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BACKGROUND: The cryoprotective effect of xylooligosaccharide (XO) and kappa-carrageenan (KC) mixture on silver carp proteins in fluctuated frozen storage from 4 to -18 °C was analyzed. Positive control as a conventional cryoprotectant mixture of sucrose (4%) and sorbitol (4%), KC (3%) and XO/KC (3%) treatments were incorporated in silver carp surimi and myofibrillar proteins to analyze the water mobility and its influence on structural attributes. RESULTS: The temperature fluctuation significantly increased the structural alteration in samples with no treatments due to oxidative changes, protein denaturation and recrystallization. Meanwhile, the mixture of XO and KC (XO/KC 3%) significantly reduced the tertiary and secondary structural alterations by preventing the oxidative changes in α-helix and tryptophan (Trp) residues. Moreover, XO/KC (3%) inhibited water mobility, hindering the T22 relaxation time, as compared to the samples added with KC (3%) and the positive control. Interestingly, the XO/KC (3%) mixture significantly reduced the formation of extracellular spaces and recrystallization by restricting the partial dehydration of muscles and extracellular solution concentration. CONCLUSION: From the current results, it can be concluded that the XO/KC mixture could be efficient in protecting aquatic food proteins during fluctuating frozen storage by preventing the exposure of Trp residues and α-helix contents. Moreover, XO/KC restricted the water mobility by establishing a bond and making water unavailable for crystallization and recrystallization. Therefore, XO/KC could be used as an effective mixture to prevent fluctuated and frozen storage changes in aquatic foods. © 2024 Society of Chemical Industry.
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We hypothesized that removing water from fish muscle homogenate by freeze-drying might be a cost-effective way to stabilize nutrients and allow higher temperatures for long-term frozen storage prior to analytical measurements. To test our hypothesis, fish muscle fillets from lipid-rich farmed Atlantic salmon (n = 5) and lean wild-caught European plaice (n = 5) were homogenized and fresh-frozen at -20 and -80°C. A subset of these samples was freeze-dried prior to further frozen storage at the respective temperatures. Using validated methods, vitamins, amino acids, and fatty acids were measured after a short time of storage (starting point) and up to 1 year (endpoint), with intermediate analytical checkpoints of 1, 3, and 6 months. Trends in the degradation of certain nutrients during the different frozen storage conditions are discussed. In general, by freeze-drying fish homogenate samples prior to frozen storage at -20°C for up to 1 year, amino acids, vitamins, and fatty acids were stabilized in both salmon and plaice when compared to wet-frozen storage of the same samples, and storage at -80°C did not improve preservation of the freeze-dried samples. For wet-frozen samples, -80°C would be recommended for 1-year storage of fillet homogenate samples, even though several nutrients preserved well at -20°C. PRACTICAL APPLICATION: We present individual nutrient stability profiles in muscle homogenates from fatty fish (salmon) and lean fish (plaice) during different frozen storage conditions over time. Based on these data, freeze-drying followed by frozen storage at -20°C for at least 1 year could be applied prior to analyses of amino acids, fat-soluble vitamins, water-soluble vitamins, and fatty acids. Of note is that freeze-drying followed by frozen storage before analysis led to slightly increased measurements of several fatty acids in plaice samples, possibly attributable to an increase in dry weight or an enhancement in extraction efficiency through freeze-drying.
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Aminoácidos , Ácidos Grasos , Almacenamiento de Alimentos , Liofilización , Congelación , Salmo salar , Alimentos Marinos , Animales , Aminoácidos/análisis , Liofilización/métodos , Almacenamiento de Alimentos/métodos , Alimentos Marinos/análisis , Ácidos Grasos/análisis , Conservación de Alimentos/métodos , Vitaminas/análisis , Salmón , Valor Nutritivo , Nutrientes/análisisRESUMEN
The purpose of this study was to clarify effects of water changes on the quality and volatile compounds of Penaeus monodon during frozen storage. The content of immobilized water decreased significantly while the bound water and free water increased significantly. Total sulfhydryl content, and Ca2+-ATPase activity decreased significantly to 68.31 µmol/g and 0.127 U/mg, meantime, carbonyl content and MFI value increased significantly to 2.04 µmol/g prot and 55.10. Total of 50 volatile compounds were identified. Nonanal (M & D), 2-nonanone and octanal were only detected in fresh samples, while 3-hydroxy-2-butanone and 1-hydroxy-2-propanone were only found in the samples after 20 days of storage. Correlation analysis revealed that 6 of the volatile compounds were associated with the change of free water. Total of 28 and 17 volatile compounds showed significant correlations with the immobilized water and bound water, respectively. Four volatile compounds have the potential to be used as the flavor marker.
