Pseudomonas weihenstephanensis through the iron metabolism pathway promotes in situ spoilage capacity of prepared beef steaks during cold storage.

In this study, we evaluated the histomorphology, reactive oxygen species (ROS), protein degradation, and iron metabolism characteristics and differential expression analysis of genes for siderophores synthesis and protease secretion in prepared beef steaks inoculated alone or co-inoculated with P. weihenstephanensis, B. thermotrichothrix and M. caseolyticus at 4 °C for 12 days. The results showed that the P. weihenstephanensis was the key bacteria that degraded protein in the process of prepared beef steaks spoilage, which led to protein oxidation by promoting ferritin degradation to release free iron and inducing ROS accumulation. The highest expression of FpvA and AprE was detected in the P. weihenstephanensis group by comparing qRT-PCR of the different inoculation groups. Both qRT-PCR and Western blot revealed that ferritin heavy polypeptide and ferritin light chain polypeptide gene and protein expressions were significantly higher in the P. weihenstephanensis inoculation group compared to the other inoculation groups. Results suggested that FpvA and AprE might play roles in meat spoilage and were potential positional, physiological and functional candidate genes for improving the quality traits of prepared beef steaks. This work may provide insights on controlling food quality and safety by intervening in spoilage pathways targeting iron carrier biosynthesis or protease secretion genes.

Cryoprotective effects and mechanisms of soybean oligosaccharides on the grass carp (Ctenopharyngodon idellus) surimi during frozen storage.

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.

Effect of processing (cutter versus continuous emulsifier) and sodium reduction on the physicochemical properties of bologna sausages.

BACKGROUND: Overcoming the impact of sodium reduction in the properties of emulsified sausages is a current challenge in the production of healthier meat products. Because the emulsifying process play a key role in the stability of sausages, the present study aimed to evaluate the effects of two mechanical emulsifying systems (cutter versus continuous emulsifier) and two levels of sodium chloride (2.50 and 1.25%) on the physicochemical characteristics of bologna sausages. RESULTS: A reduction of sodium increased the L* value and reduced the a* value, and also decreased the protein extraction yield in sausages produced in the cutter system. Moreover, the emulsion stability of reduced sodium batter was increased by cutter emulsification (F50C). On the other hand, the continuous emulsifier process did not decrease the extraction of myofibrillar proteins in F50E (sodium reduced treatment), resulting in minimal impact on emulsion stability and an increase in hardness in reduced-sodium sausages. CONCLUSION: Therefore, to produce low-sodium sausages, the continuous emulsifier was more effective producing batters with increased extracted myofibrillar proteins, improving the structure and functionality of myofibrillar proteins compared to the cutter process. © 2023 Society of Chemical Industry.

Glycosylation modification: A promising strategy for regulating the functionalities of myofibrillar proteins.

Myofibrillar proteins (MPs), the most important proteins in muscle, play a vital role in the texture, flavor, sensory and consumer acceptance of final muscle-based food products. Over the past several decades, conjugation of carbohydrates to MPs via glycosylation is of particular interest due to the substantial enhancement in MPs characteristics. Studying the covalent interactions between carbohydrates and MPs under various processing conditions and molecular mechanisms by which carbohydrates affect the functionalities of MPs can introduce new perspectives for design and production of muscle-based foods. However, there is no insightful and comprehensive summary of the structural, physicochemical and functional characteristics changes of MPs induced by glycosylation modification and how these changes can be adopted to potentially promote the science-based development of tailor-made muscle foods. Based on this, the functionalities of MPs as well as their practical limiting issues are initially highlighted. A comprehensive overview of fabrication strategies is then introduced. Additionally, changes in the structural and functional properties of MPs regulated by glycosylation have also been carefully summarized. On this basis, the research limitations to be solved and our perspectives for the future development of muscle-based foods are put forward.

Effects of quercetin on the gel properties of pork myofibrillar proteins and related changes in protein conformation.

