Abstract
The effects of different microwave heating (MH) methods on gelation properties of golden threadfin bream myosin and related mechanism were investigated in this study. Compared with conventional heating and one-step MH methods, myosin gel developed by 100 W coupled with 300 W MH method (MH100 + MH300) had stronger gel strength (p < 0.05) with more immobilized water (p < 0.05). Raman analysis suggested that this two-step method promoted the suitable unfolding of myosin before aggregation formation, and contributed to stabilizing the ordered secondary structure. Confocal laser scanning microscopy images revealed that 100 W microwave followed by 300 W MH produced a compact networked structure with small cavities and a thick cross-linked gel wall. Furthermore, from a perspective of molecular forces, the improvement of gelation properties by the MH100 + MH300 method were mainly involved in the enhancement of regular hydrophobic interaction and stabilization of weak protein-water hydrogenbonds.
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