Artificial meat offers a potential solution to consumer demand for meat, given global environmental concerns, public health problems, sustainability, and animal welfare problems. Although artificial ...meat may supplement or even replace traditional meat, it is still a challenge to reproduce muscle tissue's hierarchical structure.
This review focused on the research history of artificial meat, the current technological challenges and possible solutions, and analyzed consumer attitudes toward artificial meat.
Key findings and conclusions: With the rapid development of tissue engineering and bioreactor engineering, the new technologies for cultured meat have been continuously developed and improved. Extrusion, shear cell, and spinning are the main techniques for plant-based meat and its market has been expanding. Consumer attitudes toward cultured and plant-based meat vary by demographics and across cultures. There are some problems still needed to be overcome, including technology barriers and sensory, nutritional, health, and safety challenges in further developing the alternative meat market.
●The artificial meat market is expanding rapidly to meet consumer demands.●The technologies for artificial meat have been continuously developed and improved.●The sensory, nutritional, health, and safety of artificial meat remain hurdles.●Consumer attitude towards artificial meat varies across demographics and cultures.
The in-vitro digestive properties of myofibrillar protein (MP) in mirror carp (Cyprinus carpio L.) after freeze-thaw (F-T) cycles were analyzed in terms of the relationship between protein ...degradation, oxidation, and structural properties. The F-T samples exhibited a significant increase in glucosidase activity, N-acetyl-β-d-glucosidase activity, total protease activity, and non-protein nitrogen content. α-aminoadipate semialdehyde and γ-glutamate semialdehyde contents increased by 23.17% and 123.12%, respectively. Furthermore, 53.97% decrease in the total nitrogen content and changes in the content of different soluble proteins were observed. X-ray diffraction intensity, thermal stability, free amine content, hydrolysis degree, and digestibility of the MP samples decreased, and the 2θ angle and zeta potential were reversed. Besides, changes in the amide band wavenumbers were also detected. Therefore, the protein structure was unfolded and aggregates were formed through degradation and oxidation induced by the F-T cycles, ultimately making the in-vitro digestion of MP difficult.
The effects of ultrasound with different powers (0-500 W) on the structure and stability of protein from sea cucumber gonad were investigated, according to the changes in phenylalanine (Phe), ...α-helix, β-sheet, tryptophan (Trp), surface hydrophobicity, particle size distribution, microstructure and amino acid (AA). With the increase in ultrasound power, the contents of Phe, β-sheet and Trp, surface hydrophobicity and particle size first increased and then decreased, while α-helix content was opposite. Compared with the non-ultrasound group, the content of α-helix and random coil significantly decreased by 24.71% and 22.33% in the 200 W ultrasound group, while Phe content, β-sheet content, fluorescence intensity (FI), the surface hydrophobicity and hydrophobic AA significantly increased by 12.77%, 75.91%, 7.90%, 15.61% and 7.00%, respectively (P < 0.05). According to microstructure analysis, after 200 W ultrasound treatment, the protein particles became smaller and more uniform, and the protein structure was much looser than that without ultrasound treatment. Overall, the side chain, secondary, and tertiary structure of protein from sea cucumber gonad were unfolded under ultrasound treatment, which exposed more hydrophobic groups and decreased protein aggregation, and the effect of ultrasound with 200 W on the protein structure was prominent.
•The protein structure of sea cucumber gonad was unfolded during ultrasound process.•Effect of ultrasound treatment (200 W) on protein sturcture was significant.•Ultrasound treatment decreased the aggregation of sea cucumber gonad protein.•Particles of protein with 200 W ultrasound treatment became small and uniform.
The objective of this study was to evaluate the effect of ultrasound-assisted immersion freezing (UIF) on the freezing rate and quality of porcine longissimus muscles under different ultrasound ...powers. UIF with a certain level of ultrasound power significantly (P>0.05) accelerated the freezing rate. The phase transition times of samples treated with UIF at 180W (UIF-180) were the shortest. There were no significant differences (P>0.05) in a* (redness), b* (yellowness), pH values or cooking loss among UIF, IF, and control (fresh muscle) samples. Investigation of the microstructure of frozen muscles demonstrated that UIF-180 remarkably reduced the size of ice crystals and made their distribution more uniform. UIF-180 samples showed a significant (P<0.05) reduction in thawing loss and T21 and T22 relaxation times compared with other treatments, which meant that UIF at certain powers could reduce the mobility and loss of immobilized and free water. The results showed that UIF at certain powers significantly increased the freezing rate of muscle samples and improved meat quality.
