppl. 1 (2005) i88-i89
    • (2005) Chem Senses , vol.30 , Issue.SUPPL. 1
    • Hellekant, G.1    Danilova, V.2
  • 93
    • 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., Cheng H., and Markley J.L. Efficient production of recombinant brazzein, a small, heat-stable, sweet-tasting protein of plant origin. Arch. Biochem. Biophys. 376 (2000) 252-258
    • (2000) Arch. Biochem. Biophys. , vol.376 , pp. 252-258
    • Assadi-Porter, F.M.1    Aceti, D.2    Cheng, H.3    Markley, J.L.4
  • 95
    • 3042511803 scopus 로고    scopus 로고
    • Monkey electrophysiological and human psychophysical responses to mutants of the sweet protein brazzein: delineating brazzein sweetness
    • Jin Z., Danilova V., Assadi-Porter F.M., Markley J.L., and Hellekant G. Monkey electrophysiological and human psychophysical responses to mutants of the sweet protein brazzein: delineating brazzein sweetness. Chem. Senses 28 (2003) 491-498
    • (2003) Chem. Senses , vol.28 , pp. 491-498
    • Jin, Z.1    Danilova, V.2    Assadi-Porter, F.M.3    Markley, J.L.4    Hellekant, G.5
  • 96
    • 0343639221 scopus 로고
    • Expression of sweet protein brazzein by Saccharomyces cerevisiae
    • Guan Z., Hellekant G., and Yan W. Expression of sweet protein brazzein by Saccharomyces cerevisiae. Chem. Senses 20 (1995) 701
    • (1995) Chem. Senses , vol.20 , pp. 701
    • Guan, Z.1    Hellekant, G.2    Yan, W.3
  • 97
    • 0030199663 scopus 로고    scopus 로고
    • Synthesis and characterization of the sweet protein brazzein
    • Izawa H., Ota M., Kohmura M., and Ariyoshi Y. Synthesis and characterization of the sweet protein brazzein. Biopolymers 39 (1996) 95-101
    • (1996) Biopolymers , vol.39 , pp. 95-101
    • Izawa, H.1    Ota, M.2    Kohmura, M.3    Ariyoshi, Y.4
  • 99
    • 0027963659 scopus 로고
    • Structures of heat-stable and unstable homologues of the sweet protein mabinlin. The difference in the heat stability is due to replacement of a single amino acid residue
    • Nirasawa S., Nishino T., Katahira M., Uesugi S., Hu Z., and Kurihara Y. Structures of heat-stable and unstable homologues of the sweet protein mabinlin. The difference in the heat stability is due to replacement of a single amino acid residue. Eur. J. Biochem. 223 (1994) 989-995
    • (1994) Eur. J. Biochem. , vol.223 , pp. 989-995
    • Nirasawa, S.1    Nishino, T.2    Katahira, M.3    Uesugi, S.4    Hu, Z.5    Kurihara, Y.6
  • 100
    • 0030605258 scopus 로고    scopus 로고
    • Cloning and sequencing of a cDNA encoding a heat-stable sweet protein, mabinlin II
    • Nirasawa S., Masuda Y., Nakaya K., and Kurihara Y. Cloning and sequencing of a cDNA encoding a heat-stable sweet protein, mabinlin II. Gene 18 (1996) 225-227
    • (1996) Gene , vol.18 , pp. 225-227
    • Nirasawa, S.1    Masuda, Y.2    Nakaya, K.3    Kurihara, Y.4
  • 101
    • 0033924113 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray analysis of the thermostable sweet protein mabinlin II
    • Guan R.J., Zheng J.M., Hu Z., and Wang D.C. Crystallization and preliminary X-ray analysis of the thermostable sweet protein mabinlin II. Acta Crystallogr. D 56 (2000) 918-919
    • (2000) Acta Crystallogr. D , vol.56 , pp. 918-919
    • Guan, R.J.1    Zheng, J.M.2    Hu, Z.3    Wang, D.C.4
  • 102
