Gel properties of blue round scad (Decapterus maruadsi) mince as influenced by the addition of egg white powder

Abstract

The use of egg white powder (EWP) to enhance the physicochemical properties, molecular structure, and thermal stability of Decapterus maruadsi mince gels was investigated. The thermal stability was analyzed by adding spray‐dried EWP (0, 0.2, 0.4, 0.6, 0.8, and 1%) to the mince, and mince gels were prepared to study the changes in their fracture constant, water distribution, microstructure, and protein conformation of mince gels. In addition, the stress–strain curve of the EWP‐mince gel was measured to obtain its compressive modulus (E). The formation of the mince gel was promoted by EWP, and the whiteness, fracture constant, water‐holding capacity (WHC), and immobilized water were all enhanced. At 0.8% addition of EWP, the fracture constant increased from 176.715 ± 2.463 N/m to 348.631 ± 3.144 N/m (p < .05), which was a nearly twofold improvement. Additionally, the WHC increased from 75.21% to 79.99%, and the percentage of immobilized water increased from 94.03% to 94.91%. The EWP‐mince gel network structure was the most uniform and dense, and there were increases in hydrogen bonds, disulfide bonds, β‐sheets, and β‐turns in mince gels, as well as the storage modulus (G′) and enthalpy (ΔH). In contrast to the control group, the relative content of α‐helixes decreased from 53.34% to 37.09% and transformed into other secondary structures, and the bulk water and cooking loss also decreased to 2.41% and 8.51%, respectively. Consequently, EWP effectively improved the quality of mince products, and the effect was most apparent when 0.8% was added.

Minced Beef Meat Paste Characteristics: Gel Properties, Water Distribution, and Microstructures Regulated by Medium Molecular Mass of γ-Poly-Glutamic Acid

“…All samples displayed four characteristic peaks: T2b1 (~0-1 ms); T2b2 (~1-10 ms); T21 (~10-150 ms); and T22 (~150-1000 ms), which were related to the three types of water molecules (Figure 5a). They represented strongly and weakly bound water (tightly bound to macromolecules by molecular forces), immobile water (retained within the protein gel network structure), and free water (present outside the gel network) in correlation with the meat gel relaxation times observed by Wu et al [33]. T2 relaxation time reflects the fluidity of water.…”

“…The WHC of the meat gel was estimated by centrifugation [33]. The cooked gel samples were sliced into sections of approximately 5 mm thickness and weighed precisely to record the mass as M 1 .…”

“…The decrease in T 2b2 indicated weaker water mobility and a lower migration rate. The reason may be that the formation of aggregates by m-γ-PGA with proteins provides more water molecule binding sites, which improves the capacity of proteins to combine with water [33]. As the dosage of m-γ-PGA was raised to 0.16%, T 2b2 began to increase.…”