CHITOSAN AFFECTS TRANSGLUTAMINASE-INDUCED SURIMI GELATION

Effect of chitosan on barred garfish (Hemiramphus far) surimi gel was studied in the presence of EDTA and microbial transglutaminase (MTGase). An increase in breaking force of surimi gels added with 1.0% prawn shell chitosan indicated the gel enhancing effect of chitosan on the heat‐induced gelation of fish myofibrillar proteins. However, gel‐forming ability of surimi containing chitosan was inhibited in the presence of EDTA, especially at higher concentration. Therefore, the enhancing effect of chitosan was possibly mediated through the action of endogenous transglutaminase (TGase) during setting, resulting in the formation of protein‐protein and protein‐chitosan conjugates. In general, addition of MTGase remarkably increased both breaking force and deformation of surimi gel (P<0.05). However, enhancing effect of MTGase was retarded in the presence of chitosan, resulting in lower magnitude of breaking force and deformation (P<0.05). Scanning electron microscopy showed that chitosan particles were uniformly dispersed in the gel matrix. A tightly associated gel network was formed in surimi containing MTGase, whereas a large number of voids were noted in gels with EDTA. These results suggest that chitosan acted as a surimi gel enhancer in combination with endogenous TGase in fish muscle, but hindered gel formation in the presence of MTGase.     

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.     

Whey protein concentrate: Autolysis inhibition and effects on the gel properties of surimi prepared from tropical fish

Effects of whey protein concentrate (WPC) on autolysis inhibition and gel properties of surimi produced from bigeye snapper (Priacanthus tayenus), goatfish (Mulloidichthys vanicolensis), threadfin bream (Nemipterus bleekeri) and lizardfish (Saurida tumbil) were investigated. WPC (0–3%) showed inhibitory activity against autolysis in all surimi at both 60 and 65 °C in a concentration-dependent manner. Myosin heavy chain (MHC) of surimi was more retained in the presence of WPC. Breaking force and deformation of kamaboko gels of all surimi increased as added levels of WPC increased (P < 0.05). This was associated with lower levels of protein degradation, as evidenced by the decrease in trichloroacetic acid-soluble peptide content (P < 0.05). WPC at 3% (w/w) significantly decreased the whiteness of gels. However, water-holding capacity of kamaboko gels was improved with increasing concentration of WPC. The microstructure of surimi gels generally became denser with the addition of WPC.     

Effect of antioxidants in combination of VCO nanoemulsion on gel properties and storage stability of refrigerated sardine surimi gel

Impacts of β-glucan–virgin coconut oil (VCO) nanoemulsion containing epigallocatechin gallate (EGCG) and α-tocopherol at levels of 0–3.0 g kg⁻¹ on properties and storage stability of surimi gel were investigated. Augmented breaking force, deformation and fracture constant were obtained in gels containing 2.0 g kg⁻¹ EGCG or 1.0 g kg⁻¹ α-tocopherol (P < 0.05). Expressible moisture content increased as EGCG levels were more than 2.0 g kg⁻¹. Smoother microstructure was observed in gels containing 2.0 g kg⁻¹ EGCG. Whiter gels were obtained when β-glucan–VCO nanoemulsion was incorporated. No change in protein pattern of gels was observed regardless of antioxidant incorporation. Viscoelastic moduli decreased as β-glucan–VCO nanoemulsion was added; however, incorporation of 2.0 g kg⁻¹ EGCG or 1.0 g kg⁻¹ α-tocopherol lowered the decrease in G'. β-glucan–VCO nanoemulsion containing gels had higher likeness scores than the control (P < 0.05). Gels containing EGCG and α-tocopherol at selected levels had the improved oxidative stability and lowered microbial loads.     

Impact of lecithin incorporation on gel properties of bigeye snapper (Priacanthus tayenus) surimi

Gelling characteristics of bigeye snapper (Priacanthus tayenus) surimi functionalised by lecithin at different concentrations were investigated. Lecithin at ≤1 g 100 g⁻¹ had no impact on breaking force and deformation (P > 0.05). Expressible drip tended to decrease with increasing lecithin level up to 1 g 100 g⁻¹. Lecithin at 1–3 g 100 g⁻¹ improved the whiteness (P < 0.05). Jointed clusters were formed in the gel microstructure with 1 g 100 g⁻¹ lecithin. Gel without and with 1 g 100 g⁻¹ lecithin had the same texture profile and likeness scores (texture, odour and flavour) (P > 0.05). Peroxide value, TBARS content and rancid odour score of gels were changed considerably during refrigerated storage (4 °C/polyethylene bag) for 15 days but lower values of all indices were noticeable in gel with lecithin. Therefore, lecithin at 1 g 100 g⁻¹ was the optimum concentration for stabilising the texture, improving the water holding capacity, whitening the colour and retarding the lipid oxidation of bigeye snapper surimi gel.     

