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Carbohydrate is one kind of the most important additives in the production of surimi and surimi products, mainly due to its wide range of sources and superior functionality. In recent years, new carbohydrates (oligosaccharides and polysaccharides) have been gradually applied in the production of surimi and surimi products which is mainly driven by consumer requirement on nutritional and the flavors or taste quality and producer requirement on extending the shelf life, like low calorie intake, dietary fiber enrichment, rich taste and improvement of antioxidant properties. Besides anti-freezing and improvement in gelling ability, novel functionalities have been explored such as fat substitution, improving flavor, antibacterial effect, antioxidant effect and improving three-dimensional printability. With an in-depth study of the mechanism of carbohydrate improving the qualities of surimi and surimi products, the application of carbohydrates in surimi would be more effective. Therefore, this review summarizes the new carbohydrates applied in the processing of surimi and surimi products, and their novel functionalities. Additionally, progress of the research on the mechanism of carbohydrate improving the qualities of surimi is also reviewed. © 2023 Society of Chemical Industry.
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Antibacterianos , Antioxidantes , Géis/química , Carboidratos , Produtos Pesqueiros/análiseRESUMO
BACKGROUND: Conventional cryoprotectant mixtures (sucrose and sorbitol) impart excessive sweetness and calories to surimi. Therefore, there is a need to explore alternative cryoprotectants with low sweetness and low-calorie content. The cryoprotective effects and possible mechanisms of soybean oligosaccharides (SBOS) on the frozen stability of grass carp (Ctenopharyngodon idellus) surimi were investigated during 120 days of frozen storage in a comparison with commercial cryoprotectants (4% sucrose and 4% sorbitol, w/w). RESULTS: SBOS at 6-8% (w/w) and commercial cryoprotectants could restrain water mobility and reduce thawing loss of frozen surimi by increasing non-freezable water content. SBOS could maintain the structural stability of proteins by preventing sulfhydryl groups from being rapidly oxidized to disulfide bonds, retarding the reduction of the solubility, Ca2+-ATPase activity and α-helix content of myofibrillar proteins (MP), as well as hindering the increasing surface hydrophobicity of MP of surimi during 120 days of frozen storage. The introduction of SBOS increased the gel strength and water-holding capacity of frozen-stored surimi. Compared with commercial cryoprotectants, 8% SBOS was more effective in stabilizing protein structure, whereas it was slightly less effective with respect to ice-forming inhibition. CONCLUSION: The results obtained in the present study suggest that 8% SBOS could be potentially developed as a new cryoprotectant for surimi as a result of its ice-forming inhibition abilities and protein structure stability. © 2024 Society of Chemical Industry.
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Carpas , Crioprotetores , Armazenamento de Alimentos , Congelamento , Glycine max , Oligossacarídeos , Animais , Crioprotetores/química , Crioprotetores/farmacologia , Glycine max/química , Oligossacarídeos/química , Conservação de Alimentos/métodos , Produtos Pesqueiros/análise , Proteínas de Peixes/químicaRESUMO
BACKGROUND: The present study aimed to investigate the cryoprotective effect of epigallocatechin gallate (EGCG) replacing sucrose on surimi during frozen storage. Substitution or partial substitution of 0.1% EGCG for sucrose (1.5%) was added to surimi, and the surimi samples without and with commercial cryoprotectants (4% sucrose and 4% sorbitol) were used as the control group. RESULTS: The results obtained suggest that, with the increase in frozen storage time, the structural performance of surimi protein gradually weakened (e.g. the decrease in the surface hydrophobicity, the increase in the total sulfhydryl and solubility, and the protein myosin heavy chain bands became shallow) and surimi gel quality gradually deteriorated (e.g. the decrease in water-holding capacity, gel strength and all texture profile attributes). However, compared with the other three group surimi samples during the frozen period, the surimi proteins with partial replacement of sucrose by EGCG had a higher total sulfhydryl group content and solubility of proteins, as well as lower surface hydrophobicity of protein, suggesting that the addition of EGCG as a partial substitute for sucrose can enhance the antifreeze ability of surimi. Meanwhile, the surimi gel with the partial replacement of sucrose by EGCG had a higher water retention capacity, gel strength and texture attributes (e.g. hardness, springiness, cohesiveness, chewiness, and resilience), indicating that the addition of EGCG as a partial substitute for sucrose can inhibit the deterioration of surimi gel quality. CONCLUSION: Overall, EGCG partially replacing sucrose can play an alternative cryoprotectant with a lower sweetness to prevent the quality of surimi from deteriorating. © 2024 Society of Chemical Industry.
