Effect of Interaction between Mealworm Protein and Myofibrillar Protein on the Rheological Properties and Thermal Stability of the Prepared Emulsion Systems

Abstract

In this study, we investigated the effect of replacing myofibrillar protein (pork ham) with edible insect proteins (Tenebrio molitor L.) in meat emulsion systems and examined the interaction between the two types of proteins. We also evaluated the rheological properties and thermal stability of these meat emulsions. The replacement ratios of myofibrillar protein and edible insect protein were as follows: 100:0 (EI0), 80:20 (EI20), 60:40 (EI40), 40:60 (EI60), 20:80 (EI80), and 0:100 (EI100). The pH, redness, and yellowness of the emulsion systems, after replacing myofibrillar protein with T. molitor protein, significantly increased with T. molitor protein concentrations. In contrast, the lightness, hardness, cohesiveness, gumminess, chewiness, apparent viscosity, and differential scanning calorimetry (DSC) of the emulsion systems decreased significantly with increasing T. molitor protein concentrations. The backscattering values of EI0, EI20, and EI40 decreased evenly in all spots of the dispersions as the storage time increased. Thus, up to 40% of pork myofibrillar protein could be replaced with T. molitor protein in meat emulsion systems. The results also suggest that the interaction between edible insect protein and myofibrillar protein degrades the rheological properties and thermal stability of the meat emulsion systems.

Keywords: alternative protein; calorimetry; edible insect; food quality; viscosity.

Figure 1

Rheological properties (apparent viscosity (a), dynamic viscosity (b)) of emulsion prepared with the interaction between porcine myofibrillar protein and extracted edible insect protein. Porcine myofibrillar protein was substituted by edible insect protein at 0, 20, 40, 60, 80, and 100% (EI0, EI20, EI40, EI60, EI80, and EI100, respectively).

Figure 1

Rheological properties (apparent viscosity (a), dynamic viscosity (b)) of emulsion prepared with the interaction between porcine myofibrillar protein and extracted edible insect protein. Porcine myofibrillar protein was substituted by edible insect protein at 0, 20, 40, 60, 80, and 100% (EI0, EI20, EI40, EI60, EI80, and EI100, respectively).

Figure 2

Backscattering profiles of emulsion prepared with interaction between porcine myofibrillar protein and extracted edible insect protein: (a) EI0, (b) EI20, (c) EI40, (d) EI60, (e) EI80, and (f) EI100. Porcine myofibrillar protein was substituted by edible insect protein at 0, 20, 40, 60, 80, and 100% (EI0, EI20, EI40, EI60, EI80, and EI100, respectively).

Figure 2

Backscattering profiles of emulsion prepared with interaction between porcine myofibrillar protein and extracted edible insect protein: (a) EI0, (b) EI20, (c) EI40, (d) EI60, (e) EI80, and (f) EI100. Porcine myofibrillar protein was substituted by edible insect protein at 0, 20, 40, 60, 80, and 100% (EI0, EI20, EI40, EI60, EI80, and EI100, respectively).

Figure 2

Backscattering profiles of emulsion prepared with interaction between porcine myofibrillar protein and extracted edible insect protein: (a) EI0, (b) EI20, (c) EI40, (d) EI60, (e) EI80, and (f) EI100. Porcine myofibrillar protein was substituted by edible insect protein at 0, 20, 40, 60, 80, and 100% (EI0, EI20, EI40, EI60, EI80, and EI100, respectively).

Figure 3

Endothermic heat flow of emulsion prepared with the interaction between porcine myofibrillar protein and extracted edible insect protein. Porcine myofibrillar protein was substituted by edible insect protein at 0, 20, 40, 60, 80, and 100% (EI0, EI20, EI40, EI60, EI80, and EI100, respectively).

Figure 4

Molecular weight distribution of emulsion prepared with the interaction between porcine myofibrillar protein and extracted edible insect protein. Porcine myofibrillar protein was substituted by edible insect protein at 0, 20, 40, 60, 80, and 100% (EI0, EI20, EI40, EI60, EI80, and EI100, respectively).