Biochemical and gelling properties of tilapia surimi and protein recovered using an acid-alkaline process

The biochemical and gel properties of tilapia surimi prepared by a conventional washing method and protein isolated using alkaline-acid-aided processes were studied. Solubility and recovery of protein was found to be highest by using a conventional method, followed by an alkaline- and acid-aided process, respectively. Decreases in myoglobin and lipid contents were found in alkaline- or acid-aided process when compared to the conventional process (p < 0.05). The highest breaking force and deformation of kamaboko and modori gels was found in the gels prepared by the conventional washing method. Higher expressible water and whiteness were found in modori gels when compared to kamaboko gels. TCA-soluble peptide contents of conventional surimi gels were lower than those of acid- and alkaline-recovered protein gels. Degradation of myofibrillar protein was observed in acid-isolated protein. Microstructure of kamaboko gels showed more compact network than in modori gels in both conventional surimi and protein recovered using the pH-shift process.     

Color improvement by titanium dioxide and its effect on gelation and texture of proteins recovered from whole fish using isoelectric solubilization/precipitation

Whiteness is a critical attribute for restructured fish products such as surimi seafood. However, the whiteness of gels made from proteins recovered from fish processing by-products or whole fish using isoelectric solubilization/precipitation is poor. The by-products and whole fish contain bones, scales, skin, etc. that affect gel color. Therefore, whiteness needs to be improved if marketable products are to be developed from recovered proteins. The objectives of this study were to determine effects of titanium dioxide (TiO₂) on: (1) color; (2) texture; and (3) viscoelasticity (G′) of gels made from isolated carp proteins and Alaska pollock surimi. Carp proteins were recovered with isoelectric solubilization/precipitation. TiO₂ was added to carp proteins at 0-0.5 g/100 g. TiO₂ was not added to surimi. Due to much higher (P < 0.05) yellowness (b^∗) and lower (P < 0.05) lightness (L^∗), the whiteness of carp gels without TiO₂ was lower (P < 0.05) than surimi gels. TiO₂ at ≥ 0.2 g/100 g resulted in better (P < 0.05) whiteness of carp gels than surimi gels without chalky and artificially white appearance. TiO₂ did not affect texture or viscoelasticity. This research demonstrates that whiteness of restructured fish products based on proteins recovered from whole fish via isoelectric solubilization/precipitation can be similar to the whiteness of surimi seafood.     

Impact of microbial transglutaminase on gelling properties of Indian mackerel fish protein isolates

Impacts of microbial transglutaminase (MTGase) (0–0.6 units/g sample) on gel properties of Indian mackerel unwashed mince, surimi and protein isolates with and without prewashing were studied. Generally, lower myoglobin and lipid contents were found in protein isolate with and without prewashing, compared to those of unwashed mince and surimi (P < 0.05). Protein isolate had the decreased Ca²⁺-ATPase and protein solubility, indicating protein denaturation. When MTGase was incorporated, breaking force and deformation of all gels markedly increased, especially as MTGase levels increased (P < 0.05). At the same MTGase level, gel from protein isolate with prewashing exhibited the highest breaking force and deformation (P < 0.05). The addition of MTGase could lower the expressible moisture content of most gels. No change in whiteness of gel was observed with the addition of MTGase (P > 0.05), but gel from protein isolate gels had decreased whiteness as MTGase at high level was added. The microstructure of protein isolate gels without prewashing showed a similar network to unwashed mince gels, whilst a similar network was observed between surimi gel and gel from protein isolate with prewashing. Nevertheless, a larger void was noticeable in gels from protein isolates. All gels incorporated with MTGase (0.6 units/g) showed a slightly denser network than those without MTGase. Thus, gel with improved properties could be obtained from protein isolate from Indian mackerel with added MTGase.     