•UIF at certain powers significantly increased the freezing rate of muscle chops.•Samples treated with 180W ultrasonic power had the least thawing loss.•The smallest ice crystals were formed in samples treated with UIF-180.•Ultrasonic power at 180W could significantly shorten the T2 relaxation time.•Using the appropriate ultrasonic power is beneficial for improving frozen meat quality.
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•Ultrasonic freezing (UF) retarded protein oxidation in frozen chicken breast.•The UF samples had higher protein thermal stability than the IF and AF samples.•The UF samples had lower ...surface hydrophobicity than the IF and AF samples.•UF retarded changes in protein structures during frozen storage.
The influence of ultrasound-assisted immersion freezing (UF), immersion freezing (IF), and air freezing (AF) on the protein oxidation, structure, and thermal stability of chicken breast during frozen storage was evaluated in this study. Compared to IF and AF samples, the UF samples had a lower carbonyl content, dityrosine content, and surface hydrophobicity of myofibrillar protein (MP) (P < 0.05), as well as a higher free amino group content and total and reactive sulfhydryl content (P < 0.05). Moreover, UF significantly delayed the deterioration of protein secondary and tertiary structures and the decrease in protein thermal stability during frozen storage (P < 0.05). Additionally, the UF samples at 180 days had similar protein structures and quality characteristics to the IF samples at 90 days or the AF samples at 60 days. Overall, UF treatment can effectively retard protein oxidation, protein structure deterioration, and protein thermal stability loss caused by frozen storage.
The change in quality of quick-frozen patties containing different amounts of added fat (0%, 5%, 10%, 15%, and 20%) under different freeze-thaw (F-T) cycles (a F-T cycle was performed by freezing at ...−18 °C and thawing at 4 °C) was evaluated. The results showed that the a*-values of samples were significantly decreased, while L*-values, b*-values, thawing loss, and cooking loss were notably increased after 3 F-T cycles. Low-field nuclear magnetic resonance (LF-NMR) results showed that the water mobility of patties was enhanced. Textural properties (hardness, springiness, cohesiveness, and chewiness) of patties were significantly decreased after 5 F-T cycles (P < 0.05). Lipid and protein oxidation were aggravated with increasing fat content and number of F-T cycles, as confirmed by the increase in lipid peroxides, TBARS, and carbonyl content. Therefore, the results from instrument-based detection and consumer scores indicated that repeated F-T cycles accelerated the quality deterioration of quick-frozen pork patties, and rendered them unacceptable after 3 F-T cycles.
•Freeze-thawing (F-T) cycle induced quality decrease of quick-frozen pork patty.•Positive correlation between fat content and quality decrease of patty during F-T storage.•Increase in peroxide value, TBARS and carbonyl confirmed lipid and protein oxidation during F-T cycles.
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•Ultrasound-assisted immersion freezing reduced the changes in the MP structure.•UF-165 reduced the losses of the elastic modulus (G′), gel strength, and WHC.•UF-165 samples had less ...mobility and losses of immobilized water and free water.•The appropriate power promoted the formation of a homogeneous MP gel network.
The effects of air freezing (AF), immersion freezing (IF) and ultrasound-assisted immersion freezing (UF) at different power levels (125, 165, 205 and 245 W) on the structure and gel properties of the myofibrillar protein (MP) of chicken breast were investigated. UF at 165 W (UF-165) had no obvious negative impact on the primary structure of the MP and effectively reduced the change in the secondary and tertiary structure. In addition, UF-165 significantly reduced the losses in the elastic modulus (G′), gel strength, and gel water holding capacity (P < 0.05). According to low field nuclear magnetic resonance analysis, the T21 and T22 of the UF-165 MP gels were shorter than those of the AF and IF samples, which meant that the UF-165 reduced the mobility of the immobilized water and free water in MP gel. A scanning electron microscopy analysis showed that the appropriate ultrasonic power promoted the formation of a compact and homogeneous protein gel network. These results suggested that the appropriate ultrasonic power maintained the MP structure and reduced the loss of gel quality.