    • 0032487613 scopus 로고    scopus 로고
    • Chemical synthesis and characterization of the sweet protein mabinlin II
    • Kohmura M., and Ariyoshi Y. Chemical synthesis and characterization of the sweet protein mabinlin II. Biopolymers 46 (1998) 215-223
    • (1998) Biopolymers , vol.46 , pp. 215-223
    • Kohmura, M.1    Ariyoshi, Y.2
  • 103
    • 0029072615 scopus 로고
    • Activity and stability of a new sweet protein with taste-modifying action, curculin
    • Yamashita H., Akabane T., and Kurihara Y. Activity and stability of a new sweet protein with taste-modifying action, curculin. Chem. Senses 20 (1995) 239-243
    • (1995) Chem. Senses , vol.20 , pp. 239-243
    • Yamashita, H.1    Akabane, T.2    Kurihara, Y.3
  • 104
    • 0028240193 scopus 로고
    • Crystallization and preliminary X-ray diffraction studies of curculin. A new type of sweet protein having taste-modifying action
    • Harada S., Otani H., Maeda S., Kai Y., Kasai N., and Kurihara Y. Crystallization and preliminary X-ray diffraction studies of curculin. A new type of sweet protein having taste-modifying action. J. Mol. Biol. 238 (1994) 286-287
    • (1994) J. Mol. Biol. , vol.238 , pp. 286-287
    • Harada, S.1    Otani, H.2    Maeda, S.3    Kai, Y.4    Kasai, N.5    Kurihara, Y.6
  • 105
    • 0026588709 scopus 로고
    • Molecular cloning of curculin, a novel taste-modifying protein with a sweet taste
    • Abe K., Yamashita H., Arai S., and Kurihara Y. Molecular cloning of curculin, a novel taste-modifying protein with a sweet taste. Biochim. Biophys. Acta 1130 (1992) 232-234
    • (1992) Biochim. Biophys. Acta , vol.1130 , pp. 232-234
    • Abe, K.1    Yamashita, H.2    Arai, S.3    Kurihara, Y.4
  • 107
    • 0029008975 scopus 로고
    • Structure of mannose-specific snowdrop (Galanthus nivalis) lectin is representative of a new plant lectin family
    • Hester G., Kaku H., Goldstein I.J., and Wright C.S. Structure of mannose-specific snowdrop (Galanthus nivalis) lectin is representative of a new plant lectin family. Nat. Struct. Biol. 2 (1995) 472-479
    • (1995) Nat. Struct. Biol. , vol.2 , pp. 472-479
    • Hester, G.1    Kaku, H.2    Goldstein, I.J.3    Wright, C.S.4
  • 108
    • 0031105098 scopus 로고    scopus 로고
    • Curculin, a sweet-tasting and taste-modifying protein, is a non-functional mannose-binding lectin
    • Barre A., Van Damme E.J., Peumans W.J., and Rouge P. Curculin, a sweet-tasting and taste-modifying protein, is a non-functional mannose-binding lectin. Plant Mol. Biol. 33 (1997) 691-698
    • (1997) Plant Mol. Biol. , vol.33 , pp. 691-698
    • Barre, A.1    Van Damme, E.J.2    Peumans, W.J.3    Rouge, P.4
  • 111
    • 0024533487 scopus 로고
    • Complete amino acid sequence and structure characterization of the taste-modifying protein Miraculin
    • Theerasilp S., Hitotsuya H., Nakajo S., Nakaya K., Nakamura Y., and Kurihara Y. Complete amino acid sequence and structure characterization of the taste-modifying protein Miraculin. J. Biol. Chem. 264 (1989) 6655-6659
    • (1989) J. Biol. Chem. , vol.264 , pp. 6655-6659
    • Theerasilp, S.1    Hitotsuya, H.2    Nakajo, S.3    Nakaya, K.4    Nakamura, Y.5    Kurihara, Y.6
  • 112
    • 0029163458 scopus 로고
    • Cloning and sequencing a taste-modifying protein, Miraculin