Effect of porcine plasma protein and setting on gel properties of surimi produced from fish caught in Thailand

Effects of porcine plasma protein (PPP) and high temperature setting on gel properties of surimi from bigeye snapper, bigeye croaker, threadfin bream and barracuda were investigated. PPP was effective in increasing breaking force and deformation of kamaboko gels set at 40°C for 30 min and heated at 90°C for 20 min. The optimum levels of PPP were 0.5, 0.5, 1.5 and 1.5 g/100 g and the optimum setting times were 2, 1.5, 1.5 and 2 h for bigeye snapper, bigeye croaker, threadfin bream and barracuda surimi, respectively. However, the addition of PPP significantly decreased whiteness (P<0.05). An increase in gel-forming ability of surimi with PPP coincided with a decrease in solubility in mixture of SDS, urea and β-mercaptoethanol, indicating the formation of nondisulfide covalent bond induced by both endogenous and plasma transglutaminase. The results supported that PPP improve the gelation of surimi in combination with setting.     

Functional properties of proteins recovered from silver carp (Hypophthalmichthys molitrix) by isoelectric solubilization/precipitation

Isoelectric solubilization/precipitation at acidic and basic pH ranges was applied to whole gutted silver carp (Hypophthalmichthys molitrix) in order to recover muscle proteins. Thermal denaturation (T_onset, T_max, and ΔH), viscoelasticity (G′), and texture properties (shear stress) of proteins recovered from carp as affected by functional additives (beef plasma protein, potato starch, exogenous transglutaminase, polyphosphate, and titanium dioxide) were determined and compared to Alaska pollock surimi. Proteins recovered from carp showed typical endothermic transitions only when functional additives were used. Similar to endothermic transitions, viscoelasticity in carp proteins increased only when the additives were used. Typical endothermic peaks and viscoelasticity increase were recorded for Alaska pollock surimi. Carp protein-based gels with functional additives had lower (P < 0.05) shear stress than their surimi counterparts, but greater (P < 0.05) or similar (P > 0.05) when compared to surimi gels without functional additives. In addition, generally higher shear stress was measured for carp protein-based gels developed from basic pH treatments than the acidic counterparts. The present study indicates that proteins can be recovered from whole gutted carp using isoelectric solubilization/precipitation. However, if the recovered proteins are used for subsequent development of restructured food products, functional additives should be used.     

Gel properties of croaker–mackerel surimi blend

Gel properties of croaker surimi blended with three types of mackerel surimi at different ratios were evaluated. The gel strength of the croaker–mackerel surimi blend was higher than that of the original mackerel surimi (p < 0.05). The presence of croaker surimi in the blend resulted in the increase in myosin heavy chain (MHC) band intensity. No differences in deformation of gels were observed in croaker surimi and croaker-short-bodied mackerel blend at all ratios (p > 0.05). The addition of short-bodied mackerel surimi into croaker surimi up to a ratio of 1:2 had no effect on whiteness and metmyoglobin content of the gel (p > 0.05). Marked decrease in expressible drip and TCA-soluble peptide of gel was noticeable in croaker–frigate mackerel surimi blend (p < 0.05). Therefore, the gel properties of croaker–mackerel surimi blend were governed by the type and content of mackerel surimi used.     

EFFECT OF CHICKEN PLASMA PROTEIN AND SOME PROTEIN ADDITIVES ON PROTEOLYSIS AND GEL-FORMING ABILITY OF SARDINE (SARDINELLA GIBBOSA) SURIMI

The effect of chicken plasma protein (CPP) and various protein additives on autolysis and gel‐forming ability of sardine (Sardinella gibbosa) surimi was investigated. CPP and other protein additives showed inhibitory activity toward autolysis of sardine surimi incubated at 70C in a concentration‐dependent manner. Porcine plasma protein (PPP) and egg white (EW) were more effective in proteolysis prevention than CPP and other protein additives. Breaking force and deformation of both modori and kamaboko gels increased when CPP and other protein additives were added at levels up to 2% (P < 0.05). Nevertheless, PPP and EW showed a greater gel‐strengthening effect than CPP and other protein additives (P < 0.05). Addition of CPP and other plasma proteins resulted in decreased whiteness, especially with increasing amount (P < 0.05). However, no change in whiteness was observed with gels containing EW and soy protein isolate (SPI) (P > 0.05). Proteolysis of sardine surimi can be retarded by the addition of CPP and protein additives, leading to increased gel‐forming ability.     

