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1991 Fiscal Year Final Research Report Summary

Structure Determination of a New Type of Taste-modifying Protein with Activity of Modifying a Sour Taste into Sweet Taste.

Research Project

Project/Area Number 01480066
Research Category

Grant-in-Aid for General Scientific Research (B)

Allocation TypeSingle-year Grants
Research Field 製造化学・食品
Research InstitutionYokohama National University

Principal Investigator

KURIHARA Yoshie  Yokohama Natl. Univ., Fac. of Education, Professor., 教育学部, 教授 (90017715)

Co-Investigator(Kenkyū-buntansha) NAGASE Shigeru  Yokohama Natl. Univ., Fac. of Education, Professor, 教育学部, 教授 (30134901)
Project Period (FY) 1989 – 1991
Keywordscurculin / sweet protein / taste-modifying protein
Research Abstract

A new taste-modifylng protein named curculin was extracted with 0.5 M NaCl solution from fruits of Curculiro atifolia and purified by ammonium sulfate fractionation, CM-Sepharose Ion-exchange chromatography, and gcl filtration. The purilied curculin thus obtained gave a single band having molecular welght of 12, 000 In sodium dodecyl sulfate-polyacrylamide gel electrophoresis In the presence of 8 M urea. The molecular weight determined by low-angle light scattcring was 27, 800. These results suggested that native curculin Is a dimer of 12, 000 dalton polypeptide. The complete amino acid sequence of curculin was determined by an automatic Edman degradation method. Curculin consists of 114 amino acid residues. Curculin itself elicits a sweet taste. After curculin, water elicits a sweet taste and sour substances induce stronger sweetness. No protein carrying both a sweet-tasting activity and taste-modifying activitics has ever been known. There were 5 sets of tripeptides common to miraculin (taste-modifying protein). 6 sets of tripeptides common to thaumatln (sweet protein) and 2 sets of tripeptides common to monellin (sweet protein). An enzymc immunoassay method for curculin was established. This method can accurately quantity 0.05-20 ng of curculin, sensitivity about 3000-times that of the psychometric method. Immunoblot analysis Indicated that antiserum to curculin was faintly reactive with miraculin, but not with thaumatin or moncllin. The mechanism of the taste-modifying actions of curculin were discussed.

  • Research Products

    (13 results)

All Other

All Publications (13 results)

  • [Publications] 栗原 良枝: "甘味機能調節物質" 化学と生物. 29. 531-536 (1991)

    • Description
      「研究成果報告書概要(和文)」より
  • [Publications] 栗原 良枝: "みにれびゅう;甘味タンパク質および甘味誘導タンパク質" 生化学. 63. 1340-1345 (1991)

    • Description
      「研究成果報告書概要(和文)」より
  • [Publications] 栗原 良枝: "味を変える蛋白質一砂糖なしでも紅茶やレモンが甘くなる" 現代化学. 240. 28-33 (1991)

    • Description
      「研究成果報告書概要(和文)」より
  • [Publications] S.Nakajho,et al.: "An enzyme immunoassay and immunoblot analysis for curculin,a new type of taste modifying protein:cross-reactivity of curculin and miraculin to both antibodies" Biochim.Biophys.Acta,. 1118. 293-297 (1992)

    • Description
      「研究成果報告書概要(和文)」より
  • [Publications] H.Igcta,et al.: "Determination of disulfide array and subunit structure of taste-modifying protein,miraculin" Biochim.Biophys.Acta.1079. 303-307 (1991)

    • Description
      「研究成果報告書概要(和文)」より
  • [Publications] H.Yamashita,et al: "Purification and complete amino acid sequence of a new type of sweet protein with taste-modifying activity,curculin" J.Biol.Chem.265. 15770-15775 (1990)

    • Description
      「研究成果報告書概要(和文)」より
  • [Publications] Y.Kurihara: "Characteristics of proteins with sweet and/or taste-modifying properties(Critical Reviews in Food Sciences and Nutrition," CRC PRESS, 25 (1992)

    • Description
      「研究成果報告書概要(和文)」より
  • [Publications] H. Yamashita, S. Theerasilp, T. Aiuchi, K. Nakaya, Y. Nakamura, and Y. Kurihara: "Purification and complete amino acid sequence of a new type of sweet protein with taste-modifying activity, curculin." J. Biol. Chem.265. 15770-15775 (1990)

    • Description
      「研究成果報告書概要(欧文)」より
  • [Publications] N. Takahashi, H. Hitotsuya, H. Hanzawa, Y. Arata and Y. Kurihara: "Structural study of asparagine-linked Oligosac charide moicty of taste-modifying protein, miraculin" J. Biol. Chem.265. 7793-7798 (1990)

    • Description
      「研究成果報告書概要(欧文)」より
  • [Publications] H. Igeta, Y. Tamura, K. Nakaya, Y. Nakamura, and Y. Kurihara: "Determination of disulfide array and subunit structure of taste-modifying protein, miraculin" Biochem. Biophys. Acta.1079. 303-307 (1991)

    • Description
      「研究成果報告書概要(欧文)」より
  • [Publications] S. Nakajho, T. Akabane, K. Nakaya, Y. Nakamur a, nad Y. Kurihara: "An enzyme immunoassay and immunoblot analysis for curculin, a new type of taste modifying protein : cross-reactivity of curculin and miraculin to both antibodies" Biochem. Biophys. Acta.1118. 293-297 (1992)

    • Description
      「研究成果報告書概要(欧文)」より
  • [Publications] K. Abe, H. Yamashita, S. Arai and Y. Kurihara: "Molecular cloning of curculin, a novel taste-modifying protein with sweet taste" Biochem. Biophys. Acta. (1992)

    • Description
      「研究成果報告書概要(欧文)」より
  • [Publications] Y. Kurihara: "Characteristics of proteins with sweet and/or taste-modifying properties" Critical Reviews in Food Sciences and Nutriti. CRC Press.

    • Description
      「研究成果報告書概要(欧文)」より

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Published: 1993-03-16  

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