BACKGROUND: To study the effects of quercetin on the functionality of myofibrillar proteins (MPs), various levels of quercetin (0, 10, 50, 100 and 200 µmol g-1 protein) were added to MP solution and the structure and gel properties of MPs were determined. RESULTS: Compared with the control MPs not treated with quercetin, adding 10, 50 and 100 µmol g-1 quercetin caused a significant (P < 0.05) loss of sulfhydryls; 10 and 50 µmol g-1 quercetin enhanced the surface hydrophobicity significantly (P < 0.05), and 50, 100 and 200 µmol g-1 quercetin reduced the fluorescence intensity of tryptophan. Additions of 50, 100 and 200 µmol g-1 quercetin resulted in a significant (P < 0.05) reduction in MP solubility. Adding 10, 50 and 100 µmol g-1 quercetin did not significantly (P > 0.05) change the gel strength and water-holding ability of MPs than control, but 200 µmol g-1 quercetin declined the gel properties significantly (P < 0.05). The microstructure and dynamic rheological properties confirmed the results of the gel properties of MPs affected by various levels of quercetin. CONCLUSION: The results obtained in the present study show that mildly high levels of quercetin can maintain the gel properties of MPs, which may be a result of the moderate MP cross-linkage and aggregation caused by the covalent and non-covalent interactions of MPs. © 2023 Society of Chemical Industry.

Effect of lentinan on gelling properties and structural changes of goose myofibrillar protein under oxidative stress.

BACKGROUND: The reduction of protein oxidation is important for maintaining the product quality of reconstituted meat. In this study, the dose-dependent effects of lentinan (LNT) on gelling properties and chemical changes in oxidatively stressed goose myofibrillar protein were investigated. RESULTS: Myofibrillar protein (MP) with 200 µmol g-1 protein LNT increased gel strength by 87.90 ± 9.26% in comparison with LNT-free myofibrillar protein after oxidation. Scanning electron microscopy analysis revealed that the gel network containing LNT was compact, with small pores and uniform distribution. The absolute value of the zeta potential reduced significantly following oxidation of LNT with 200 µmol g-1 protein at 4 °C for 12 h compared with the zeta potential without LNT, according to the laser particle size analyzer. The incorporation of LNT increased protein solubility and -SH content, inhibited carbonyl formation, enhanced α-helix content and tryptophan intrinsic fluorescence intensity, and reduced exposure of hydrophobic groups and protein aggregation. CONCLUSION: The results indicated that adding LNT to myofibrillar protein could improve gel. This is related to its protective effect on conformational changes in the oxidation system. Lentinan is therefore recommended for oxidatively stressed goose meat processing to enhance the MP gelling potential. © 2023 Society of Chemical Industry.

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

Myofibrillar protein (MP) endows muscle foods with texture and important functional properties, such as water-holding capacity (WHC) and emulsifying and gel-forming abilities. However, thawing deteriorates the physicochemical and structural properties of MPs, significantly affecting the WHC, texture, flavor, and nutritional value of muscle foods. Thawing-induced physicochemical and structural changes in MPs need further investigation and consideration in the scientific development of muscle foods. In this study, we reviewed the literature for the thawing effects on the physicochemical and structural characters of MPs to identify potential associations between MPs and the quality of muscle-based foods. Physicochemical and structural changes of MPs in muscle foods occur because of physical changes during thawing and microenvironmental changes, including heat transfer and phase transformation, moisture activation and migration, microbial activation, and alterations in pH and ionic strength. These changes are not only essential inducements for changes in spatial conformation, surface hydrophobicity, solubility, Ca2+ -ATPase activity, intermolecular interaction, gel properties, and emulsifying properties of MPs but also factors causing MP oxidation, characterized by thiols, carbonyl compounds, free amino groups, dityrosine content, cross-linking, and MP aggregates. Additionally, the WHC, texture, flavor, and nutritional value of muscle foods are closely related to MPs. This review encourages additional work to explore the potential of tempering techniques, as well as the synergistic effects of traditional and innovative thawing technologies, in reducing the oxidation and denaturation of MPs and maintaining the quality of muscle foods.

Sarcoplasmic and myofibrillar phosphoproteins profile of beef M. longissimus thoracis with different pHu at different days postmortem.