Effect of microwave heating on the low-salt gel from silver carp (Hypophthalmichthys molitrix) surimi

Gels from silver carp (Hypophthalmichthys molitrix) surimi were obtained using microwave (MW) heating (15 W/g power intensity for 20–80 s) at different levels of salt (0 g/100 g, 1 g/100 g, or 2 g/100 g). And the gel heated by MW was compared with the gel obtained by conventional water-bath heating (85 °C for 30 min). The gel strength increased when the salt level was increased. The mechanical and functional properties of non-salted, low-salt and regular-salt products were improved by MW heating for 60 s and 80 s, significantly (p < 0.05), except for the cook loss. The content of TCA-soluble peptides indicated that the MW heating inhibited the autolysis of proteins significantly (p < 0.05) during gelling. The SDS-PAGE and total content of –SH group proved that MW enhanced the cross-linking of proteins effectively through disulphide bonds and non-disulphide covalent bonds. The microstructure of the samples revealed that a fine compact network, with particles of protein aggregates, was formed in the low-salt gels (1 g/100 g) heated by MW for 60 s. All of these properties might be responsible for the formation of a superior textural low-salt gel induced by MW.     

Physicochemical properties and gel-forming ability of surimi from three species of mackerel caught in Southern Thailand

Physicochemical and gelation properties of surimi prepared from three species of mackerel were investigated. The highest whiteness with the lowest redness index corresponding to the lowest myoglobin content especially its oxidised form, metmyoglobin, was found in short-bodied mackerel (Rastrelliger brachysoma) surimi (p < 0.05). Frigate mackerel (Auxis thazard) surimi contained the highest lipid content (p < 0.05). The pH of all surimi was in the range of 6.58–6.80. The highest sulfhydryl group and Ca²⁺-ATPase activity was found in natural actomyosin extracted from short-bodied mackerel surimi (p < 0.05). The highest TCA-soluble peptide content was found in frigate mackerel surimi gels (p < 0.05). Kamaboko gel of short-bodied mackerel surimi exhibited the highest breaking force with the lowest expressible drip (p < 0.05). Heating regime had no effect on deformability of gels from Indian mackerel (Rastrelliger kanagurta) and short-bodied mackerel but not for frigate mackerel. The highest metmyoglobin content with the lowest whiteness was found in frigate mackerel surimi gel (p < 0.05). Therefore, short-bodied mackerel was the best suited for the production of surimi with superior functional attributes including whiteness and gel-forming ability.     

Effect of chitin and chitosan on gelling properties of surimi from barred garfish (Hemiramphus far)

The addition of chitin/chitosan significantly increased the breaking force and deformation of gels prepared from barred garfish surimi (P < 0.05). Addition of 7B chitosan with 65.6% degree of deacetylation (% DD) at the level of 15 mg g⁻¹ resulted in the maximum increases in both breaking force and deformation of suwari and kamaboko gels compared to the control and gels containing chitin or chitosan with other % DD (P < 0.05). A chitosan concentration of 10 mg g⁻¹ was found to render the highest breaking force of kamaboko gel compared to other concentrations tested (P < 0.05). Kamaboko gel containing chitosan had an increased breaking force as the calcium chloride concentration increased (P < 0.05), indicating the role of endogenous transglutaminase in cross‐linking of protein–protein and protein–chitosan conjugates. Therefore the incorporation of chitosan and calcium chloride greatly improved the gelling properties of surimi from barred garfish without changes in colour. © 2000 Society of Chemical Industry     

Enhancement of gel strength of bigeye snapper (Priacanthus tayenus) surimi using oxidised phenolic compounds

Effects of different oxidised phenolic compounds (ferulic acid, OFA; tannic acid, OTA; catechin, OCT and caffeic acid, OCF) at different levels (0–0.25% of protein content) on the properties of gels from bigeye snapper (Priacanthus tayenus) surimi were investigated. Breaking force and deformation of surimi gel varied with types and amounts of oxidised phenolic compounds. Gels added with 0.20% OFA, 0.05% OTA, 0.15% OCF and 0.05% OCT exhibited the marked increases in both breaking force and deformation, compared with the control (P < 0.05). Those increases were associated with lower expressible moisture content. No increases in both breaking force and deformation were observed when ferulic acid without oxygenation at alkaline pH was added, regardless of amount added (P > 0.05). No changes in the whiteness of gel were found with addition of OFA (P > 0.05), but the decreases in whiteness were noticeable as other oxidised phenolics were incorporated (P < 0.05). Different microstructures were obtained among gels with different oxidised phenolics. The physicochemical properties of natural actomyosin suggest that oxidised phenolics could induce conformational changes and the cross-linking through amino groups or the induction of disulphide bond formation. Therefore, the addition of oxidised phenolic compounds at the optimum level could increase the gel strength of surimi gel.     