    • Masuda Y., Nirasawa S., Nakaya K., and Kurihara Y. Cloning and sequencing a taste-modifying protein, Miraculin. Gene 161 (1995) 175-177
    • (1995) Gene , vol.161 , pp. 175-177
    • Masuda, Y.1    Nirasawa, S.2    Nakaya, K.3    Kurihara, Y.4
  • 113
    • 0013619932 scopus 로고
    • Sweet proteins in general
    • Witty M., and Higginbotham J.D. (Eds), CRC Press, Boca Raton, FL
    • Kurihara Y. Sweet proteins in general. In: Witty M., and Higginbotham J.D. (Eds). Thaumatin (1994), CRC Press, Boca Raton, FL 1-18
    • (1994) Thaumatin , pp. 1-18
    • Kurihara, Y.1
  • 114
    • 30644477446 scopus 로고    scopus 로고
    • Functional expression of the taste-modifying protein, miraculin, in transgenic lettuce
    • Sun H.-J., Cui M.-L., Ma B., and Ezura H. Functional expression of the taste-modifying protein, miraculin, in transgenic lettuce. FEBS Lett. 580 (2006) 620-626
    • (2006) FEBS Lett. , vol.580 , pp. 620-626
    • Sun, H.-J.1    Cui, M.-L.2    Ma, B.3    Ezura, H.4
  • 115
    • 22844450329 scopus 로고    scopus 로고
    • Effects of chemical modification of lysine residues on the sweetness of lysozyme
    • Masuda T., Ide N., and Kitabatake N. Effects of chemical modification of lysine residues on the sweetness of lysozyme. Chem. Senses 30 (2005) 253-264
    • (2005) Chem. Senses , vol.30 , pp. 253-264
    • Masuda, T.1    Ide, N.2    Kitabatake, N.3
  • 116
    • 27244449766 scopus 로고    scopus 로고
    • Structure-sweetness relationship in egg white lysozyme: role of lysine and arginine residues on the elicitation of lysozyme sweetness Chem
    • Masuda T., Ide N., and Kitabatake N. Structure-sweetness relationship in egg white lysozyme: role of lysine and arginine residues on the elicitation of lysozyme sweetness Chem. Senses 30 (2005) 667-681
    • (2005) Senses , vol.30 , pp. 667-681
    • Masuda, T.1    Ide, N.2    Kitabatake, N.3
  • 117
    • 0016288414 scopus 로고
    • Widespread distribution of lysozyme g in egg white of birds
    • Prager E.M., Wilson A.C., and Arnheim N. Widespread distribution of lysozyme g in egg white of birds. J. Biol. Chem. 249 (1974) 7295-7297
    • (1974) J. Biol. Chem. , vol.249 , pp. 7295-7297
    • Prager, E.M.1    Wilson, A.C.2    Arnheim, N.3
  • 119
    • 0021490172 scopus 로고
    • Review of progress in lysozyme research
    • Jollès P., and Jollès J. Review of progress in lysozyme research. Mol. Cell. Biochem. 53 (1984) 165-189
    • (1984) Mol. Cell. Biochem. , vol.53 , pp. 165-189
    • Jollès, P.1    Jollès, J.2
  • 120
    • 0141450720 scopus 로고    scopus 로고
    • Antimicrobial properties of lysozyme in relation to foodborne vegetative bacteria
    • Masschalck B., and Michiels C.W. Antimicrobial properties of lysozyme in relation to foodborne vegetative bacteria. Crit. Rev. Microbiol. 29 (2003) 191-214
    • (2003) Crit. Rev. Microbiol. , vol.29 , pp. 191-214
    • Masschalck, B.1    Michiels, C.W.2
  • 121
    • 0036257549 scopus 로고    scopus 로고
    • Strategies for new antimicrobial proteins and peptides: lysozyme and aprotinin as model molecules
    • Ibrahim H.R., Aoki T., and Pellegrini A. Strategies for new antimicrobial proteins and peptides: lysozyme and aprotinin as model molecules. Curr. Pharm. Des. 8 (2002) 671-693
    • (2002) Curr. Pharm. Des. , vol.8 , pp. 671-693
