Thermal denaturation and aggregation of threadfin bream actomyosin

J. Yongsawatdigul, J. W. Park

Research output: Contribution to journalArticlepeer-review

180 Citations (Scopus)


Threadfin bream (Nemipterus bleekeri) actomyosin formed insoluble aggregates at >40°C. Conformational changes, as measured by surface hydrophobicity, began at >30°C and continued to increase with heating temperature. Reactive sulfhydryl groups increased as heating progressed and decreased at 50°C, indicating the formation of disulfide linkages of threadfin bream actomyosin at >50°C. Two distinct a-helical transition temperatures of actomyosin were found at 36.1 and 47.9°C, while major endothemic transitions were at 38.4, 51.0, and 80.7°C. Storage modulus (G′) started to increase at 34.5°C, implying the simultaneous occurrence of denaturation and aggregation. Gel network formation began to develop at >41°C.

Original languageEnglish
Pages (from-to)409-416
Number of pages8
JournalFood Chemistry
Issue number3
Publication statusPublished - 2003 Nov

Bibliographical note

Funding Information:
The authors would like to thank the Thailand Research Fund for financially supporting this research under grant RSA/15/2545. The authors also thank Walter A. Baase, Institute of Molecular Biology, University of Oregon, Eugene, OR, USA for technical assistance on circular dichroism measurements.


  • Actomyosin
  • Aggregation
  • Thermal denaturation
  • Threadfin bream

ASJC Scopus subject areas

  • Analytical Chemistry
  • Food Science


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