Research progress on quality deterioration mechanism and control technology of frozen muscle foods

Abstract

Freezing can prolong the shelf life of muscle foods and is widely used in their preservation. However, inevitable quality deterioration can occur during freezing, frozen storage, and thawing. This review explores the eating quality deterioration characteristics (color, water holding capacity, tenderness, and flavor) and mechanisms (irregular ice crystals, oxidation, and hydrolysis of lipids and proteins) of frozen muscle foods. It also summarizes and classifies the novel physical-field-assisted-freezing technologies (high-pressure, ultrasound, and electromagnetic) and bioactive antifreeze (ice nucleation proteins, antifreeze proteins, natural deep eutectic solvents, carbohydrate, polyphenol, phosphate, and protein hydrolysates), regulating the dynamic process from water to ice. Moreover, some novel thermal and nonthermal thawing technologies to resolve the loss of water and nutrients caused by traditional thawing methods were also reviewed. We concluded that the physical damage caused by ice crystals was the primary reason for the deterioration in eating quality, and these novel techniques promoted the eating quality of frozen muscle foods under proper conditions, including appropriate parameters (power, time, and intermittent mode mentioned in ultrasound-assisted techniques; pressure involved in high-pressure-assisted techniques; and field strength involved in electromagnetic-assisted techniques) and the amounts of bioactive antifreeze. To obtain better quality frozen muscle foods, more efficient technologies and substances must be developed. The synergy of novel freezing/thawing technology may be more effective than individual applications. This knowledge may help improve the eating quality of frozen muscle foods.

Effect of Potato Dietary Fiber on the Quality, Microstructure, and Thermal Stability of Chicken Patty

“…The moisture migration of the chicken patty is characterized by T 2 b , T 21 , and T 22, and P 2 b , P 21 , and P 22 using low-field nuclear magnetic resonance (LF-NMR), a fast, non-destructive technique [ 26 , 27 ]. The changes in T 2 b , T 21 , and T 22 , and P 2 b , P 21 , and P 22 of the chicken patty with different PDF content are presented in Table 1 .…”

Physicochemical and structural changes of myofibrillar proteins in muscle foods during thawing: Occurrence, consequences, evidence, and implications

“…On the one hand, the physicochemical and structural properties of MPs can be dramatically altered by oxidative modification during thawing, with the representative result of increasing the net charge of MPs and forming cross‐linked protein aggregates (Ling et al., 2021; Zhang et al., 2017b). The elevated net charge can promote the swelling of myofibrils and compress the interfilamental spaces (Du et al., 2022). Although shrinkage of the interfilamental spaces expands the extracellular space, it weakens its capillary force to retain water (Wang et al., 2021b).…”

Research Progress on the Preparation and Action Mechanism of Natural Deep Eutectic Solvents and Their Application in Food

“…This is due to the fact that NADES is formed by the combination of HBAs and HBDs through hydrogen bonds. The charge delocalization effect in the hydrogen bond network system will lead to the FP decrease in NADES [ 30 ]. Numerous hydrogen bonds in the system provide supramolecular network structure for NADES, which significantly increases the viscosity of NADES [ 6 ].…”