Gelling properties of white shrimp (Penaeus vannamei) meat as influenced by setting condition and microbial transglutaminase

The properties of white shrimp (Penaeus vannamei) gel added with different levels of microbial transglutaminase (MTGase) and subjected to setting at 25 °C for 2 h or 40 °C for 30 min, prior to heating at 90 °C for 20 min were studied. Breaking force of gels with and without setting increased with increasing MTGase amount added (P<0.05). However, no changes in deformation in all samples were noticeable (P>0.05). Directly heated gels showed the lower breaking force than those with prior setting at all MTGase levels added (P<0.05). Generally, gels prepared by setting at 25 °C exhibited the greater breaking force than those set at 40 °C, possibly associated with the appropriate protein structure for cross-linking at 25 °C and greater degradation at 40 °C as evidenced by a greater trichloroacetic acid soluble peptide content (P<0.05). Sodium dodecyl sulfate polyacrylamide gel electrophoretic study revealed that myosin heavy chain (MHC) underwent polymerization to a higher extent in the presence of MTGase, but the strengthening effect on gel was dependent on setting temperature. Regardless of setting condition, microstructure of gel added with MTGase was finer with a smaller void, compared with those of gel without MTGase. Therefore, setting temperature played an essential role in gel property of white shrimp meat added with MTGase.     

Effect of formaldehyde on protein cross-linking and gel forming ability of surimi from lizardfish induced by microbial transglutaminase

Impact of formaldehyde (FA) at various levels (0–9 μmol/g surimi) on gel properties of surimi from lizardfish added with microbial transglutaminase (MTGase) was studied. During iced storage of 10 days, total and free FA in lizardfish flesh increased continuously (P < 0.05). In the presence of FA, breaking force of gels slightly increased, whilst the deformation decreased (P < 0.05). The addition of MTGase (0.4 units/g surimi) was able to increase gel strength and water holding capacity of resulting gel. Nevertheless, gel strengthening effect of MTGase was lowered when FA at higher level was present. Myosin heavy chain (MHC) dominantly underwent polymerisation to a higher extent when either MTGase or FA was added. The higher reduction in ε-amino group content was observed in natural actomyosin (NAM) when FA at higher levels (0–30 μmol/g protein) was incorporated. Acyl transfer reaction mediated by MTGase was impeded in NAM containing FA, especially at higher levels. Generally, FA had an adverse effect on cross-linking ability towards surimi proteins induced by MTGase. Therefore, cross-linking and gel-forming ability of lizardfish surimi could be maximised by MTGase when surimi contained no FA.     

Effect of zinc sulphate on gelling properties of phosphorylated protein isolate from yellow stripe trevally

Impacts of zinc sulphate (ZnSO₄) (0–140 μmol/kg) on gel properties of yellow stripe trevally surimi added with sodium tripolyphosphate (STPP) (0.25% and 0.5%, w/w) and protein isolate phosphorylated with STPP at 0.25% and 0.5% (w/w) were studied. Gels from surimi added with 60 μmol ZnSO₄/kg in the absence and presence of 0.5% STPP had the increases in breaking force and deformation by 20.9% and 33.3%, and 11.6% and 18.6%, respectively, compared with the control surimi gel (without additives). Gel of protein isolate phosphorylated with 0.5% STPP containing 100 μmol ZnSO₄/kg had the increases in breaking force and deformation by 14.87% and 5.6%, respectively, compared with the gel from non-phosphorylated protein isolate at the same ZnSO₄ level, suggesting that the phosphorylated protein isolate was more crosslinked by Zn²⁺. The addition of ZnSO₄ at the suitable level lowered the expressible moisture content, but increased whiteness of surimi or protein isolate gels (P < 0.05). Non-covalent bonds, more likely salt bridge and ionic interactions, played a major role in cross-linking of proteins in both surimi and protein isolate added with ZnSO₄, regardless of phosphates incorporated. Microstructure study revealed that a gel having highly interconnected and denser network with smaller voids was formed when protein isolate phosphorylated with 0.5% STPP was added with ZnSO₄ at a level of 100 μmol/kg. Thus, gel with improved properties could be obtained from protein isolate from yellow stripe trevally phosphorylated with STPP in conjunction with addition of ZnSO₄ at an appropriate level.     