BACKGROUND: The abnormal ultimate pH (pHu ) in postmortem muscles affect the meat quality and results in substantial economic losses. Dark, firm, and dry (DFD) meat linked with the higher postmortem pHu values and exhibited many quality issues such as dark color, tough texture and shorter shelf life. This research aimed to investigate the effect of protein phosphorylation on variations in beef pHu in order to explore the possible mechanisms underlying DFD meat formation. RESULTS: Glycogen and lactate contents were higher, while L* and a* were lower in high pHu beef. Shear force was higher in intermediate pHu group. Global phosphorylation of sarcoplasmic proteins was higher in low pHu samples on day 1 and of myofibrillar proteins was higher in intermediate pHu meat on days 1 and 2 postmortem. Sarcoplasmic protein bands with different phosphorylation levels were identified as containing some glycometabolism and stress response proteins and phosphorylated myofibrillar protein bands were identified sarcomeric and metabolic proteins. CONCLUSIONS: Phosphorylation of multiple proteins of glycolytic pathway and contractile machinery may play critical roles in development of DFD beef. © 2021 Society of Chemical Industry.

Influence of epicatechin on oxidation-induced physicochemical and digestibility changes in porcine myofibrillar proteins during refrigerated storage.

BACKGROUND: The influence of epicatechin (EC) on the physicochemical properties and digestibility changes of porcine myofibrillar protein (MP) under oxidative stress during refrigerated storage was investigated. RESULTS: The incubation of MP suspensions (20 mg mL-1 in piperazine-N,N'-bis(2-ethanesulfonic acid) buffer, with 0.6 mol L-1 sodium chloride, pH 6.25) at 4 °C for 24 h under an iron-catalyzed hydroxyl radical generating system (Fenton reaction) promoted the formation of thiobarbituric acid reactive substances and protein carbonyls, which was attenuated by EC (5, 50, and 100 µmol g-1 protein). Reduced protein sulfhydryl content, tryptophan fluorescence, protein solubility, as well as increased surface hydrophobicity were found by the co-incubation of EC. Analysis by scanning electron microscopy revealed increased protein aggregation and fragments in oxidized MP, which were further enhanced by the addition of EC. However, the protein digestibility of MP was not affected. CONCLUSION: EC was demonstrated to be effective in alleviating lipid oxidation and protein carbonylation in MP under oxidative stress. Additionally, the physicochemical and digestibility changes accompanying the incorporation of EC was complicated due to the possible phenol-protein interactions. An in-depth understanding of protein physicochemical and digestibility changes will be helpful in the application of polyphenolic compounds as antioxidants in low-temperature-processed muscle foods. © 2020 Society of Chemical Industry.

Myoprotein-phytophenol interaction: Implications for muscle food structure-forming properties.

Phenolic compounds are commonly incorporated into muscle foods to inhibit lipid oxidation and modify product flavor. Those that are present in or extracted from plant sources (seeds, leaves, and stems) known as "phytophenols" are of particular importance in the current meat industry due to natural origins, diversity, and safety record. Apart from these primary roles as antioxidants and flavorings, phytophenols are now recognized to be chemically reactive with a variety of food constituents, including proteins. In processed muscle foods, where the structure-forming ability is critical to a product's texture-related quality attributes and palatability, the functional properties of proteins, especially gelation and emulsification, play an essential role. A vast amount of recent studies has been devoted to protein-phenol interactions to investigate the impact on meat product texture and flavor. Considerable efforts have been made to elucidate the specific roles of phytophenol interaction with "myoproteins" (i.e., muscle-derived proteins) probing the structure-forming process in cooked meat products. The present review provides an insight into the actions of phytophenols in modifying and interacting with muscle proteins with an emphasis on the reaction mechanisms, detection methods, protein functionality, and implications for structural characteristics and textural properties of muscle foods.

Covalent chemical modification of myofibrillar proteins to improve their gelation properties: A systematic review.

To improve the quality of meat products is a constant focus for both the meat industry and scientists. As major components in meat protein, the gelation properties of myofibrillar proteins (MPs) predominantly determine the sensory quality and product yield of the final product. Naturally or artificially occurring covalent modifications are known to largely affect MP functionality by changing the protein structure and forming aggregates, leading to both favorable and unfavorable outcomes. The review aims to summarize the mechanisms associated with several covalent modifications and the recent developments in enhancing MP gelation properties. Various extrinsic and intrinsic parameters controlling oxidation, phenolic-protein interactions, enzyme catalysis, glycation, and isoelectric solubilization/precipitation, and their effects on the characteristics of heat-induced MP gels are discussed. This article provides an improved understanding of the covalent modifications that occur mainly in the MP system and how they can be utilized to promote its gelation properties. Covalent modifications exhibited dose-dependent and dual-role manners for MP gelation properties. Mild oxidation, enzyme catalysis, and isoelectric solubilization/precipitation treatment would be beneficial to form more aligned and cross-linked three-dimensional networks for MP gels because of moderate protein aggregation. However, an excessive aggregate impedes the MP gelation behavior, leading to reduced gelation quality. Glycation effectively increased hydrophilicity of MPs and phenolic conjugation provides MPs with novel bioactivity. A proper utilization of such a process or even a rational combination of them allowed us to enhance the gelation properties of MP with assorted appreciated functionalities and further improve the quality of meat products.