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Catequina , Crioprotetores , Produtos Pesqueiros , Conservação de Alimentos , Armazenamento de Alimentos , Congelamento , Sacarose , Crioprotetores/química , Crioprotetores/farmacologia , Catequina/análogos & derivados , Catequina/química , Animais , Produtos Pesqueiros/análise , Sacarose/química , Conservação de Alimentos/métodos , Interações Hidrofóbicas e Hidrofílicas , SolubilidadeRESUMO
BACKGROUND: Morden advanced analytical tools offer valuable information into the understanding of molecular mechanism of traditional food processing. Chopping temperature is well-known to affect the surimi gel quality of silver carp, but the detailed molecular mechanism is not very clear. In this study, a gel-based proteomics was performed on the extracted surimi proteins under different chopping temperatures (0, 5, 10, and 25 °C) along with other physicochemical characterization of surimi proteins and gels. RESULTS: With increased chopping temperature, protein extractability (in 3% sodium chloride) generally decreased, while the extracted protein generally exhibited larger surface hydrophobicity, reduced intrinsic fluorescence intensity, lower sulfhydryl content. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) profile of extracted protein showed a clear difference at 25 °C when compared with the other three temperatures, and more protein fragmentation occurred. Proteomic analysis of selected bands indicated that major myofibrillar proteins react differently with chopping temperatures, especially at 25 °C. The selected bands contained a variety of other proteins or their fragments, including adenosine triphosphate (ATP) synthase, glyceraldehyde-3-phosphate dehydrogenase, glucose-6-phosphate isomerase, heat shock protein, parvalbumin, collagen, and so forth. For the surimi gel, water-holding capacity and gel strength generally decreased with increased chopping temperature. CONCLUSION: Our results suggested that chopping at 0-10 °C is acceptable for the production of silver carp surimi in terms of gel strength and water-holding capacity. However, a chopping temperature near 0 °C led to less protein oxidation and denaturation. The inferior gel quality at 25 °C is linked to a decreased concentration of extracted protein and degradation of major myofibrillar protein, the latter is likely crosslinked with sarcoplasmic proteins. © 2024 Society of Chemical Industry.
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BACKGROUND: Hairtail (Trichiurus haumela) surimi exhibits poor gelation properties and a dark gray appearance, which hinder its utilization in high-quality surimi gel products. The effect of Pickering emulsions stabilized by myofibrillar proteins (MPE) on the gel properties of hairtail surimi has been unclear. In particular, the impact of MPE under NaCl and KCl treatments on the quality of hairtail surimi gels requires further elucidation. RESULTS: Pickering emulsions stabilized by myofibrillar proteins and treated with NaCl or KCl (Na-MPE, K-MPE) were added to hairtail surimi in amounts of 10-70 g kg-1. The addition of 50 g kg-1 Na-MPE and K-MPE improved the gel strength, textural properties, whiteness, and water-holding capacity (WHC) of hairtail surimi. The relative content of ß-turn and ß-sheet in the surimi gels increased and the relative content of random coils and α-helix decreased with the addition of oil. The addition of Na-MPE and K-MPE did not affect the secondary structure of surimi gels but stimulated the gelation of hairtail surimi gels. Hairtail surimi containing K-MPE demonstrated similar performance in terms of hardness, microstructure, and WHC compared with the addition of Na-MPE. CONCLUSION: The quality of hairtail surimi gels can be improved by the addition of Na-MPE or K-MPE. The K-MPE proved to be an effective option for enhancing the properties of hairtail surimi gels at 50 g kg-1 to replace Na-MPE. © 2024 Society of Chemical Industry.