Effects of CaCl<Subscript>2</Subscript> on chemical interactions and gel properties of surimi gels from two species of carps

Effects of CaCl₂ on chemical interactions, textural properties and expressible moisture content of suwari and kamaboko gels from yellowcheek carp and grass carp were investigated. And the correlations between the contents of chemical interactions and physical properties of surimi gels were analyzed. The contents of chemical interactions, especially non-disulfide covalent bonds, disulfide bonds and hydrophobic interactions of suwari and kamaboko gels, varied with addition concentration of CaCl₂ and fish species. Suwari and kamaboko gels from yellowcheek carp exhibited higher breaking force, deformation and gel strength than these from grass carp. Surimi gels (suwari and kamaboko gels) from yellowcheek carp and grass carp exhibited their maximum gel strength when 40 mmol/kg and 100 mmol/kg CaCl₂ was added, respectively. Addition of CaCl₂ at high concentration resulted in low water holding capacity of surimi gels. Correlation analysis indicated that the contents of nonspecific associations, ionic bonds, hydrophobic interactions and sulfhydryl groups exhibited significant correlation with breaking force of surimi gels from yellowcheek carp and grass carp. Additionally, the content of non-disulfide covalent bonds had significant positive correlations with breaking force and expressible moisture of surimi gel from yellowcheek carp.     

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.     

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.     

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.     

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.     

Physicochemical properties, gel-forming ability and myoglobin content of sardine (Sardinella gibbosa) and mackerel (Rastrelliger kanagurta) surimi produced by conventional method and alkaline solubilisation process

Characteristics and gel properties of sardine and mackerel surimi produced by conventional washing process and alkaline solubilising process were investigated. The decrease in Ca²⁺-ATPase activity with the changes in the surface hydrophobicity was found in surimi produced by alkaline solubilising process (p<0.05), suggesting the denaturation of protein induced by this process. The alkal-ine solubilising process with prewashing could remove myoglobin most effectively from sardine muscle, whereas the process without prewashing resulted in the greatest myoglobin removal in mackerel muscle (p<0.05). Surimi conventionally prepared by water or NaCl washing showed the gel with greater breaking force and deformation than that from alkaline solubilising process (p<0.05). The hig-her expressible moisture was found in the gels of surimi pre-pared by alkaline process, indicating the poor water holding capacity of the gel matrix. The highest whiteness was found in the gel of sardine surimi produced by alkaline process with prewashing but the highest whiteness was obtained in the gel of mackerel surimi washed with distilled water.     

Comparative study on protein cross-linking and gel enhancing effect of microbial transglutaminase on surimi from different fish

BACKGROUND: Microbial transglutaminase (MTGase) has been used to increase the gel strength of surimi. Nevertheless, its effectiveness varies with fish species. The aim of this study was to elucidate the effect of MTGase at different levels on protein cross‐linking and gel property of surimi from threadfin bream, Indian mackerel and sardine in the presence and absence of endogenous transglutaminase. RESULT: Breaking force of all surimi gels increased as MTGase levels (0–0.6 U g^?1) increased except for threadfin bream surimi gel, where the breaking force decreased at 0.6 U g^?1 (P < 0.05). In the presence of EDTA, the gel strengthening effect was lower, suggesting the combined effect of endogenous transglutaminase with MTGase. With the addition of MTGase, the gel with the highest increase in breaking force showed highest decrease in myosin heavy chain. When cross‐linking activity of MTGase on natural actomyosin (NAM) was determined, the highest decreasing rate in ε‐amino group content with the concomitant increased formation of cross‐linked proteins was found in NAM from threadfin bream. The reactivity of muscle proteins toward MTGase‐induced cross‐linking was in agreement with surimi gel strengthening. CONCLUSION: The composition and properties of muscle proteins of varying fish species more likely determined protein cross‐linking induced by MTGase, thereby affecting their gel properties. Copyright © 2011 Society of Chemical Industry     

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.     

Effects of vegetable oils on gel properties of surimi gels

The objective of this study was to determine effects of vegetable oils (soybean, peanut, corn, and rap oils) on the textural, color, microstructural, sensory and rheological properties of surimi gels. As the vegetable oil concentration increased in surimi gels, breaking force of gels was decreased (P < 0.05), while expressible water and whiteness values were increased (P < 0.05). Surimi gels with peanut oil had higher breaking force values, comparing to those with other vegetable oils. Transmission electron microscope shows the similar-size droplets of peanut oil and corn oil in surimi gels. Sensory evaluation indicated that fish balls with 10 g/kg vegetable oils were accepted in term of taste, color and overall likeness by the panelists. Storage modulus (G′) and loss modulus (G″) decreased along with increasing vegetable oil concentration. Results demonstrated that vegetable oils could be used potentially to modify the qualities of surimi-based products, such as color and taste.     