•Effect of three new thawing methods on gel property of protein was analyzed.•Change in MP gel surface morphology was observed by atomic force microscopy.•Effect of ultrasound and vacuum thawing on ...gel property was lower than others.•Destruction in gel property of microwave thawing was obvious.
Effect of new thawing methods (ultrasound thawing (UT), vacuum thawing, (VT), microwave thawing (MT)) on gelling properties of myofibrillar protein (MP) from porcine longissimus dorsi was investigated, compared with traditional thawing methods (water immersion thawing, (WT)) and fresh meat (FM). The results showed that a decrease in MP gelling properties of all thawing samples was observed. The increase in roughness of MP gel from all thawing samples explained that the flatter, smoother, and denser surface morphology of that from FM samples was destroyed based on the observation by atomic force microscopy. There was significant difference (P < 0.05) in all gel indicators (particle size, turbidity, whiteness, water-holding capacity (WHC), moisture distribution, rheological characteristics, surface morphology) of MP from MT samples and there was insignificant difference (P > 0.05) in turbidity, whiteness, WHC of MP from VT samples compared with that from FM samples. There was insignificant difference (P > 0.05) in gel properties between UT and VT. The effect of UT and VT (new thawing methods) on MP gelling properties was significantly lower (P < 0.05) than that of WT (traditional thawing methods), and the effect of that from MT was obviously compared with other thawing methods.
Ultrasound‐assisted freezing (UF) has proven to be a method that can effectively increase the freezing rate of frozen food and improve its quality. The functional properties of myofibrillar proteins ...(MP) are important factors that affect the further processing quality of meat products. At present, the effect of UF on the functional properties of frozen MP is not yet clear. Therefore, in the present study, changes in the functional properties (emulsifying and gel properties) of MP in common carps (Cyprinus carpio) frozen with UF at different power levels were investigated. The results revealed that, compared with immersion freezing (IF), UF at 175 W (UF‐175) effectively inhibited the decrease in protein solubility, absolute Zeta potential, emulsion activity index, storage modulus (G'), and loss modulus (G'') caused by freezing. UF‐175 sample had lower protein turbidity, and smaller protein particle size than any other frozen samples (P < 0.05), which suggested that UF‐175 inhibited protein aggregation induced by freezing. In addition, shorter T21 and T22 relaxation times were obtained in UF‐175 sample than other frozen samples, indicating that UF‐175 reduced the mobility of immobilized and free water. Accordingly, UF‐175 sample had higher gel strength and water holding capacity than other frozen samples (P < 0.05). A denser and more uniform gel network structure was also found in UF‐175 sample than other frozen samples. In general, improved functional properties of common carp MP can be achieved by optimal UF.
This study evaluated the effect of ultrasound-assisted immersion freezing (UIF) on the freezing speed and quality of common carp (Cyprinus carpio) at different ultrasonic power levels. The results ...revealed that UIF increased the speed of freezing, with UIF at 175 W (UIF-175) being optimal. Compared to refrigerator freezing and immersion freezing, UIF samples had less thawing and cooking loss. Microstructural observation showed that UIF-175 reduced pore diameter and ice crystal size. As ultrasonic power increased, the L*-value first decreased and then increased (P < 0.05), and there were no significant differences in a*- or b*-values (P > 0.05). UIF-175 samples exhibited the shortest T21 and T22 relaxation time, which indicated that this appropriate ultrasonic power level reduced the mobility of free and immobilized water. Therefore, UIF at appropriate ultrasonic power significantly decreased the freezing time of fish samples and improved the fish meat quality.
•Ultrasound immersion freezing (UIF) accelerated fish freezing.•Ultrasonic power at 175 W markedly reduced thawing and cooking loss.•Fish samples treated with UIF-175 had smaller ice crystals.•Freezing under UIF-175 reduced the mobility and loss of immobilized and free water.
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