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Proteínas de Peixes , Manipulação de Alimentos , Proteínas de Peixes/química , Emulsões , Cloreto de Sódio , Produtos Pesqueiros/análise , Géis/químicaRESUMO
BACKGROUND: Adding appropriate exogenous substances is an effective means to improve the quality of freshwater fish surimi. The present study investigated the effects of chicken breast on the gel properties of mixed minced meat products. RESULTS: With the increase in the proportion of chicken breast, the breaking force of mixed gels gradually increased. When the addition ratio was 30:70, the gel strength of mixed gels had the highest strength of 759.00 g cm-1 and also the highest water holding capacity of 87.36%. Compared with surimi gels (0:100), the hardness, adhesiveness and chewiness of mixed gels were significantly improved. The increase in the proportion of chicken breast increased the thermal stability of the mixed sol and improved the rheological properties of the mixed sol. When the proportion was 40:60, the area of immobile water (A22 ) in the mixed gel increased significantly, and the highest A22 was 3463.24. The hydrophobic interactions and disulfide bonds in the mixed gel were significantly increased as a result of the addition of chicken breast. The results of microstructure, electrophoresis and Raman spectroscopy indicated that the addition of chicken breast promoted the cross-linking of the proteins in mixed gels, which facilitated the transformation of the protein secondary structure from α-helical to ß-folded structure, thus forming a more uniform and orderly network structure. CONCLUSION: These results suggest that improving the gel properties of silver carp surimi by use of chicken breast has practical implications for the development of new blended products for surimi processing. © 2023 Society of Chemical Industry.
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Carpas , Proteínas de Peixes , Animais , Proteínas de Peixes/química , Galinhas , Manipulação de Alimentos/métodos , Géis/química , Água , Produtos Pesqueiros/análiseRESUMO
BACKGROUND: The present study aimed to investigate the effects of large yellow croaker roe phospholipids (LYCRPLs) on the physical properties of surimi gels and to clarify their interaction mechanism with myofibrillar proteins (MPs) in terms of chemical forces and the spatial conformation. RESULTS: LYCRPLs could improve the gel strength, textural properties, rheological properties and water-holding capacity of surimi gels. Moreover, the interaction mechanism between LYCRPLs with MPs was revealed through intermolecular forces, Fourier transform infrared spectroscopy and ultraviolet visible absorption spectroscopy. The findings demonstrated that LYCRPLs enhanced the surface hydrophobicity and particle size of MPs, facilitating expansion and cross-linking of MPs. CONCLUSION: These results provide a theoretical basis for improving the characteristics of surimi gels and thus facilitate the application of LYCRPLs in the aquatic food industry. © 2023 Society of Chemical Industry.
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Proteínas de Peixes , Perciformes , Animais , Proteínas de Peixes/química , Manipulação de Alimentos/métodos , Géis/química , Interações Hidrofóbicas e Hidrofílicas , Produtos Pesqueiros/análiseRESUMO
BACKGROUND: The gelation properties of surimi gel under various high temperatures (115, 118, and 121 °C) and sterilization intensities (F0 values of 3-7 min) were systematically investigated. A kinetic model detailed quality changes during heat treatment through mathematical analysis, elucidating mechanisms for gel quality degradation. RESULTS: Increased sterilization intensity significantly reduced the quality characteristics of surimi gel. Compared to the gel without sterilization treatment, when the sterilization intensity was increased to 7 min, the gel strength of the groups treated at 115 °C, 118 °C, and 121 °C decreased by 68.35%, 51.4%, and 51.71%, respectively, and the water-holding capacity decreased by 24.87%, 16.85%, and 22.5%, respectively. The hardness, chewiness, and whiteness of the gel also significantly decreased, and the changes in these indicators all conformed to a first-order kinetic model. Activation energy of 291.52 kJ mol-1 highlighted gel strength as the least heat-resistant. At equivalent sterilization intensities, 115 °C exhibited the poorest gel quality, followed by 121 °C, with 118 °C showing relatively better gel quality. Increased T22 and decreased PT22 suggested heightened water mobility and transition of immobilized water within the gel into free water. Protein degradation, weakened disulfide bonds and hydrophobic interaction, and protein conformation changes collectively led to a rough and incoherent gel network structure with large fissures, as verified by the results of scanning electron microscopy. Correlation analysis indicated potential for precise control over surimi gel quality by modulating physicochemical attributes. CONCLUSION: The outcomes may be beneficial to improve the production and quality control of ready-to-eat surimi-based products. © 2024 Society of Chemical Industry.