Effect of phosphate compounds on gel-forming ability of surimi from bigeye snapper (Priacanthus tayenus)

The properties of surimi gel from bigeye snapper (Priacanthus tayenus) added with various phosphate compounds (sodium pyrophosphate, PP; sodium tripolyphosphate, TPP; and sodium hexametaphosphate, HMP) at different levels (0%, 0.05%, 0.1%, 0.3% and 0.5% w/w) and heated under various conditions were studied. Kamaboko and directly heated gels from bigeye snapper surimi added with 0.05% PP had the increase in breaking force and deformation by 17.35% and 11.52%, and 13.54% and 3.53%, respectively, compared with the control gel (without PP addition). At the same level used (0.05%), TPP had no influence, but HMP exhibited a detrimental effect on kamaboko gel. The addition of PP (0.025%) in combination with 50 mmol CaCl₂/kg increased the breaking force by 38.68% as compared with the control gel (without additives), suggesting that the sufficient amount of CaCl₂ could enhance the setting of the gel. Generally, the marked decrease in breaking force with the coincidental increased expressible moisture was observed when the excessive amount of phosphate compounds was used (p<0.05). Microstructure study revealed that a gel with a fine network was formed with addition of PP. Therefore, the addition of PP in combination with CaCl₂ could increase the gel strength as well as water holding capacity of surimi gel.     

ɛ-POLYLYSINE IMPROVES THE QUALITY OF SURIMI PRODUCTS

To apply ɛ-polylysine (PL) as a natural food preservative for the preparation of surimi products, effects of added PL on the textural properties and shelf-life of kamaboko gels were investigated. Kamaboko gels were prepared by setting at 30C for 1 h, then heating at 80C for 20 min. Breaking force and breaking strain of kamaboko gels increased slightly with increasing PL concentration up to 0.2% and decreased at 0.4%. However, the protein subunit component composition of kamaboko gels did not vary with the amount of PL added, indicating that PL did not promote the polymerization of myosin heavy chain. The increased pH value of surimi to around 7.6 as the result of the incorporation of 0.2% PL was found to be attributable to the increased textural properties of kamaboko gels. The shelf-life of kamaboko gels was significantly extended by the addition of 0.2% PL in surimi, especially at 5C and 10C storage.     

Thermal Gel Degradation (Modori) in Sturgeon (Acipenseridae) Surimi Gels

Sturgeon meat has been found to be suitable as surimi raw materials. The present study determined the modori phenomenon in sturgeon surimi gels and identified its relationship with cathepsins. In all heat‐treated gels (25 to 90 °C, at 5 °C intervals), the 40 °C‐incubated sturgeon surimi gel showed the weakest gel properties and water‐holding capacity (P < 0.05), a rough protein gel network under SEM, and the highest protein solubility and trichloroacetic acid‐soluble peptides content (P < 0.05). SDS‐PAGE indicated that the myosin heavy chain band of sturgeon surimi gels was almost completely degraded at 40 °C. Moreover, the highest cathepsin L activity was observed in 40 °C‐treated sturgeon surimi gels (P < 0.05). Our results suggested that the modori phenomenon in sturgeon surimi gels occurred at 40 °C, which was partially attributed to cathepsin L, thereby allowing for the better exploitation and utilization of sturgeon surimi.     

Effect of high-temperature setting on gelling characteristic of surimi from some tropical fish

The effect of setting at 40 °C on the textural properties and the changes in myofibrillar proteins in surimi produced from threadfin bream (Nemipterus bleekeri), bigeye snapper (Priacanthus tayenus), barracuda (Sphyraena jello) and bigeye croaker (Pennahai macrophthalmus) was investigated. An increase in the time of setting generally resulted in higher breaking force and also the deformation of both suwari and kamaboko gels. Maximum increases in gel‐breaking force were obtained in 1 h for threadfin bream, 2 h for bigeye snapper, 1.5 h for barracuda and 3 h for bigeye croaker. Extended setting time caused decreases in breaking force and deformation in all surimi, except that produced from bigeye croaker. Gel strengthening was associated with an increase in non‐disulphide covalent bond formation. Degradation of proteins occurred with prolonged setting. Therefore, setting at 40 °C for an appropriate time is a promising means to improve the gelling property of surimi produced from tropical fish.     

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.     

GEL PROPERTIES OF BIGEYE SNAPPER (PRIACANTHUS TAYENUS) SURIMI AS AFFECTED BY SETTING AND PORCINE PLASMA PROTEINS

Effects of setting temperature, time, and addition of porcine plasma protein (PPP) on gel properties of surimi from bigeye snapper (Priacanthus tayenus) were investigated. Breaking force and deformation of the surimi gels increased as the setting time and temperature increased. The gel preincubated at 35C for 90 min in the presence of 0.5% PPP, followed by cooking at 90C for 20 min showed the maximum force and deformation. The decrease in solubility of the resultant suwari and kamaboko gels in solution containing sodium dodecyl sulfate, urea and β‐mercaptoethanol suggested that gel enhancement was mainly mediated through the formation of nondisulfide covalent bonds catalyzed by both transglutaminase (TGase) in fish muscle and porcine plasma. Addition of PPP slightly decreased the whiteness of the kamaboko gels.