    • Ibrahim, H.R.1    Aoki, T.2    Pellegrini, A.3
  • 122
    • 0023398206 scopus 로고
    • Construction of a plasmid vector for the regulatable high level expression of eukaryotic genes in Escherichia coli: an application to overproduction of chicken lysozyme
    • Miki T., Yasukochi T., Nagatani H., Furuno M., Orita T., Yamada H., Imoto T., and Horiuchi T. Construction of a plasmid vector for the regulatable high level expression of eukaryotic genes in Escherichia coli: an application to overproduction of chicken lysozyme. Protein Eng. 1 (1987) 327-332
    • (1987) Protein Eng. , vol.1 , pp. 327-332
    • Miki, T.1    Yasukochi, T.2    Nagatani, H.3    Furuno, M.4    Orita, T.5    Yamada, H.6    Imoto, T.7    Horiuchi, T.8
  • 123
    • 0028917544 scopus 로고
    • Effective renaturation of reduced lysozyme by gentle removal of urea
    • Maeda Y., Koga H., Yamada H., Ueda T., and Imoto T. Effective renaturation of reduced lysozyme by gentle removal of urea. Protein Eng. 8 (1995) 201-205
    • (1995) Protein Eng. , vol.8 , pp. 201-205
    • Maeda, Y.1    Koga, H.2    Yamada, H.3    Ueda, T.4    Imoto, T.5
  • 124
    • 10644284101 scopus 로고    scopus 로고
    • Improvement of the refolding yield and solubility of hen egg-white lysozyme by altering the Met residues attached to its N-terminus to Ser
    • Mine S., Ueda T., Hashimoto Y., and Imoto T. Improvement of the refolding yield and solubility of hen egg-white lysozyme by altering the Met residues attached to its N-terminus to Ser. Protein Eng. 13 (1997) 299-307
    • (1997) Protein Eng. , vol.13 , pp. 299-307
    • Mine, S.1    Ueda, T.2    Hashimoto, Y.3    Imoto, T.4
  • 125
    • 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., and Goodenough P. Physiological consequence of expression of soluble and active hen egg white lysozyme in Escherichia coli. Appl. Microbiol. Biotechnol. 39 (1993) 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
  • 128
    • 19644388513 scopus 로고    scopus 로고
    • Medium optimization for hen egg white lysozyme production by recombinant Aspergillus niger using statistical methods
    • Gheshlaghi R., Scharer J.M., Moo-Young M., and Douglas P.L. Medium optimization for hen egg white lysozyme production by recombinant Aspergillus niger using statistical methods. Biotechnol. Bioeng. 90 (2005) 754-760
    • (2005) Biotechnol. Bioeng. , vol.90 , pp. 754-760
    • Gheshlaghi, R.1    Scharer, J.M.2    Moo-Young, M.3    Douglas, P.L.4
  • 129
    • 0022312788 scopus 로고
    • Expression of chicken egg white lysozyme by Saccharomyces cerevisiae
    • Oberto J., and Davison J. Expression of chicken egg white lysozyme by Saccharomyces cerevisiae. Gene 40 (1985) 57-65
    • (1985) Gene , vol.40 , pp. 57-65
    • Oberto, J.1    Davison, J.2
  • 130
    • 0023423761 scopus 로고
    • Conversion of Trp 62 of hen egg-white lysozyme to Tyr by site-directed mutagenesis
    • Kumagai I., Kojima S., Tamaki E., and Miura K. Conversion of Trp 62 of hen egg-white lysozyme to Tyr by site-directed mutagenesis. J. Biochem. 102 (1987) 733-740
    • (1987) J. Biochem. , vol.102 , pp. 733-740
    • Kumagai, I.1    Kojima, S.2    Tamaki, E.3    Miura, K.4
  • 132
    • 0032991055 scopus 로고    scopus 로고