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BACKGROUND: Future applications of high-internal-phase emulsions (HIPEs) are highly regarded, but poor freeze-thaw stability limits their utilization in frozen products. This study aimed to characterize the structure of chickpea protein microgel particles (HCPI) induced by NaCl and to assess its impact on the freeze-thaw stability of HIPEs. RESULTS: The results showed that NaCl induction (0-400 mmol L-1) increased the surface hydrophobicity (175.9-278.9) and interfacial adsorbed protein content (84.9%-91.3%) of HCPI. HIPEs prepared with HCPI induced by high concentration of NaCl exhibited superior flocculation index and centrifugal stability, and their freeze-thaw stability was better than that of natural chickpea protein. The increase in NaCl concentration reduced the droplet aggregation and coalescence index of the freeze-thaw emulsions, diminishing the precipitation of oil from the emulsion. Linear and nonlinear rheology showed that the strengthened gel structure (higher G' values) restricted water flow and counteracted the damage to the interfacial film by ice crystals at 100-400 mmol L-1 NaCl, thus improving the viscoelasticity of the freeze-thaw emulsions. Finally, the thawing loss of surimi gel with HCPI-200 HIPE was reduced by 2.04% compared to directly adding oil. CONCLUSION: This study provided a promising strategy to improve the freeze-thaw stability of HIPEs and reduce the thawing loss of frozen products. © 2024 Society of Chemical Industry.
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BACKGROUND: Potentilla anserina L. is rich in various nutrients, active ingredients and unique flavor, comprising a natural nutrition and health food. However, its application in aquatic food has been rarely reported. Therefore, the effects of Potentilla anserina L. powder (PAP) on gel properties and volatile flavor profile of silver carp surimi were investigated. RESULTS: The gel strength and water-holding capacity of the surimi gels were significantly improved (P < 0.05), and the whiteness and cooking loss of all the samples decreased slightly with the increase in PAP content. The addition of PAP shortened the relaxation time (T2) of the surimi gels and converted some of the free water into immobile or bound water, which resulted in a better immobilization of water in the surimi. Scanning electron microscopy images demonstrated that the network of surimi gels with PAP added was denser and had a smoother surface compared to the control. Volatile components (VCs) analysis showed that 33 VCs were identified in the surimi gel samples with different additions of PAP, among which aldehydes, alcohols and esters were the major VCs, accounting for more than 50% of the VCs in the surimi gels. PAP addition reduced the fishy and rancid flavor compounds in surimi gels, such as 1-propanol, 1-octen-3-ol, etc., and promoted the production of aldehydes, alcohols, esters and other flavor substances. CONCLUSION: These results of the present study provide theoretical support for the investigation and development of new nutrient-health-flavored surimi products. © 2024 Society of Chemical Industry.
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Carpas , Produtos Pesqueiros , Aromatizantes , Géis , Potentilla , Paladar , Compostos Orgânicos Voláteis , Animais , Compostos Orgânicos Voláteis/química , Compostos Orgânicos Voláteis/análise , Produtos Pesqueiros/análise , Géis/química , Aromatizantes/química , Potentilla/química , Pós/química , Extratos Vegetais/química , Culinária , HumanosRESUMO
BACKGROUND: The rinsing process in the production of surimi can cause the loss of some important nutrients. To investigate the differences in nutritional properties between rinsed surimi (RS) and unrinsed surimi (US), this study compared the elemental composition, amino acid composition, fatty acid composition, proteomics, and an immunosuppression mouse model of surimi before and after rinsing, and analyzed the nutritional and immunological properties of RS and US. RESULTS: The results showed that the protein, fat, and ash contents of RS were decreased compared with those of US; specifically, the contents of essential amino acids, semi-essential amino acids, non-essential amino acids, saturated fatty acids, monounsaturated fatty acids, and polyunsaturated fatty acids were decreased. In the non-labeled quantitative proteomics analysis, three high-abundance quantifiable protein contents and 68 low-abundance quantifiable protein contents were found in RS (P-values < 0.05, ratio > 2). Immune function experiments in mice revealed that both RS and US contributed to the recovery of immunity in immunocompromised mice. The effect of US was better than that of RS. CONCLUSION: The rinsing process in surimi processing leads to the loss of nutrients in surimi. US promotes the recovery of immunity in immunocompromised mice more effectively than RS. © 2023 Society of Chemical Industry.
