Peptide gelation contributes to the tenderness and viscoelasticity of candy abalone

Abstract

Dried abalones are precious products, in which candy abalone is the most treasured one, owing to its unique taste. After rehydration and simmering, the core part tastes extraordinarily tender and viscoelastic, just like a soft candy which may almost melt in mouth. However, the reason for this has yet to be elucidated. The purpose of this study is to research the formation mechanism of the candy-like core in candy abalone. First of all, we characterized the viscoelasticity, microstructure and protein changes of candy abalone during the simmering process. The texture results indicated that the springiness and adhesiveness of candy abalone showed an increase. Scanning and transmission electron microscopy suggested that myofibrillar protein in candy abalone formed a dense three-dimensional network hydrogel structure. Sodium dodecyl sulfate–polyacrylamide gel electrophoresis revealed such a hydrogel structure might be derived from the degradation of the myofibrillar protein during the drying process. Also, we identified degraded peptides mainly stemmed from paramyosin by mass spectrometry. Moreover, molecular dynamics simulation revealed that the hydrogen bonds and hydrophobic interactions are mainly responsible for the self-assembly of peptides during the rehydration and simmering stages. Different from reported protein hydrogels, the rheological and morphological properties of the formed peptide hydrogels in candy abalone have significant changes. In this study, we found that the myofibrillar protein of fresh abalone degraded into peptides during the drying process, which further cross-linked to form a peptide hydrogel during the rehydration and simmering stages, thereby producing a unique viscoelastic candy-like core in candy abalone.

Graphical abstract