메뉴 건너뛰기




Volumn 71, Issue 1, 2000, Pages 105-110

Refolding the sweet-tasting protein thaumatin II from insoluble inclusion bodies synthesised in Escherichia coli

Author keywords

Protein refolding; Sweet taste; Thaumatin; Thiol disulfide redox

Indexed keywords

GLUTATHIONE; RECOMBINANT PROTEIN; THAUMATIN; THAUMATIN II; UNCLASSIFIED DRUG;

EID: 0033897334     PISSN: 03088146     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0308-8146(00)00151-5     Document Type: Article
Times cited : (23)

References (23)
  • 3
    • 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., 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
  • 4
    • 0021941768 scopus 로고
    • Microbial synthesis of the sweet-tasting plant protein thaumatin
    • Edens L., Van der Wel H. Microbial synthesis of the sweet-tasting plant protein thaumatin. Trends in Biotechnology. 3:1985;61-64.
    • (1985) Trends in Biotechnology , vol.3 , pp. 61-64
    • Edens, L.1    Van Der Wel, H.2
  • 5
    • 0011796549 scopus 로고
    • The sales and marketing of Talin
    • In M. Witty & J.D. Higginbotham, Boca Raton, FL:CRC Press
    • Etheridge, K. (1994) The sales and marketing of Talin. In M. Witty & J.D. Higginbotham, Thaumatin. Boca Raton, FL:CRC Press.
    • (1994) Thaumatin
    • Etheridge, K.1
  • 8
    • 0001285486 scopus 로고
    • Expression and secretion of thaumatin from Aspergillus oryzae
    • Hahm Y.T., 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
  • 10
    • 0000634855 scopus 로고
    • Secretion of the sweet-tasting plant protein thaumatin by Bacillus subtilis
    • Illingworth C., Larson G., Hellekant G. Secretion of the sweet-tasting plant protein thaumatin by Bacillus subtilis. Biotechnology Letters. 10:1988;587-592.
    • (1988) Biotechnology Letters , vol.10 , pp. 587-592
    • Illingworth, C.1    Larson, G.2    Hellekant, G.3
  • 11
    • 0002337293 scopus 로고
    • Secretion of the sweet-tasting plant protein thaumatin by Streptomyces lividans
    • Illingworth C., Larson G., 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
  • 12
    • 0033371883 scopus 로고    scopus 로고
    • Heat-induced formation of intermolecular disulfide linkages between thaumatin molecules that do not contain cysteine residues
    • Kaneko R., Kitabatake N. Heat-induced formation of intermolecular disulfide linkages between thaumatin molecules that do not contain cysteine residues. Journal of Agricultural Food Chemistry. 47:1999;4950-4955.
    • (1999) Journal of Agricultural Food Chemistry , vol.47 , pp. 4950-4955
    • Kaneko, R.1    Kitabatake, N.2
  • 13
    • 0015908718 scopus 로고
    • Spectrometric investigation of thaumatin I and II, two sweet-tasting proteins from Thaumatococcus daniellii Benth
    • Korver O., Gorkom M.V., Van der Wel H. Spectrometric investigation of thaumatin I and II, two sweet-tasting proteins from Thaumatococcus daniellii Benth. European Journal of Biochemistry. 35:1973;554-558.
    • (1973) European Journal of Biochemistry , vol.35 , pp. 554-558
    • Korver, O.1    Gorkom, M.V.2    Van Der Wel, H.3
  • 14
    • 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., 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
  • 15
    • 0027096460 scopus 로고
    • Crystal structure of a sweet tasting protein thaumatin I, at 1 65A resolution
    • Ogata C.M., Gordon P.F., de Vos A.M., Kim S.H. Crystal structure of a sweet tasting protein thaumatin I, at 1 65A resolution. Journal of Molecular Biology. 228:1992;893-908.
    • (1992) Journal of Molecular Biology , vol.228 , pp. 893-908
    • Ogata, C.M.1    Gordon, P.F.2    De Vos, A.M.3    Kim, S.H.4
  • 16
    • 0019873820 scopus 로고
    • Estimation of globular protein secondary structure from circular dichroism
    • Provencher S.W., Glöckner J. Estimation of globular protein secondary structure from circular dichroism. Biochemistry. 20:1981;33-37.
    • (1981) Biochemistry , vol.20 , pp. 33-37
    • Provencher, S.W.1    Glöckner, J.2
  • 17
    • 0025861478 scopus 로고
    • Convex constraint analysis: A natural deconvolution of circular dichroism curves of proteins
    • Perczel A., Hollósi M., Tusnády G., Fasman G.D. Convex constraint analysis. A natural deconvolution of circular dichroism curves of proteins Protein Eng. 4:1991;669-679.
    • (1991) Protein Eng. , vol.4 , pp. 669-679
    • Perczel, A.1    Hollósi, M.2    Tusnády, G.3    Fasman, G.D.4
  • 18
    • 0026279733 scopus 로고
    • Use of bacteriophage T7 lysozyme to improve an inducible T7 expression system
    • Studier F.W. Use of bacteriophage T7 lysozyme to improve an inducible T7 expression system. Journal of Molecular Biology. 219:1991;37-44.
    • (1991) Journal of Molecular Biology , vol.219 , pp. 37-44
    • Studier, F.W.1
  • 19
    • 0006003191 scopus 로고
    • Structure-activity relations in the thaumatin molecule
    • In M. Witty, J.D. Higginbotham Boca Raton, FL:CRC Press
    • Van der Wel, H. (1994). Structure-activity relations in the thaumatin molecule. In M. Witty, J.D. Higginbotham Thaumatin., Boca Raton, FL:CRC Press.
    • (1994) Thaumatin
    • Van Der Wel, H.1
  • 21
    • 0015494327 scopus 로고
    • Isolation and characterization of thaumatin I and II, the sweet-tasting proteins from Thaumatococcus daniellii Benth
    • Van der Wel H., Loeve K. Isolation and characterization of thaumatin I and II, the sweet-tasting proteins from Thaumatococcus daniellii Benth. European Journal of Biochemistry. 31:1972;221-225.
    • (1972) European Journal of Biochemistry , vol.31 , pp. 221-225
    • Van Der Wel, H.1    Loeve, K.2
  • 22
    • 0031743874 scopus 로고    scopus 로고
    • New technologies for taste modifying proteins
    • Witty M. New technologies for taste modifying proteins. Trends in Food Science & Technology. 9:1998;275-280.
    • (1998) Trends in Food Science & Technology , vol.9 , pp. 275-280
    • Witty, M.1
  • 23
    • 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., Wasserman B.P. 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. 35:1995;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.