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Ácidos Graxos Insaturados , Peixes , Animais , Camundongos , Ácidos Graxos/análise , Proteínas , Aminoácidos , Nutrientes/análise , Ciclofosfamida , Géis/químicaRESUMO
BACKGROUND: Polysaccharides are the most widely used additives to enhance the quality of surimi gels. Oat ß-glucan (OG), a functional polysaccharide, is known to affect the gelation characteristics of surimi. However, it has been rarely reported. Therefore, the effect of OG at different levels on gelling properties, protein conformation, and microstructures of silver carp surimi gels were investigated. RESULTS: An increase in the OG content from 0 to 1.0% significantly improved the hardness, springiness, chewiness, puncture properties, storage modulus, and loss modulus of surimi gels. Moreover, the incorporation of OG (0-1.0%) facilitated the unfolding of proteins, resulting in the conformational transformation from α-helix to ß-sheet and ß-turn. Consequently, surimi-OG gels displayed a denser network structure with smaller and more uniform voids. Furthermore, partial free water in the gel network was converted into immobile water, increasing the water-holding capacity. However, a further increase in the OG concentration (1.0-2.0%) resulted in a looser and more uneven network structure with large and numerous cavities. In addition, the whiteness of composite gels decreased with increasing content of OG. CONCLUSION: The addition of 1.0% OG dramatically improved the gelation performance of silver carp surimi, providing a theoretical foundation for the exploitation and manufacture of functional surimi products. © 2023 Society of Chemical Industry.
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Carpas , Proteínas de Peixes , Animais , Proteínas de Peixes/química , Manipulação de Alimentos/métodos , Géis/química , Conformação Proteica , Água , Produtos Pesqueiros/análiseRESUMO
BACKGROUND: Epigallocatechin-3-gallate (EGCG) is well known for excellent chain-breaking antioxidant capability. However, browning by oxidation and aggregation of EGCG is a non-negligible defect that hinders its applications as an antioxidant in various foodstuffs. Therefore, how to eliminate or mitigate browning efficiently, while retaining functionalities as food additive is a challenge in the food industry. RESULTS: Our results demonstrated that EGCG could be anchored within the internal cavity of γ-cyclodextrin (γ-CD) to form an inclusion structure, where hydrophobic interaction, hydrogen bonding, and π-stacking were identified to be the primary drivers. The interplay between two molecules and the steric hindrance from γ-CD could restrict the motion and aggregation of EGCG efficiently, thus alleviating the browning effect. In addition, the conformational adaption of EGCG within the inclusions would result in general decreases in hydrogen-bond dissociation enthalpies for the pyrogallol-type structure on the b ring, thus enhancing the antioxidant capability. In practical application, the nanoscale γ-CD/EGCG inclusion complexes were validated preliminarily as efficient additives in the preservation of shrimp surimi, presenting significant effects on prolonging the shelf-life of products. CONCLUSION: Here, nanoscale γ-CD/EGCG inclusion complexes as alternatives to EGCG were tailored as food antioxidants for the preservation of shrimp surimi products, exerting antioxidant effects while mitigating the browning effects of EGCG on products. Through self-assembly, EGCG would be anchored with the cavity of γ-CD, which could regulate the release modes and restrict the aggregation of EGCG. This facile strategy has great potential in food preservation. © 2023 Society of Chemical Industry.
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Catequina , gama-Ciclodextrinas , Antioxidantes/química , Catequina/química , Conformação MolecularRESUMO
BACKGROUND: Frozen storage often leads to quality deterioration of surimi-based products. At present, most of the research focuses on improving the quality of surimi products by adding cryoprotectants, and there are few studies available on preparation technology. Therefore, the effects of different gelation-freezing treatments, high temperature heating-freezing treatment (HF), low temperature heating-high temperature heating-freezing treatment (LHF) and low temperature heating-freezing-high temperature heating treatment (LFH) on the quality changes of surimi gels containing hydroxypropyl distarch phosphate (HPDSP) during frozen storage were investigated. RESULTS: With the extension of frozen storage time, the quality of surimi gel in all groups decreased, but the quality of surimi gel with HPDSP was better than that of surimi gel without HPDSP. Compared with HF and LHF, the change range of breaking force, hardness, gumminess, whiteness and disulfide bond content of HPDSP-surimi gel treated with LFH was the least during the frozen storage. In the reheating process of LFH, HPDSP could absorb the water lost during freezing. Therefore, the change in the transverse relaxation time of HPDSP-surimi gels treated with LFH was smaller, with more immobile water and less free water and P22 of 96.81% and P23 of 0% at 16 weeks. In addition, the breaking deformation, cohesiveness, resilience, springiness and protein composition of surimi gels with and without HPDSP treated with HF, LHF and LFH did not change significantly during frozen storage. CONCLUSION: The combination of LFH and HPDSP could effectively reduce the quality change of surimi gel during frozen storage. © 2023 Society of Chemical Industry.