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Congelación , Penaeidae , Compuestos Orgánicos Volátiles , Agua , Animales , Compuestos Orgánicos Volátiles/química , Compuestos Orgánicos Volátiles/análisis , Agua/análisis , Agua/química , Penaeidae/química , Penaeidae/metabolismo , Almacenamiento de AlimentosRESUMEN
Whitespotted conger (Conger myriaster) muscle proteins were susceptible to oxidative denaturation during frozen storage. The objective of this study was to investigate the alterations in quality through physicochemical analysis and proteomics after whitespotted conger stored at temperatures of -18 °C and -60 °C. The microstructural observation revealed the noticeable variations such as increased interstitial space and fractured muscle fibre with extension of frozen storage time, and the muscle fibre of whitespotted conger stored at -60 °C were more intact than those stored at -18 °C. The raised TVB-N value indicated that the freshness of whitespotted conger decreased during 120-day frozen storage period. Analysis of myofibrillar protein content and SDS-PAGE demonstrated that compared to -18 °C, lower storage temperature (-60 °C) could better maintain the structure of whitespotted conger muscle by inhibiting protein degradation and oxidation. To reveal the mechanism of protein degradation, label-free quantitative proteomic analysis was performed through LC-MS/MS. The structural proteins including domain-associated proteins and actin-related proteins were up-regulated during frozen storage, but the phosphoglycerate kinase, phosphoglycerate mutase, and fructose-bisphosphate aldolase were down-regulated. Storage at -18 °C accelerated the up- or down-regulation of those differentially abundant proteins. According to KEGG analysis, up- or down-regulated pathways such as glycolysis/gluconeogenesis, carbon metabolism, biosynthesis of amino acids, and calcium signalling pathway mainly accounted for the protein degradation and quality reduction of whitespotted conger at low temperature. These results provided a theoretical basis for improving the quality stability of whitespotted conger during frozen storage.
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In this study, large yellow croaker (Larimichthys crocea) was frozen using multi-frequency ultrasound-assisted freezing (MUIF) with different powers (160 W, 175 W, and 190 W, respectively) and stored at -18 °C for ten months. The effect of different ultrasound powers on the myofibrillar protein (MP) structures and lipid oxidation of large yellow croaker was investigated. The results showed that MUIF significantly slowed down the oxidation of MP by inhibiting carbonyl formation and maintaining high sulfhydryl contents. These treatments also held a high activity of Ca2+-ATPase in the MP. MUIF maintained a higher ratio of α-helix to ß-sheet during frozen storage, thereby protecting the secondary structure of the tissue and stabilizing the tertiary structure. In addition, MUIF inhibited the production of thiobarbituric acid reactive substances value and the loss of unsaturated fatty acid content, indicating that MUIF could better inhibit lipid oxidation of large yellow croaker during long-time frozen storage.
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Congelación , Oxidación-Reducción , Perciformes , Animales , Factores de Tiempo , Almacenamiento de Alimentos , Proteínas Musculares/química , Proteínas Musculares/metabolismo , Ondas Ultrasónicas , ATPasas Transportadoras de Calcio/metabolismoRESUMEN
Freezing of biological drug substance (DS) is a critical unit operation that may impact product quality, potentially leading to protein aggregation and sub-visible particle formation. Cryo-concentration has been identified as a critical parameter to impact protein stability during freezing and should therefore be minimized. The macroscopic cryo-concentration, in the following only referred to as cryo-concentration, is majorly influenced by the freezing rate, which is in turn impacted by product independent process parameters such as the DS container, its size and fill level, and the freezing equipment. (At-scale) process characterization studies are crucial to understand and optimize freezing processes. However, evaluating cryo-concentration requires sampling of the frozen bulk, which is typically performed by cutting the ice block into pieces for subsequent analysis. Also, the large amount of product requirement for these studies is a major limitation. In this study, we report the development of a simple methodology for experimental characterization of frozen DS in bottles at relevant scale using a surrogate solution. The novel ice core sampling technique identifies the axial ice core in the center to be indicative for cryo-concentration, which was measured by osmolality, and concentrations of histidine and polysorbate 80 (PS80), whereas osmolality revealed to be a sensitive read-out. Finally, we exemplify the suitability of the method to study cryo-concentration in DS bottles by comparing cryo-concentrations from different freezing protocols (-80°C vs -40°C). Prolonged stress times during freezing correlated to a higher extent of cryo-concentration quantified by osmolality in the axial center of a 2 L DS bottle.