Alternative Techniques for Producing a Quality Surimi and Kamaboko from Common Carp (Cyprinus carpio)

ABSTRACT: The demand for surimi and kamaboko is increasing in the world at the same time as the supply of the fish traditionally used has declined. In an effort to increase the range and hence supply of fish used, factors increasing the quality of surimi and kamaboko from common carp were investigated. The best surimi and kamaboko characteristics were produced by a modified conventional method (MCM) rather than traditional method (TM), alkaline‐aided method (AAM), and pH modified method (PMM). MCM processing used centrifugation instead of decanting and filtering to optimize dewatering and remove the sarcoplasmic proteins (Sp‐P). The temperature sweep test, at the end of sol–gel transition stage (at 75 °C), showed significantly (P < 0.05) greater G′ for the kamaboko from MCM than that from other methods tested. Furthermore, the greatest and the least gel strengths were obtained with MCM and TM kamaboko, respectively. The protein recovery was about 67%, 74%, 87%, and 92% for TM, AAM, MCM, and PMM, respectively. TM and MCM resulted in the removal of Sp‐P as determined by SDS‐PAGE. The superiority of MCM kamaboko gel characteristics was supported by scanning electron micrographs (SEM) of the gel, which showed a significantly (P < 0.05) greater number of polygonal structures than for the TM kamaboko, which had the fewest and largest polygonal structures. The pH‐shifting methods improved the textural quality of the resultant kamaboko compared with TM. However, a simple modification (centrifugation compared with decanting) by MCM in the surimi process can further improve the quality of the surimi and kamaboko gels. Furthermore, because it removed Sp‐P and still preserved gel strength, it suggests that Sp‐P are not required for gel strength.     

Viscoelastic behaviour of heat-treated whey protein concentrate suspensions

The viscoelastic behaviour of heat-treated whey protein concentrate (WPC) suspensions was studied. Suspensions with total protein (TP) content of 5% and 9% w/v prepared from a commercial WPC with 38% w/w protein were treated at two temperatures (72.5 and 77.5 °C) during selected times to obtain 60% of denatured protein content. Unheated WPC suspensions were used as control. Frequency sweeps were performed in the range of 0.01–10 Hz at 20 °C. Mechanical spectra of WPC suspensions were similar to viscoelastic fluids. However, unheated WPC suspensions showed some mechanical characteristics of colloidal crystals, like little dependency of elastic (G′) and viscous (G″) moduli with TP content, solid-like mechanical spectra, and difficulty to flow at low content of TP. At a selected frequency of 1 Hz, viscous modulus was more frequency (ω) dependant on experimental conditions (TP and temperature) than elastic modulus. Mechanical spectra were modelled using power law equations (G′ = aω^x, G″ = bω^y), but only parameters of heat-treated WPC suspensions containing 9% of TP showed temperature dependency. Characteristic relaxation times (τ_c) were calculated as the inverse of the crossover frequency, where G″ = G′. Heat treatments produced a decrease in the extent of the elastic behaviour because heat-treated WPC suspensions presented higher phase angle and smaller τ_c values than unheated WPC suspensions for the same TP content. The τ_c decreased when treatment temperature increased but only in heat-treated WPC suspensions with 5% of TP.     

Effect of medium temperature setting on gelling characteristics of surimi from some tropical fish

Effects of setting at 25 °C on textural properties and cross-linking of myofibrillar proteins in surimi produced from threadfin bream (Nemipterus bleekeri), bigeye snapper (Priacanthus tayenus), barracuda (Sphyraena jello) and bigeye croaker (Pennahai macrophthalmus) were investigated. Increase in setting time (0–8 h) resulted in a higher breaking force and deformation for all surimi gels tested (P<0.05). Increased gel strength was associated with increase in non-disulfide bond formation and decreased heavy chain myosin. Proteins underwent degradation during setting; however polymerization occurred to a much higher extent, leading to a strengthened gel matrix. Therefore, setting at 25 °C, for an appropriate time, should be a promising means to improve gelling properties of surimi produced from tropical fish.     