Effects of Oil Droplet Size and Interfacial Protein Film on the Properties of Fish Myofibrillar Protein-Oil Composite Gels.

The effects of oil droplet size and the formation of an interfacial protein film (IPF) on silver carp myofibrillar protein (MP)-oil composite gels were studied. MP- or Tween 80-stabilized camellia seed oil emulsions with different droplet sizes were prepared and added to MPs to prepare composite gels. The oil droplet size of the Tween 80-stabilized emulsion was significantly smaller (p < 0.05) than that of the MP-stabilized emulsion with the same homogenization speed. However, polymerization of Tween 80-stabilized emulsions during the preparation of the composite gels was found. Composite gels with the MP-stabilized emulsions of a small droplet size showed significantly improved water-holding capacity, texture, and dynamic rheological properties. Interfacial shear rheology studies revealed that the storage modulus (G') of the MP-stabilized emulsion composite gels was higher than that of the Tween 80-stabilized gels, and the tan δ of the MP-stabilized oil emulsion composite gels was smaller than that of the Tween 80-stabilized gels, indicating that stronger elastic gel structures were formed. These results suggested that the IPF formed in the MP-stabilized emulsion helped stabilize the oil droplets embedded in the protein gel network, and the smaller the droplet size, the more stable the composite gel. This work provides a better understanding of how oil emulsions interact with protein and affect the properties of MP-oil composite gels.

Binding of aldehydes to myofibrillar proteins as affected by two-step heat treatments.

BACKGROUND: The present study investigated the effect of two-step heat treatments on the structure of grass carp myofibrillar proteins (MPs) and their binding ability for selected aldehydes (hexanal, heptanal, octanal and nonanal). RESULTS: Within 30 min of the first heating step at 40 °C and 5-10 min of the second heating step at 90 °C, the enhancement of the flavor-binding ability was likely explained by the increases in surface hydrophobicity and total sulfhydryl content due to the unfolding of secondary structures of MPs through exposure of hydrophobic amino acids and sulfhydryl groups. Nevertheless, lengthy heating at 90 °C accelerated the aggregation of unfolded MPs and reduced the hydrophobic bonding sites, thus weakening the hydrophobic interactions and decreasing the resultant binding ability of MPs with aldehydes. CONCLUSION: The binding ability of aldehydes to MPs was found to be strongly influenced by changes in protein structure and surface during the two-step heating process. The results provided insight into improving the flavor characteristics of freshwater fish surimi products. © 2019 Society of Chemical Industry.

Effects of starch type and concentration on the physicochemical properties of bilayer-stabilized oil-in-water emulsion gels enriched with ß-1,3/1,6-D-glucans.

BACKGROUND: In recent years, consumer interest in low-fat foodstuffs having a clean label and potential benefits over physiological functions has shown a growing trend. ß-1,3/1,6-d-Glucans (BGs) from Saccharomyces cerevisiae have been recognized as excellent immune-modulating compounds. Bilayer-stabilized oil-in-water emulsion gels (BEGs) containing oil droplets covered by myofibrillar proteins-gum arabic membranes were used for entrapping BGs in the inner phase. This study investigated the effects of starch type (waxy maize starch, WMS; potato starch, PS) and concentration (0.0-50 g kg-1 ) on the physicochemical properties of BEGs composed of: 200 g kg-1 rapeseed oil, 40 g kg-1 myofibrillar proteins, 14 g kg-1 gum arabic, 15 g kg-1 BGs, 1 g kg-1 citric acid. RESULTS: The results showed that BGs were successfully incorporated into the inner phase of BEGs and stability testing showed no separated oil and sediment layer. BEGs were characterized by droplet diameter of d3,2 = 3.62 ± 0.209 µm and electrical charge of the outer membrane of -27.4 ± 0.257 mV. Increasing starch concentration significantly (P < 0.05) affected values of the studied rheological parameters, but to a greater extent in relation to PS than WMS. Sensory analysis showed that BEGs were most desirable at WMS and PS concentrations of 40-50 and 30-40 g kg-1 , respectively. CONCLUSIONS: BEGs containing oil droplets covered by myofibrillar proteins-gum arabic membranes can be used as carriers for insoluble ß-glucans and manufactured with a wide range of rheological properties and sensory features desired by consumers. © 2020 Society of Chemical Industry.

