Effect of salt and heating on a mesoscopic structure composed of ovalbumin globules in aqueous solution

M. Sugiyama, A. Nakamura, N. Hiramatsu, M. Annaka, S. Kuwajima, K. Hara

研究成果: ジャーナルへの寄稿記事

9 引用 (Scopus)

抄録

Mesoscopic structural changes of an ovalbumin solution by heating and adding NaCl have been investigated with a small-angle neutron scattering method. In the natural solution, a broad peak at q = 0.057 Å-1, which disappeared by adding NaCl, indicates the existence of an electrostatic long-range interaction between the ovalbumin globules. Along with the broad peak, a prominent intensity increase in a very small q region was observed on heating except for the initial and final stages, indicating the coexistence of a disordered structure of the denatured ovalbumin and a regular-interspacing structure of the natural ovalbumin globules. Though the macroscopic feature in the final stage, whether the solution forms a gel (10 wt %) or not (5 wt %), strongly depended on the concentration of the ovalbumin, the scattering profiles showed a common characteristic feature: the appearance of a new peak around q = 0.023 Å-1, which indicates the emergence of another regular structure.

元の言語英語
ページ(範囲)1071-1073
ページ数3
ジャーナルBiomacromolecules
2
発行部数4
DOI
出版物ステータス出版済み - 12 1 2001

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Ovalbumin
Heating
Salts
Neutron scattering
Electrostatics
Small Angle Scattering
Gels
Scattering
Neutrons
Static Electricity

All Science Journal Classification (ASJC) codes

  • Organic Chemistry
  • Biochemistry, Genetics and Molecular Biology(all)
  • Polymers and Plastics
  • Materials Chemistry

これを引用

Effect of salt and heating on a mesoscopic structure composed of ovalbumin globules in aqueous solution. / Sugiyama, M.; Nakamura, A.; Hiramatsu, N.; Annaka, M.; Kuwajima, S.; Hara, K.

:: Biomacromolecules, 巻 2, 番号 4, 01.12.2001, p. 1071-1073.

研究成果: ジャーナルへの寄稿記事

Sugiyama, M. ; Nakamura, A. ; Hiramatsu, N. ; Annaka, M. ; Kuwajima, S. ; Hara, K. / Effect of salt and heating on a mesoscopic structure composed of ovalbumin globules in aqueous solution. :: Biomacromolecules. 2001 ; 巻 2, 番号 4. pp. 1071-1073.
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abstract = "Mesoscopic structural changes of an ovalbumin solution by heating and adding NaCl have been investigated with a small-angle neutron scattering method. In the natural solution, a broad peak at q = 0.057 {\AA}-1, which disappeared by adding NaCl, indicates the existence of an electrostatic long-range interaction between the ovalbumin globules. Along with the broad peak, a prominent intensity increase in a very small q region was observed on heating except for the initial and final stages, indicating the coexistence of a disordered structure of the denatured ovalbumin and a regular-interspacing structure of the natural ovalbumin globules. Though the macroscopic feature in the final stage, whether the solution forms a gel (10 wt {\%}) or not (5 wt {\%}), strongly depended on the concentration of the ovalbumin, the scattering profiles showed a common characteristic feature: the appearance of a new peak around q = 0.023 {\AA}-1, which indicates the emergence of another regular structure.",
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AU - Sugiyama, M.

AU - Nakamura, A.

AU - Hiramatsu, N.

AU - Annaka, M.

AU - Kuwajima, S.

AU - Hara, K.

PY - 2001/12/1

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N2 - Mesoscopic structural changes of an ovalbumin solution by heating and adding NaCl have been investigated with a small-angle neutron scattering method. In the natural solution, a broad peak at q = 0.057 Å-1, which disappeared by adding NaCl, indicates the existence of an electrostatic long-range interaction between the ovalbumin globules. Along with the broad peak, a prominent intensity increase in a very small q region was observed on heating except for the initial and final stages, indicating the coexistence of a disordered structure of the denatured ovalbumin and a regular-interspacing structure of the natural ovalbumin globules. Though the macroscopic feature in the final stage, whether the solution forms a gel (10 wt %) or not (5 wt %), strongly depended on the concentration of the ovalbumin, the scattering profiles showed a common characteristic feature: the appearance of a new peak around q = 0.023 Å-1, which indicates the emergence of another regular structure.

AB - Mesoscopic structural changes of an ovalbumin solution by heating and adding NaCl have been investigated with a small-angle neutron scattering method. In the natural solution, a broad peak at q = 0.057 Å-1, which disappeared by adding NaCl, indicates the existence of an electrostatic long-range interaction between the ovalbumin globules. Along with the broad peak, a prominent intensity increase in a very small q region was observed on heating except for the initial and final stages, indicating the coexistence of a disordered structure of the denatured ovalbumin and a regular-interspacing structure of the natural ovalbumin globules. Though the macroscopic feature in the final stage, whether the solution forms a gel (10 wt %) or not (5 wt %), strongly depended on the concentration of the ovalbumin, the scattering profiles showed a common characteristic feature: the appearance of a new peak around q = 0.023 Å-1, which indicates the emergence of another regular structure.

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