2007年8月
Gelation mechanism of surimi studied by H-1 NMR relaxation measurements
JOURNAL OF FOOD SCIENCE
- ,
- ,
- ,
- 巻
- 72
- 号
- 6
- 開始ページ
- E362
- 終了ページ
- E367
- 記述言語
- 英語
- 掲載種別
- 研究論文(学術雑誌)
- DOI
- 10.1111/j.1750-3841.2007.00411.x
- 出版者・発行元
- BLACKWELL PUBLISHING
In order to elucidate the gelation mechanism of surimi, the temperature dependence of water proton, spin-spin relaxation time (H-1 T-2) has been described by a theoretical approach, in which the exposed protein surface is taken into account. Water H-1 T2 measured for horse mackerel surimi in the presence of 2.5% NaCl was analyzed on the basis of the consideration for the denaturation and the aggregation of protein in order to explain the-macroscopic structural change during the heating and the cooling processes. The temperature dependence of water H-1 T2 and the fraction of rigid component gave a clear explanation for the getation, mechanism of surimi. Differential scanning calorimetry thermogram, and dynamic viscoelastic measurements supported the results of nuclear magnetic resonance (NMR) measurements. It has been demonstrated that the measurement of NMR relaxation times is useful to describe the gelation mechanism of surimi.
- リンク情報
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- DOI
- https://doi.org/10.1111/j.1750-3841.2007.00411.x
- CiNii Articles
- http://ci.nii.ac.jp/naid/80018215574
- PubMed
- https://www.ncbi.nlm.nih.gov/pubmed/17995681
- Web of Science
- https://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=JSTA_CEL&SrcApp=J_Gate_JST&DestLinkType=FullRecord&KeyUT=WOS:000248725200015&DestApp=WOS_CPL
- URL
- https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=34547829770&origin=inward
- ID情報
-
- DOI : 10.1111/j.1750-3841.2007.00411.x
- ISSN : 0022-1147
- CiNii Articles ID : 80018215574
- PubMed ID : 17995681
- SCOPUS ID : 34547829770
- Web of Science ID : WOS:000248725200015