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Embalaje de Medicamentos , Congelación , Hielo , Embalaje de Medicamentos/métodos , Concentración Osmolar , Polisorbatos/química , Histidina/química , Productos Biológicos/químicaRESUMEN
This work investigated the cryoprotective effect of trehalose (TH) and sodium pyrophosphate (SPP) alone and in combination on myofibrillar protein (MP) oxidation and structural changes in silver carp surimi during 90 days of frozen storage (-20 °C). TH combined with SPP was significantly more effective than single TH or SPP in preventing MP oxidation (P < 0.05), showing a higher SH content (6.05 nmol/mg protein), and a lower carbonyl (4.24 nmol/mg protein) and dityrosine content (1280 A.U.). SDS-PAGE results indicated that TH combined with SPP did not differ significantly from TH and SPP in inhibiting protein degradation but was more effective in inhibiting protein crosslinking. Moreover, all cryoprotectants could stabilise the secondary and tertiary structures and inhibit unfolded and aggregation of MP, with the combination of TH and SPP being the best. It's worth noting that TH combined with SPP had a synergistic effect on inhibiting the decrease in α-helix content and gel-forming ability, and the increase in surface hydrophobicity. Overall, TH combined with SPP could significantly inhibited MP oxidation and structural changes in surimi during frozen storage and improve the gel-forming ability, which was significantly better than single TH or SPP.
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Carpas , Crioprotectores , Difosfatos , Almacenamiento de Alimentos , Congelación , Proteínas Musculares , Oxidación-Reducción , Trehalosa , Animales , Trehalosa/química , Almacenamiento de Alimentos/métodos , Difosfatos/química , Proteínas Musculares/química , Crioprotectores/química , Crioprotectores/farmacología , Proteínas de Peces/química , Conservación de Alimentos/métodos , Productos Pesqueros/análisis , Miofibrillas/químicaRESUMEN
To inhibit the quality deterioration caused by the frozen storage of surimi products, this work investigated the effect of freezing methods, including raw-freezing-setting-heating, raw-setting-freezing-heating, and raw-setting-heating-freezing, on quality changes in surimi gel. The moisture loss, physical-chemical properties, and protein structure conformation of surimi gel derived from Bombay duck (BD) were assessed following frozen storage periods of 20, 40, and 60 days. The findings suggest that the raw-setting-heating-freezing method yielded optimal surimi gel properties with extended frozen storage time. Employing this approach led to a reduction in thawing loss, while cooking loss remained constant. After 60 days of frozen storage, the hardness exhibited an initial increase followed by a subsequent decrease, and water-holding capacity increased to 68.2%. Notably, the impact on surimi gel during the late stage of frozen storage was more pronounced throughout the formation of ice crystals, resulting in decreased disulfide bond content. Scanning hematoxylin-eosin (HE) staining slices of samples following thawing and heating demonstrated that the raw-setting-heating-freezing method could better resist the effect of ice crystals in frozen storage period on surimi tissue, while the gel on setting process could delay the erosion imposed on by ice crystals during frozen storage. This study provides a scientific foundation for the industrialization on frozen BD surimi products.