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Crioprotetores , Água , Congelamento , Crioprotetores/farmacologia , Géis/química , Produtos Pesqueiros/análise , Manipulação de Alimentos , Proteínas de Peixes/químicaRESUMO
BACKGROUND: This investigation focused on the use of mosambi peel extract (MPE) fortification (at 0% to 1.50%, w/w) in silver carp surimi to improve the gelling, textural, and other physicochemical properties of the surimi. RESULTS: The peels were extracted in ethanol (40-100% concentrations, v/v) and water. It was found that 100% ethanol had significantly (P < 0.05) higher yield and total phenolic, flavonoid, and tannin content. The fortification of MPE at optimum level (0.75%) improved the breaking force (55.1%) and gel strength (89.9%) significantly (P < 0.05) in comparison with 0% MPE gel samples. Moreover, 0.75% MPE-fortified gels had higher hydrogen and hydrophobic bonds, higher water-holding capacity, and lower sulfhydryl groups and free amino groups. The myosin heavy chain (MHC) bands in sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) disappeared completely in the MPE-fortified gels. Fortification with MPE affected the secondary structures of protein as shifting of peaks was observed in Fourier-transform infrared (FTIR) spectra. Scanning electron microscopy (SEM) images showed relatively organized finer and denser gel networks in MPE-treated gels. CONCLUSION: The surimi gels fortified with 0.75% MPE demonstrated improved gelling properties, with an overall higher acceptability than the unfortified gels (0% MPE). The fortified gels also became enriched with bioactive polyphenols, which are generally not present in surimi. This study provides an efficient way to utilize mosambi peel to develop functional surimi and surimi-based products with improved gel ability. © 2023 Society of Chemical Industry.
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Carpas , Citrus , Animais , Proteínas de Peixes/química , Produtos Pesqueiros/análise , Géis/química , Água , Etanol/análise , Manipulação de Alimentos/métodosRESUMO
BACKGROUND: Nano starch-lutein (NS-L) can be used in three-dimensional (3D) printed functional surimi. However, the lutein release and printing effect are not ideal. The purpose of this study was to facilitate the function and printing properties of surimi by adding the combination of calcium ion (Ca2+ ) and NS-L. RESULTS: Printing properties, lutein release and antioxidation of printed Ca2+ -NS-L-surimi were determined. The NS-L-surimi with 20 mM kg-1 Ca2+ had the best printing effects (fine accuracy, 99 ± 1%). Compared to NS-L-surimi, the structure became denser after adding Ca2+ , the gel strength, hardness, elasticity, yield stress (τ), water holding capacity of Ca2+ -NS-L-surimi increased by about 17 ± 4%, 3 ± 1%, 9 ± 2%, 20 ± 4%, 40 ± 5% respectively. These enhanced mechanical strength and self-supporting ability to resist binding deformation and improve printing accuracy. Moreover, salt dissolution and increased hydrophobic force by Ca2+ stimulated protein stretching and aggregation, leading to enhancement of gel formation. Decreased printing effects of NS-L-surimi with excessive Ca2+ (> 20 mM kg-1 ) caused by excessive gel strength and τ, leading to strong extrusion force and low extrudability. Additionally, Ca2+ -NS-L-surimi had higher digestibility and lutein release rate (increased from 55 ± 2% to 73 ± 3%), because Ca2+ made NS-L-surimi structure porous, which promoted contact of enzyme-protein. Furthermore, weakened ionic bonds reduced electron binding bondage that combined with released lutein to provide more electrons for enhancing antioxidation. CONCLUSION: Collectively, 20 mM kg-1 Ca2+ could better promote printing process and function exertion of NS-L-surimi, facilitating the application of 3D printed functional surimi. © 2023 Society of Chemical Industry.
