Thermal denaturation and aggregation of threadfin bream actomyosin

J. Yongsawatdigul, Jae W. Park

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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 1
Externally publishedYes


ASJC Scopus subject areas

  • Food Science

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