    • 15N-labeled hen lysozyme in Pichia pastoris and identification of the site in hen lysozyme where phosphate ion binds using NMR measurements
    • 15N-labeled hen lysozyme in Pichia pastoris and identification of the site in hen lysozyme where phosphate ion binds using NMR measurements. FEBS Lett. 448 (1999) 33-37
    • (1999) FEBS Lett. , vol.448 , pp. 33-37
    • Mine, S.1    Ueda, T.2    Hashimoto, Y.3    Tanaka, Y.4    Imoto, T.5
  • 133
    • 0033219409 scopus 로고    scopus 로고
    • Human lysozyme secretion increased by α-factor pro-sequence in Pichia pastoris
    • Oka C., Tanaka M., Muraki M., Suzuki K., and Jigami Y. Human lysozyme secretion increased by α-factor pro-sequence in Pichia pastoris. Biosci. Biotechnol. Biochem. 63 (1999) 1977-1983
    • (1999) Biosci. Biotechnol. Biochem. , vol.63 , pp. 1977-1983
    • Oka, C.1    Tanaka, M.2    Muraki, M.3    Suzuki, K.4    Jigami, Y.5
  • 134
    • 0034060883 scopus 로고    scopus 로고
    • Effect of extra N-terminal residues on the stability and folding of human lysozyme expressed in Pichia pastoris
    • Goda S., Takano K., Yamagata Y., Katakura Y., and Yutani K. Effect of extra N-terminal residues on the stability and folding of human lysozyme expressed in Pichia pastoris. Protein Eng. 13 (2000) 299-307
    • (2000) Protein Eng. , vol.13 , pp. 299-307
    • Goda, S.1    Takano, K.2    Yamagata, Y.3    Katakura, Y.4    Yutani, K.5
  • 136
    • 0035189012 scopus 로고    scopus 로고
    • Construction of an expression system of insect lysozyme lacking thermal stability: the effect of selection signal sequence on level of expression in the Pichia pastoris expression system
    • Koganesawa N., Aizawa T., Masaki K., Matsuura A., Nimori T., Bando H., Kawano K., and Nitta K. Construction of an expression system of insect lysozyme lacking thermal stability: the effect of selection signal sequence on level of expression in the Pichia pastoris expression system. Protein Eng. 14 (2001) 705-710
    • (2001) Protein Eng. , vol.14 , pp. 705-710
    • Koganesawa, N.1    Aizawa, T.2    Masaki, K.3    Matsuura, A.4    Nimori, T.5    Bando, H.6    Kawano, K.7    Nitta, K.8
  • 137
    • 0037296902 scopus 로고    scopus 로고
    • Expression, purification, and characterization of an unstable lysozyme mutant in Pichia pastoris
    • Liu S.T., Saito A., Azakami H., and Kato A. Expression, purification, and characterization of an unstable lysozyme mutant in Pichia pastoris. Protein Expr. Purif. 27 (2003) 304-312
    • (2003) Protein Expr. Purif. , vol.27 , pp. 304-312
    • Liu, S.T.1    Saito, A.2    Azakami, H.3    Kato, A.4
  • 138
    • 0037287049 scopus 로고    scopus 로고
    • Expression of a synthetic gene coding for ostrich egg-white lysozyme in Pichia pastoris and its enzymatic activity
    • Kawamura S., Fukamizo T., Araki T., and Torikata T. Expression of a synthetic gene coding for ostrich egg-white lysozyme in Pichia pastoris and its enzymatic activity. J. Biochem. 133 (2003) 123-131
    • (2003) J. Biochem. , vol.133 , pp. 123-131
    • Kawamura, S.1    Fukamizo, T.2    Araki, T.3    Torikata, T.4
  • 139
    • 10644257662 scopus 로고    scopus 로고
    • High yield secretion of the sweet-tasting protein lysozyme from the yeast Pichia pastoris