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Patos , Hielo , Animales , Congelación , Peces , CulinariaRESUMEN
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 , Crioprotectores , Almacenamiento de Alimentos , Congelación , Glycine max , Oligosacáridos , Animales , Crioprotectores/química , Crioprotectores/farmacología , Glycine max/química , Oligosacáridos/química , Conservación de Alimentos/métodos , Productos Pesqueros/análisis , Proteínas de Peces/químicaRESUMEN
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 , Crioprotectores , Productos Pesqueros , Conservación de Alimentos , Almacenamiento de Alimentos , Congelación , Sacarosa , Crioprotectores/química , Crioprotectores/farmacología , Catequina/análogos & derivados , Catequina/química , Animales , Productos Pesqueros/análisis , Sacarosa/química , Conservación de Alimentos/métodos , Interacciones Hidrofóbicas e Hidrofílicas , SolubilidadRESUMEN
The effect of ultrasound-assisted immersion freezing (UIF), air freezing (AF), and immersion freezing (IF) on the protein structure, aggregation, and emulsifying properties of common carp (Cyprinus carpio) myofibrillar protein during frozen storage were evaluated in the present study. The result showed that, compared with AF and IF samples, UIF sample had higher reactive/total sulfhydryl, protein solubility, and lower protein turbidity (Pâ¯<â¯0.05), indicating that UIF was beneficial to inhibit protein oxidation and aggregation induced by frozen storage. UIF inhibited the alteration of secondary structure and tertiary structure during frozen storage. Meanwhile, UIF sample had higher emulsifying activity index, and smaller emulsion droplet diameter than AF and IF samples (Pâ¯<â¯0.05), suggesting that UIF was beneficial for maintaining the emulsifying properties of protein during storage. In general, UIF is a potential and effective method to suppress the decrease in protein emulsifying properties during long-term frozen storage.
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Carpas , Animales , Congelación , Carpas/metabolismo , Agregado de Proteínas , Proteínas Musculares/química , Proteínas de Peces/químicaRESUMEN
Salting pretreatment is an effective method to improve the quality of frozen fish. This study investigated the quality changes and proteomic profile differences of frozen yellowfin tuna fillets pretreated with ultrasound-assisted salting (UAS) and static salting (SS). This study was centered on three aspects: physicochemical indicators' determination, histological observation, and proteomic analysis. The results showed that UAS significantly increased yield, salt content, and water-holding capacity (WHC), decreased total volatile base nitrogen (TVBN) compared to SS (p < 0.05), and significantly increased water in the protein matrix within myofibrils. Histological observations showed that the tissue cells in the UAS group were less affected by frozen damage, with a more swollen structure and rougher surface of myofibrils observed. Furthermore, 4D label-free proteomics revealed 56 differentially abundant proteins (DAPs) in UAS vs. NT comparison, mainly structural proteins, metabolic enzymes, proteasomes, and their subunits, which are associated with metabolic pathways such as calcium signaling pathway, gap junction, actin cytoskeletal regulation, and necroptosis, which are intimately associated with quality changes in freeze-stored tuna fillets. In brief, UAS enhances the potential for the application of salting pretreatment to improve frozen meat quality, and 4D label-free proteomics provides knowledge to reveal the potential links between quality and molecular changes in processed frozen meat to optimize future UAS meat processing.
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The physicochemical indexes and microbial diversity were investigated to compare the altered quality properties of the abdomen and cheliped muscle in swimming crab (Portunus trituberculatus) during 100 days of frozen storage at -20â. Over the extended duration of frozen storage, the sensory evaluation, moisture content, water activity (Aw), and water-holding capacity (WHC) in the abdomen and cheliped muscles of swimming crab decreased, while the pH, total volatile basic nitrogen (TVB-N), and trimethylamine (TMA) increased. The increase and decrease rates of these indicators were smaller in the abdomen than those in the cheliped muscle. High-throughput sequencing results indicated a reduction in the microbial richness and diversity in the abdomen and cheliped muscles of the swimming crab as frozen storage time extended. Proteobacteria, Actinobacteriota, and Firmicutes, Achromobacter, Kocuria, and Staphylococcus were the dominant phylum and genus in both muscle tissues, respectively. Furthermore, the correlation analysis between the composition of the microbiota and physiochemical properties revealed that the growths of Kocuria, Vibrio, Staphylococcus, and Aliiroseovarius were closely related to the physiochemical factors. The study provides a theoretical reference for quality deterioration and develops new products of different parts in the swimming crab during frozen storage.
