Effects of the Mixture of Xylooligosaccharides and Egg White Protein on the Physicochemical Properties, Conformation, and Gel-Forming Ability of Culter alburnus Myofibrillar Protein during Multiple Freeze–Thaw Cycles

Abstract

This study focuses on the effect of the mixture (XO/EW) of xylooligosaccharides (XO) and egg white protein (EW) on the physicochemical properties, conformation, and gel-forming ability of Culter alburnus myofibrillar proteins (MP) during multiple freeze–thaw (FT) cycles. In our methodology, MP samples added with EW, XO, or XO/EW mixture (1%, v/v) are prepared, and after multiple FT cycles, the XO or XO/EW-treated samples show significant (p < 0.05) inhibition on the decrease of sulfhydryl content and the increase of carbonyl content of MP. Compared with EW, XO or XO/EW could delay the increase of surface hydrophobicity and the decline of secondary and tertiary structural properties of MP, indicating that XO or XO/EW could more effectively increase the stability of MP conformation. Meanwhile, XO/EW could more effectively reduce the decrease of gel strength and gel water holding capacity, and the increase in the T2 relaxation time of MP gel, confirming that XO/EW could substantially improve the MP gel-forming ability. Analysis of intermolecular interaction force proves that, compared with EW, XO/EW could reduce the content decrease of ionic and hydrogen bonds in MP gel. Overall, XO/EW could improve the stability of MP functional properties over multiple FT cycles. This study provides a new perspective for the potential commercial application of EW as a low-calorie cryoprotectant in aquatic products.

Complex organic acids treatment on crayfish (Procambarus clarkii): the relationship between myofibrillar protein structure and meat quality

“…Consistent with previous studies, the low pH environment induced higher levels of β‐sheet content (Lu et al ., 2022). It has also been shown that MP oxidation can also transform ordered α‐helical structures into loose β‐sheets (Zhang et al ., 2021).…”

Control on moisture distribution and protein changes of Antarctic krill meat by antifreeze protein during multiple freeze–thaw cycles

“…As shown in Figure 6a, the content of ionic bonds decreased from 4.61 mg/ml to 4.05 mg/ml in the control group and from 3.99 mg/ml to 2.80 mg/ml in the 0.1% AFP group after F–T cycles ( p < 0.05), which may be due to F–T cycles that disrupt the tertiary structure of Antarctic krill meat proteins (D. Zhang et al., 2020). Moreover, the ice crystals growth during F–T cycles changes the chemical groups of proteins, which affects the surface charge distribution and leads to irregular aggregation of proteins, resulting in a lower ionic bonding content (Zhang, Xiong, et al., 2021). The ionic bond content of the control group was higher than that of the 0.1% AFP group in the first F–T cycle ( p < 0.01) and seventh F–T cycle ( p < 0.05).…”

Thermal aggregation behavior of egg white protein and blue round scad (Decapterus maruadsi) myofibrillar protein

“…Previous studies have mainly discussed the improvement of EWP on the gel strength and freezing denaturation of MP, including EWP mixed with low temperature protectant (xylooligosaccharides or β‐cyclodextrin) to form an effective cryoprotectant and slow down the oxidation of MP during freezing storage or repeated freezing and thawing (Walayat et al., 2021; Zhang et al., 2021). However, the degree of aggregation and the interaction mechanism of the EWP and MP mixed continuous phases have not been investigated, especially the effect of the heat treatment mode on the protein conformation of the mixed continuous phase.…”