Extreme pH treatments enhance the structure-reinforcement role of soy protein isolate and its emulsions in pork myofibrillar protein gels in the presence of microbial transglutaminase

Alkali (pH₁₂) and acid (pH_1.5) pH-treated soy protein isolates (SPI) were incorporated (0.25–0.75% protein) into sols of myofibrillar protein (MP, 3%, in 0.6 M NaCl at pH 6.25) with or without 0.1% microbial transglutaminase (TG) to investigate the potential as meat processing ingredients. Static and dynamic rheological measurements showed significant enhancements of MP gelling ability by the inclusion of pH_1.5-treated as well as preheated SPI (90 °C, 3 min). A 7-h incubation with TG accentuated the gel-strengthening effect by these SPI samples. The B subunit in 11S of SPI was the main component manifesting structure reinforcement in the mixed gels. The MP gelling properties were also greatly improved (P < 0.05) by the addition of 10% canola oil emulsions stabilized by pH-treated SPI. The principal force in the MP gels incorporated with pH-treated SPI was hydrophobic patches; in the presence of TG, cross-linking of previously dissociated A and B subunits of 11S was also intimately involved.     

Effects of Bambara Groundnut Protein Isolates and Microbial Transglutaminase on Textural and Sensorial Properties of Surmi Gel from Sardine (Sardinella albella)

Effects of different bambara groundnut protein isolates (BGPIs) at a level of 6 % (w/w) in combination with microbial transglutaminase (MTGase) at a concentration of 0.6 U g^?1 surimi on gel properties of sardine (Sardinella albella) surimi were investigated. In the absence of MTGase, all BGPIs showed the adverse effect on gel-forming properties of surimi, as evidenced by the decreases in breaking force and deformation (P?<?0.05). When MTGase was incorporated, the increases in breaking force and deformation were found for all BGPIs used. Water-holding capacity of all gels was improved when BGPIs were added in combination with MTGase (P?<?0.05). Whiteness of gels slightly decreased with the addition of BGPIs; however, MTGase had no impact on whiteness (P?>?0.05). Surimi gel added with BGPI prepared from defatted flour with heat treatment in the presence of ethylenediaminetetraacetic acid (DF-BGPI-HE) and MTGase showed well-ordered network and exhibited the lowest peroxide value and thiobarbituric acid-reactive substances than those containing other BGPIs. Gel containing DF-BGPI-HE had negligible beany flavour. Additionally, DF-BGPI-HE had the lower amount of volatile compounds after storage of 30 days at room temperature than other BGPIs. Thus, the addition of DF-BGPI-HE and MTGase was an effective means to render sardine surimi gel with improved gel property and caused no beany flavour in resulting gel.     

Use of Konjac glucomannan as additive to reinforce the gels from low-quality squid surimi

This paper reports a study of the influence of a Konjac glucomannan aqueous dispersion (KAD) as ingredient, at different alkalinity levels, on the thermal stability of low-quality squid surimi (Dosidicus gigas) and the viscoelastic properties of its gel. An increase in elastic (G^′) and viscous (G^″) moduli at T < 50 °C, reflecting protein aggregation, and a strong decrease at T > 50 °C, reflecting structural damage, were observed in thermal gelation profiles of low-quality squid surimi. The contribution of 1% KAD (10%) to enhancement of gelation ability was assessed by evaluating the viscoelastic properties of the gels, with and without KAD, at increasing alkalinity levels. Gels with KAD at high-pH had the best rheological properties. Small amplitude oscillatory shear (SAOS) tests showed a significant decrease in rigidity, an increase in strain amplitude and a decrease in the frequency-dependence of G^′ and G^″. These results were in agreement with instrumental texture analyses, meaning that KAD may be used to overcome the negative effect of the poor protein functionality of low-quality squid surimi and achieve better gels from them.