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Human milk is the best source of nutrition for infants. Lower freezing temperatures and faster freezing rates allow for better preservation of human milk. However, research on the freezing conditions of human milk is limited. This study investigated the effectiveness of quick freezing and suitable freezing conditions for home preservation. Human milk was stored under different freezing conditions (-18 °C, -18 °C quick freezing, -30 °C, -40 °C, -60 °C, and - 80 °C) for 30, 60, and 90 days and then evaluated for changes in the microbial counts, bioactive protein, and lipid. The results showed that the total aerobic bacterial and Bifidobacteria counts in human milk after storage at freezing temperatures of - 30 °C and lower were closer to those of fresh human milk compared to - 18 °C. Furthermore, the lysozyme loss, lipid hydrolysis degree, and volatile organic compound production were lower. However, -18 °C quick freezing storage was not markedly different from -18 °C in maintaining human milk quality. Based on the results, for household and environmental reasons, the recommended temperature for storing human milk is suggested as -30 °C.
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Frío , Leche Humana , Humanos , Congelación , Leche Humana/microbiología , Refrigeración , LípidosRESUMEN
Low-voltage electrostatic fields (LVEF) are recognized as a new technology that can improve the quality of frozen meat. To determine the extent to which LVEF assistance affects the quality of frozen pork for long-term storage, pork was frozen and stored at -18 and -38 °C for up to 5 months. Water-holding capacity, muscle microstructure, and protein properties were investigated after up to 5 months of frozen storage with and without LVEF assistance. In comparison to traditional -18 and -38 °C frozen storage, LVEF treatment inhibited water migration during frozen storage and thawing. As a result, thawing losses were reduced by 15.97% (-18 °C) and 3.38% (-38 °C) in LVEF-assisted compared to conventional freezing methods. LVEF helped to maintain the muscle fiber microstructure and reduce muscle protein denaturation by miniaturizing ice crystal formation by freezing. As a result of this study, LVEF is more suitable for freezing or short-term frozen storage, while a lower temperature plays a more significant role in long-term frozen storage.
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Carne de Cerdo , Carne Roja , Animales , Porcinos , Congelación , Carne Roja/análisis , Conservación de Alimentos/métodos , Electricidad Estática , Agua/químicaRESUMEN
The purpose of this study was to compare the influences of gamma-poly glutamic acid (γ-PGA) (1, 2, 3, and 4 %) to see which could outperform conventional cryoprotectant mixture (4 % sorbitol + 4 % sucrose) on cooked crayfish properties, such as physicochemical, textural qualities, oxidation reaction, water distributions, and microstructure integrity, during different freeze-thaw cycles. Crayfish quality characteristics improved significantly as γ-PGA concentration increased compared to control samples.Adding γ-PGA 4 % reduced the carbonyl content from 4.20 to 3.00 nmol/ mg protein during fluctuation-1 (F1), and from 4.15 to 2.80 nmol/ mg protein during fluctuation-2 (F2) compared to control samples. Furthermore, it increased the total sulfhydryl content from 4.15 and 4.76 to 6.19 and 6.47 mol/105 g protein during F1 and F2 and after five freeze-thaw cycles (FTC). This suggests that this concentration was more effective at controlling protein changes than other concentrations. γ-PGA generally enhanced the water-holding capacity by preventing protein denaturation and limiting ice crystal recrystallization. As a result, microstructure stability was evident, texture degradation was avoided, and the crayfish's color was preserved.
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Astacoidea , Ácido Poliglutámico/análogos & derivados , Agua , Animales , Temperatura , Congelación , Agua/químicaRESUMEN
Ice glazing containing 0.3 % D-sodium erythorbate (DSE), combined with vacuum packaging, was used as a method to maintain the quality of large yellow croaker during frozen storage. This study aimed to assess various aspects, including water properties (water holding capacity and moisture distribution), protein-related characteristics (secondary and tertiary structure of myofibrillar protein), freshness indicators (K value and total volatile base nitrogen (TVB-N)), and non-volatile flavor compounds (free amino acids (FAAs) and nucleotides) in samples stored for 300 days at -23 °C. The results showed that vacuum packaging had a significant inhibitory effect on the growth of ice crystal. Notably, it successfully maintained the cross-sectional area of nearly all ice crystals below 20,000 µm2, effectively curtailing water loss. Simultaneously, the combination of vacuum packaging with the complex ice glaze effectively mitigated the degradation of IMP and free amino acids, maintaining low levels of K value (12.85 %) and TVB-N (11.28 mg N/100 g) throughout the 300-day frozen storage, retaining first-class freshness. Among the various treatment modalities assessed, the combined application of vacuum packaging and 0.3 % DSE-infused ice glazing emerged as the most effective in terms of preservation outcomes. This efficacious combination shows promising potential for the frozen storage of aquatic products and is therefore recommended for practical implementation.