Effect of high-pressure processing enzymatic hydrolysates of soy protein isolate on the emulsifying and oxidative stability of myofibrillar protein-prepared oil-in-water emulsions.

BACKGROUND: Oil-in-water (O/W) emulsions are thermodynamically unstable and are easily oxidized. Recently, protein hydrolysates have been used to enhance the emulsifying and oxidative stability of emulsions. High-pressure processing (HPP) enzymatic hydrolysates of soy protein isolate have higher bioactivities. The objective of the study was to investigate the effects of various soy protein isolate hydrolysate (SPIH) concentrations obtained during different 4 h pressure treatments on improving the emulsifying and oxidative stability of myofibrillar protein (MP) emulsions. RESULTS: Emulsions with 4 mg mL-1 SPIH obtained at 200 MPa had the highest emulsifying activity index and emulsion stability index (P ≤ 0.05). This increase in emulsion stability was related to increased zeta potential and reduced average particle size. Optical microscopy and confocal laser scanning microscopy observations confirmed that emulsions with 4 mg mL-1 SPIH possessed relatively small oil droplets. The addition of SPIH obtained at 200 MPa significantly reduced thiobarbituric acid reactive substance values (P ≤ 0.05) of emulsions during 8 days of storage. Concurrently, the carbonyl content remained the lowest and the sulfhydryl content remained the highest, which indicated that the emulsions had higher protein oxidative stability. CONCLUSIONS: SPIH obtained under HPP could improve the emulsifying and oxidative stability of MP-prepared O/W emulsions.

Glucose-conjugated chicken myofibrillar proteins derived from random-centroid optimization present potent hydroxyl radical scavenging activity.

The optimal conditions for the preparation of glucose-conjugated chicken myofibrillar proteins (Mfs) via the Maillard reaction, presenting strong antioxidant activity against hydroxyl radicals (ï½¥OH) and high solubility in low ionic strength medium, were sought using random-centroid optimization (RCO). Four parameters of temperature, relative humidity (RH), reaction time, and glucose-to-Mfs mixing ratio, were examined, resulting in a total of 24 vertices. Evaluations were carried out relatively to each individual vertex, and the optimal preparatory conditions to obtain the highest antioxidant activity were determined as follows: temperature of 52 °C, RH of 38%, reaction time of 6.79 h, and a glucose to Mfs mixing ratio of 11.7 (w/w). The resulting glucose-conjugated chicken Mfs gained thermal gel-forming ability and its ï½¥OH averting capacity reached 9.7 ± 0.7 µmol of gallic acid equivalent/g of protein.Abbreviations: GA: gallic acid; HORAC: hydroxyl radical averting capacity; IC50: half-maximal inhibitory concentration; 2-ME, 2-mercaptoethanol; Mfs: myofibrillar proteins; MHC: myosin heavy chain; ï½¥OH: hydroxyl radical; PAGE: polyacrylamide gel electrophoresis; RCO: random-centroid optimization; RH: relative humidity; RLU: relative light units; SDS: sodium dodecyl sulfate; SEM: scanning electron microscope; SS: disulfide.

Effect of ultrasonic thawing on the water-holding capacity, physicochemical properties and structure of frozen tuna (Thunnus tonggol) myofibrillar proteins.

BACKGROUND: The effect of ultrasonic thawing (0, 160, 280, 400 W) on water-holding capacity (WHC), physicochemical properties and structure of tuna myofibrillar proteins was investigated. RESULTS: Thawing time was shown to decrease and thawing loss to increase significantly (P < 0.05) as power increased (160-400 W), whereas there was no significant difference (P > 0.05) in cooking loss. Changes in T2 relaxation time were investigated using low-field nuclear magnetic resonance. Ultrasonic thawing could significantly (P < 0.05) improve the immobilised water content compared to the control (0 W). surface hydrophobicity decreased significantly and then increased significantly (P < 0.05), whereas there was no significant difference (P > 0.05) in the reactive sulfhydryl content as power was increased. Tuna thawed at 280 W suffered fewer negative effects on its microstructure. Roman spectral date showed that the α-helix changed to a random coil and ß-turn as power was increased (up to 400 W). CONCLUSION: The application of ultrasonic thawing at a specified power was showed to be a beneficial process when used in the seafood industry, but application of excessive power resulted in lower WHC and structural changes to myofibrillar proteins. © 2019 Society of Chemical Industry.

