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Development and creation of food materials having novel characteristics by thermal treatment of food proteins

Research Project

Project/Area Number 11558006
Research Category

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

Allocation TypeSingle-year Grants
Section展開研究
Research Field 食生活
Research InstitutionKYOTO UNIVERSITY

Principal Investigator

KITABATAKE Naofumi  Research Institute for Food, 食糧科学研究所, 教授 (30135610)

Co-Investigator(Kenkyū-buntansha) HASUDA Tetsuya  Science, Kyoto University Instructor Professor, 食糧科学研究所, 助手 (80311744)
Project Period (FY) 1999 – 2000
Project Status Completed (Fiscal Year 2000)
Budget Amount *help
¥4,700,000 (Direct Cost: ¥4,700,000)
Fiscal Year 2000: ¥2,000,000 (Direct Cost: ¥2,000,000)
Fiscal Year 1999: ¥2,700,000 (Direct Cost: ¥2,700,000)
KeywordsMilk Whey Protein / Food Functionality / Lactoglobulin / 牛乳乳清 / βラクトグロブリン / 加熱 / 可溶性凝集体 / 食品物性
Research Abstract

Milk whey protein consists of globular proteins such as β-lactoglobulin (βLG), α-lactalbumin, and serum albumin βLG, the major protein component, is largely responsible for the aggregation and gelation of whey protein on heating. A βLG molecule consists of 162 amino acid residues and has two disulfide (S S) bonds, at Cys^<66>-Cys^<160> and Cys^<106>-Cys^<119>, and a free sulfhydryl group at Cys^<121>. Under physiological conditions, this globular protein exists as a dimer consisting of antiparallel β-sheets formed by nine β-strands. βLG has seven variants and most of them are variant A and B.βLG variant A (βLG A) was used throughout this study. βLG A molecules aggregate when they are heated, and intermolecular disulfide bonds seem to play an important role for such molecular aggregation. Aggregation of βLG A depends on pH, salt concentration, and heating temperature. Although the importance of free sulfhydryl residue is accepted for molecular aggregation of βLG on heating, the molecula … More r events occurring on the thermal denaturation and aggregation via intermolecular disulfide formation have not been revenaled in detail. To reveal the mechanism of heat-induced molecular aggregation of βLG, it is important to clarify the participation of sulfhydryl residue. Milk whey protein is widely used as a food ingredient due to its high gelation and emulsification ability. Change in the conformation of the protein at molecular level strongly influences the functional properties of the food protein. The gel formation is usually induced by formation of network structure with protein molecules when heated in the food system. Heating induces the conformational change in a protein molecule. The molecular interaction among the denatured protein molecules is necessary for the construction of the three-dimensional network structure. In the present study the conformational change of βLG A by heating was examined, particularly its reversibility and pH dependency. In addition, the molecular interactions through disulfide bridge and other non-covalent forces have been analyzed to reveal the mechanism of molecular polymerization and gelation. Less

Report

(3 results)
  • 2000 Annual Research Report   Final Research Report Summary
  • 1999 Annual Research Report
  • Research Products

    (11 results)

All Other

All Publications (11 results)

  • [Publications] N.Kitabatake,R.Wada and Y.Fujita: "Reversible Conformational Change in the β-Lactoglobulin A Modified with N-ethylmaleimide and Resistance to Molecular Aggregation on Heating"J.Aqric.Food.Chem.. (in press). (2001)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      2000 Final Research Report Summary
  • [Publications] Y.Koga,T.Koga,Y.Kinekawa,and Naofumi Kitabatake: "Properties of a Thermostable Emulsion Prepared from the Process Whey Protein and Olive Oil ; Use as a Cream-Substitute and Its Practical Application to Panna-Cotta"J.Cookery Sci.Jp. (in press). (2001)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      2000 Final Research Report Summary
  • [Publications] N.Kitabatake, R.Wada and Y.Fujita: "Reversible Conformational Change in the β-Lactoglobulin A Modified with N-ethylmaleimide and Resistance to Molecular Aggregation on Heating"J.Agric.Food Chem.. (in press.). (2001)

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      2000 Final Research Report Summary
  • [Publications] Y.Koga, T.Koga, Y.Kinekawa, and Naofumi Kitabatake: "Properties of a Thermostable Emulsion Prepared from the Process Whey Protein and Olive Oil ; Use as a Cream-Substitute and Its Practical Application to Panna-Cotta"J.Cookery Sci.Jp. (in press). (2001)

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      2000 Final Research Report Summary
  • [Publications] N.Kitabatake,R.Wada & Y.Fujita: "Reversible Conformational Change in the β-hactoglobulin A Modified with N-ethylmaleimide and Resistance to Holecular Aggregetion in Heating"J.Agric.Food Chem. (in press). (2001)

    • Related Report
      2000 Annual Research Report
  • [Publications] Y.Koga,T.Koga,Y.Kinekawa,N.Kitabatake: "Properties of Themostable Emulsion Pregrared with the Process whey and Olive Oil; Use for a Cream-Substitute and Its Practical Application to Panna-Cotta"J.Cookery Sci.Jp.. (in press). (2001)

    • Related Report
      2000 Annual Research Report
  • [Publications] R.Kaneko and N.Kitabatake: "Heat-induced Formation of Intermolecular Disulfide Linkages…"J. Agric Food Chem.. 47. 4950-4955 (1999)

    • Related Report
      1999 Annual Research Report
  • [Publications] Y.Koga,T.Izumi,Y.Kinekawa,N.Kitabatake: "Effects of Nacl, Sucrose and Heat…"J. Cookery Sci. Jp.. 32. 2-9 (1999)

    • Related Report
      1999 Annual Research Report
  • [Publications] N.Kitabatake and Y.Fujita: "Functionality of Dialyed Soybean Extract"J. Amer. Oil Chem. Soc.. 77. 441-446 (2000)

    • Related Report
      1999 Annual Research Report
  • [Publications] T.Masuda,K.Yasumoto,N.Kitabatake: "Monitoring the irradiation-induced conformational…"Bio Sci. Biotech. Biochem. (in press). (2000)

    • Related Report
      1999 Annual Research Report
  • [Publications] 北畠直文(分相)日本栄養食糧学会監修: "大豆タンパク質の加工特性と生理機能"建帛社. 213 (1999)

    • Related Report
      1999 Annual Research Report

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Published: 1999-04-01   Modified: 2016-04-21  

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