    • Masuda T., Ueno Y., and Kitabatake N. High yield secretion of the sweet-tasting protein lysozyme from the yeast Pichia pastoris. Protein Expr. Purif. 39 (2005) 35-42
    • (2005) Protein Expr. Purif. , vol.39 , pp. 35-42
    • Masuda, T.1    Ueno, Y.2    Kitabatake, N.3
  • 140
    • 0033582645 scopus 로고    scopus 로고
    • Putative mammalian taste receptors: a class of taste-specific GPCRs with distinct topographic selectivity
    • Hoon M.A., Adler E., Lindemeier L., Battey J.F., Ryba N.J.P., and Zuker C.S. Putative mammalian taste receptors: a class of taste-specific GPCRs with distinct topographic selectivity. Cell 96 (1999) 541-551
    • (1999) Cell , vol.96 , pp. 541-551
    • Hoon, M.A.1    Adler, E.2    Lindemeier, L.3    Battey, J.F.4    Ryba, N.J.P.5    Zuker, C.S.6
  • 144
    • 0035023861 scopus 로고    scopus 로고
    • Identification of a novel member of the T1R family of putative taste receptors
    • Sainz E., Korley J.N., Battey J.F., and Sullivan S.L. Identification of a novel member of the T1R family of putative taste receptors. J. Neurochem. 77 (2001) 896-903
    • (2001) J. Neurochem. , vol.77 , pp. 896-903
    • Sainz, E.1    Korley, J.N.2    Battey, J.F.3    Sullivan, S.L.4
  • 147
    • 4644308014 scopus 로고    scopus 로고
    • Different functional roles of T1R subunits in the heteromeric taste receptors
    • Xu H., Staszewski L., Tang H., Adler E., Zoller M., and Li X. Different functional roles of T1R subunits in the heteromeric taste receptors. Proc. Natl. Acad. Sci. USA 101 (2004) 14258-14263
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 14258-14263
    • Xu, H.1    Staszewski, L.2    Tang, H.3    Adler, E.4    Zoller, M.5    Li, X.6
  • 150
    • 0037189912 scopus 로고    scopus 로고
    • Why are sweet proteins sweet? Interaction of brazzein, monellin and thaumatin with the T1R2-T1R3 receptor
    • Temussi P.A. Why are sweet proteins sweet? Interaction of brazzein, monellin and thaumatin with the T1R2-T1R3 receptor. FEBS Lett. 526 (2002) 1-4
    • (2002) FEBS Lett. , vol.526 , pp. 1-4
    • Temussi, P.A.1
  • 151
    • 0037414437 scopus 로고    scopus 로고
    • The mechanism of interaction of sweet proteins with the T1R2-T1R3 receptor: evidence from the solution structure of G16A-MNEI
    • Spadaccini R., Trabucco F., Saviano G., Picone D., Crescenzi O., Tancredi T., and Temussi P.A. The mechanism of interaction of sweet proteins with the T1R2-T1R3 receptor: evidence from the solution structure of G16A-MNEI. J. Mol. Biol. 328 (2003) 683-692
    • (2003) J. Mol. Biol. , vol.328 , pp. 683-692
    • Spadaccini, R.1    Trabucco, F.2    Saviano, G.3    Picone, D.4    Crescenzi, O.5    Tancredi, T.6    Temussi, P.A.7
  • 152
    • 2942574363 scopus 로고    scopus 로고
    • Interaction of sweet proteins with their receptor. A conformational study of peptides corresponding to loops of brazzein, monellin and thaumatin
    • Tancredi T., Pastore A., Salvadori S., Esposito V., and Temussi P.A. Interaction of sweet proteins with their receptor. A conformational study of peptides corresponding to loops of brazzein, monellin and thaumatin. Eur. J. Biochem. 271 (2004) 2231-2240
    • (2004) Eur. J. Biochem. , vol.271 , pp. 2231-2240
    • Tancredi, T.1    Pastore, A.2    Salvadori, S.3    Esposito, V.4    Temussi, P.A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.