Study On The Chemical Interaction Of Abalone Protein During Heating Treatment

Abalone (Haliotis discus hannai) is an important commercial seafood species. Pleopodmuscle is the edible part of abalone, which is rich in protein and mainly composed ofmyofibril protein and collagen. The change in conformation and aggregation of protein duringheating would affect the quality of the product. In this study, we investigated the change ofchemical interaction and texture in different part from abalone pleopod muscle during heatingprocess, and compared with those of scallops adductor and tilapia mossambica in order toexplore the change of chemical interaction among different species. In addition, myofibrilprotein was extracted from abalone gastropod muscle, the change of chemical interaction andgel properties during heating process were studied and then compared with that of wholeabalone pleopod muscle.In this essay, we determined the change of chemical interaction in different parts fromabalone pleopod muscle under different heating conditions (60℃,80℃,100℃). Results showthat as temperature increasing, the content of ionic bonds and hydrogen bonds decreasedgradually, the content of hydrophobic bonds firstly increased and then decreased; the contentof disulfide bonds and covalent bonds increased progressively. Whereas amplitude ofvariation of different parts were different, which was related to the content of myofibrilprotein and collagen. The change of texture parameters of different parts was studied. Theresults show that hardness and resilience of middle part of abalone pleopodmuscle(MPAPM)and the edge and transition part of abalone pleopod muscle (ETPAPM)increase as temperature rose; chewiness of the middle part decreased while chewiness of theedge and transition part increased firstly and then decreased; Springiness of two parts changedslowly andthe change of cohesiveness were not significant at high temperature. We found aclose correlation between textural characteristics and chemical interaction. Ionic bond,hydrogen bond and hydrophobic bond played important role in gel formation at the stage oflow temperature. The gel strength was soft and showed low value oftextural parameters.Whereas, disulfide bond and covalent bond were the main chemical interaction for gelmaintenance in the stage of high temperature, and the gel strength showed hard and high value of the textural parameters. The result from the comparison among abalone pleopodmuscle, scallops adductor and tilapia mossambica showed that the change of chemicalinteraction were different. The reduction of ionic bond and hydrogen bond of scallopsadductor and the edge and transition part howed higher value; the rise of disulfide bond andcovalent bond of tilapia mossambica, scallops adductor and the middle part showed highervalue, which was consistent with the protein content of myofibril protein and collagen amongdifferent species.The change of chemical interaction and gel properties of abalone myofibril protein wereinvestigated during heating process, which showed that the content of ionic bond, andhydrogen bond decreased sharply; the content of hydrophobic bond was firstly increased andthen decreased in all the treatments, and the content of hydrophobic bond at100℃, disulfidebond and covalent bond increased apparently. The gel strength of the abalone myofibrilprotein increased during heating process, and exhibited a remarkably correlation withchemical interaction. In the early stage of heating (30~60℃), hydrogen bond played the mostimportant part in enhancing gel strength, whereas, hydrophobic bond and disulfide bond werethe main chemical interactions for gel formation and maintenance from70℃to100℃. Theresult showed that the change of chemical interaction in abalone myofibril protein and in thewhole abalone pleopod muscle during heating were similar.