The effect of cooking temperature on the aggregation and digestion rate of myofibrillar proteins in Jinhua ham.

BACKGROUND: In order to evaluate the effect of cooking temperature on the nutrition quality of dry-cured hams, 60 biceps femoris samples from 16 Jinhua hams were divided into four groups (control, 70, 100 and 120 °C) and cooked for 30 min. Carbonyl content, sulfhydryl groups, surface hydrophobicity, microstructure, protein aggregation and digestibility of myofibrillar proteins were investigated. RESULTS: Cooking promoted carbonylation and decreased sulfhydryl groups in a temperature-dependent way. Scanning electron microscopy and Nile Red revealed that protein aggregation became a main phenomenon at 120 °C; it coincided with surface hydrophobicity. The increased carbonyl content and decreased sulfhydryl groups contributed to the formation of aggregates. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis profiles showed the initial difference in proteolysis rate among four groups. The in vitro digestibility of pepsin and of trypsin and α-chymotrypsin increased from the control to 100 °C and decreased from 100 to 120 °C. CONCLUSION: The increased digestibility could be attributed to the oxidation of proteins and exposing recognition sites of digestive enzymes, while the decreased digestibility was due to the formation of aggregates. Cooking was a main factor that affected the digestibility of Jinhua ham, and cooking at 100 °C could be an ideal way to gain the highest digestibility of Jinhua ham. © 2018 Society of Chemical Industry.

Effects of konjac glucomannan and acetylated distarch phosphate on the gel properties of pork meat myofibrillar proteins.

The effects of konjac glucomannan (KGM) and acetylated distarch phosphate (ADSP) on properties of pork meat myofibrillar protein (MP) were investigated using rotary rheometer, colorimeter, texture analyzer, Fourier transform infrared spectroscopy (FTIR), scanning electron microscope (SEM) and confocal laser scanning microscope (CLSM). The addition of KGM and ADSP resulted in increase in both storage modulus (G') and water holding capacity. Whiteness of MP gels was not influenced by the addition of KGM or ADSP, but the texture of MP gels changed apparently with the incorporation of KGM or ADSP. The temperature sweep showed that the increase in G' was associated with the gelatinization of ADSP and its synergistic effect with KGM. The FTIR indicated that the addition of KGM and ADSP enhanced the hydrogen bond in the gel system. The addition of KGM and ADSP changed the microstructures of MP gels, indicating the possible interactions among KGM, ADSP and MP. The images of CLSM showed that starch granules filled in the gap in the protein network, meanwhile the KGM evenly dispersed in the protein network structure.

The Effect of High Pressure and Subzero Temperature on Gelation of Washed Cod and Salmon Meat.

The objective of the present work is to examine the influence of pressure up to 193 MPa at subzero temperature (without freezing of water) on myofibrillar proteins of salmon and cod meat and on the properties of gels obtained from washed mince of these fish. The solubility of proteins from myofibrils of cod and salmon meat suspended in 100 mM KCl solution increased after treating the samples with pressure above 60 MPa. The results of SDS- -PAGE analysis showed that under these conditions two myosin light chains, tropomyosin and troponin T were released from myofibrils. The solubility of proteins in 0.9 M NaCl solution of washed fish meat after pressure treatment at 60 MPa and -5 °C decreased to about 80-90% and at 193 MPa and -20 °C to 60%. Pressurization of cod meat decreased only slightly the solubility of proteins in SDS and urea solution and the solubility of salmon meat was similar to that in the unpressurized sample. There were no differences in the electrophoretic pattern of proteins from untreated and pressurized cod and salmon meat in the range of 60 to 193 MPa and -5 to -20 °C. The pressure treatment of washed salmon and cod meat at a temperature below 0 °C induced gelation; on the other hand, hardness of gels was lower by 28 and 26%, respectively, than that of gels formed by heating. The salmon and cod gels pressurized at 193 MPa and -20 °C and then heated were much harder than only pressurized or heated gels.