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Conservación de Alimentos , Perciformes , Animales , Conservación de Alimentos/métodos , Hielo , Vacio , Embalaje de Alimentos/métodos , Agua , AminoácidosRESUMEN
Frozen mandarin fish (MF) is utilized for preparation fermented MF. However, how raw material (RM) affects the quality and flavor of fermented MF is unclear. This study investigated the impact and mechanism of RM frozen storage on the microstructure, texture, water distribution, and flavor of fermented MF by light microscopy, texture profile analysis, low-field nuclear magnetic resonance, gas chromatography-ion mobility spectrometry, and multivariate analysis. With increasing RM frozen storage time, both frozen MF and frozen-based fermented MF decreased in muscle fiber density while increased in muscle fiber diameter. Additionally, RM frozen storage exhibited a significant impact on the water distribution of frozen MF, while no obvious effect on that of frozen-based fermented MF. Seven odorant (2-methyl-1-propanol, 3-hydroxy-2-butanone, 2,3-butanedione, hexanal-D, ethyl acetate-D, 3-pentanone, and acetone) were shown as potential markers to distinguish fermented MF. This study could provide a theoretical basis for the production of high-quality frozen-based fermented MF.
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Fish skin gelatin, as a waste product of sea bream, was used to obtain fish gelatin hydrolysate (FGH) with the treatment of alcalase (alc) and savinase (sav). The functional properties of FGHs and their usage possibilities in frozen dough bread making were investigated. FGH treated with alc showed a higher emulsifying stability index (189 min), while FGH treated with sav showed greater foaming capacity (27.8%) and fat-binding capacity (1.84 mL/g). Bread doughs were produced using two FGHs (alc and sav) and their combination (FGH-alc + FGH-sav). Using FGH treated with these enzymes individually was more effective than their combination in terms of polyacrylamide gel electrophoresis (SDS-PAGE) results and bread quality (specific volume and hardness). The addition of FGH into bread dough showed no significant effect on bread dough viscoelasticity (tan δ), while the increment level of tan δ value for control dough was higher than the dough containing FGH after frozen storage (-30 °C for 30 days). The highest freezable water content (FW%) was found in control dough (33.9%) (p < 0.05). The highest specific volume was obtained for control fresh bread and bread with FGH-alc, while the lowest volume was obtained for fresh bread containing FGH-sav (p < 0.05). After frozen storage of the doughs, the bread with FGH-alc showed the highest specific volume. FGH addition caused a significant reduction in the L* (lightness) value of fresh bread samples when compared to control bread (p < 0.05). This study suggested that usage of FGH-alc in bread making decreased the deterioration effect of frozen storage in terms of the specific volume and hardness of bread.
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In this study, the effects of frozen storage time, thawing treatments, and their interaction on the rheological properties of non-fermented dough were evaluated. Texture profile analysis (TPA), rheological measurements, including strain/frequency sweep, and creep-recovery measurement were applied to the dough. Compared with unfrozen fresh dough, the frozen storage time (S) and thawing treatment (T) influenced almost all indicators significantly, and their mutual effects (S × T) mainly affected the hardness and springiness. Frozen time was the main factor resulting in the destruction of non-fermented dough during the thawing treatments. Moreover, refrigerator thawing (4 °C) produced a dough with minimal changes in the rheological properties, regardless of the frozen storage time. Meanwhile, microwave thawing resulted in lower G' and lower zero shear viscosity (η0) values, as well as higher maximum creep compliance (Jmax) and hardness values. Moreover, the difference between the three thawing treatments was exacerbated after 30 days of frozen storage. SEM images also showed that long-term frozen storage combined with microwave thawing seriously destroyed the rheological properties, structural stability, and inner microstructure of the dough.