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Antioxidantes , Manipulação de Alimentos , Manipulação de Alimentos/métodos , Luteína , Géis/química , Proteínas de Peixes/química , Amido/química , Impressão TridimensionalRESUMO
Globally, the Peruvian squid (Dosidicus gigas) has the highest productivity among squid species. However, due to its high-water content and astringent taste, it has limited fresh food value. This study used Peruvian squid meat as the primary material to prepare thin slices of dried squid meat paper mixed with pork. Here, different proportions (20, 40, 60, 80, and 100%, while 0% as the control group) of squid surimi have used to mix with pork for the meat paper preparation and the changes in physicochemical properties, microstructure, and sensory evaluation were analyzed. The results showed that the total volatile basic nitrogen (TVB-N) contents increased with the storage period, where 20% squid surimi substitution had the lowest TVB-N content. The 20% squid surimi substitution group had the highest expansion rate, the lowest peroxide value (PV), and moisture content. The food-borne microorganisms (E. coli, coliforms, and Salmonella spp.) were within the legal limits or negative. Hardness and crispiness, 20-40% squid surimi substitution were closely similar to the control group. This study has provided an effective investigation of the possibility of expanding the utilization of Peruvian squid resources by combining appropriate squid surimi with minced pork for high-quality thin slices of dried meat paper.
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Salt is a necessary condition to produce a surimi product that is based on the gelation of salt-soluble myofibrillar proteins. Recently, there has been a growing concern among consumers to consume healthy foods due to the threat of several chronic diseases caused by an unhealthy diet. Methods of reducing salt content out of concern for health issues caused by excessive sodium intake may affect the gel properties of surimi, as can many health-oriented food additives. Several studies have investigated different strategies to improve the health characteristics of surimi products without decreasing gel properties. This review reports recent developments in this area and how the gel properties were successfully maintained under reduced-salt conditions and the use of additives. This review of recent studies presents a great deal of progress made in the health benefits of surimi and can be used as a reference for further development in the surimi product processing industry.
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Produtos Pesqueiros , Manipulação de Alimentos , Manipulação de Alimentos/métodos , Géis , Aditivos Alimentares , Cloreto de Sódio , Cloreto de Sódio na Dieta , Proteínas de PeixesRESUMO
Heating is a vital step in the gelation of surimi. Conventional water bath heating (WB) has the advantages of easy operation and low equipment requirements. However, the slow heat penetration during WB may lead to poor gel formation or gels prone to deterioration, especially with one-step heating. The two-step WB is time-consuming, and a large amount of water used tends to cause environmental problems. This review focuses on key factors affecting the quality of surimi gels in various heating technologies, such as surimi protein structure, chemical forces, or the activity of endogenous enzymes. In addition, the relationships between these factors and the gel performance of surimi under various heating modes are discussed by analyzing the heating temperature and heating rate. Compared with WB, the gel performance can be improved by controlling the heating conditions of microwave heating and ohmic heating, which are mainly achieved by changing the molecular structure of myofibrillar proteins or the activity of endogenous enzymes in surimi. Nevertheless, the novel thermal technologies still face several limitations and further research is needed to realize large-scale industrial production. This review provides ideas and directions for developing heat-induced surimi products with excellent gel properties.
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BACKGROUND: Surimi is produced from the various sequences of filleting, deboning, washing, dehydrating, blending with cryprotectant, and freezing. Deboning, after which fish flesh is minced and separated from bone, skin, etc., is a vital step in the surimi production. In this study, effects of repeated deboning on yield, structure, composition, and gelling properties of silver carp surimi were investigated. RESULTS: Surimi yield increased rapidly from 10% to 23% as the cycle of repeated deboning was increased from one to three, and then slowly increased up to 26%. As the cycle increased, cellular structure and ultrastructure of muscle fibers progressively fractured. Contents of fat, cathepsins, heme proteins, and transglutaminase of surimi obviously increased and then decreased. Three-dimensional network of surimi gel without setting (NS gel) became more porous with the increase of cycles. It became more compact, and then turned to aggregated forms with lower homogeneity, for the surimi gel with setting (WS gel). Correspondently, the NS gel textural values gradually decreased with the cycles, while the WS gel textural values increased up to three cycles and then decreased. Regardless of setting, whiteness of surimi gels decreased and then increased with the cycles. CONCLUSION: Our results suggested that structure and compositions of surimi changed with the cycle of repeated deboning, which affected gelling properties of surimi. It is recommended to debone three or four cycles in silver carp surimi production. © 2022 Society of Chemical Industry.