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.
Bibliographical noteFunding 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.
- Thermal denaturation
- Threadfin bream
ASJC Scopus subject areas
- Analytical Chemistry
- Food Science