Influence of texture of suwari gels on kamaboko gels made from sardine (Sardina pilchardus) surimi

The textural characteristics and water holding capacity of suwari (set) and kamaboko (set and cooked) sardine surimi gels were examined in order to clarify the influence of the initial network formed in setting conditions (25, 35 and 40°C for 30 and 60 min) on the texture of the kamaboko gels. Although the texture of suwari gels set at 35°C improved with longer setting, both setting times ensured kamaboko gels with the highest gel strength. Suwari gels set at 25°C also improved with longer setting but the gel strength of both suwari and kamaboko gels was lower than at 35°C. For gels set at 40°C prolonged setting weakened the suwari networks formed, leading to kamaboko gels with poorer textural characteristics. ©1997 SCI     

The Pepsin Digestibility of Thermal Gel Products Made from White Croaker (Pennahia argentata) Muscle in Associating with Myosin Polymerization Levels

Thermal gels were made from white croaker (Pennahia argentata) surimi at various polymerization levels of myosin heavy chains induced by suwari treatment at 38 °C for various time periods and subsequently heated at 85 °C for 20 min. Myosin heavy chain polymerization levels were also achieved in the presence of microbial transglutaminase (MTG) added at various concentrations in the surimi. The breaking strength and breaking strain rate were markedly increased during suwari treatment up to 60 min in accordance with the increased levels of myosin heavy chain polymerization. MTG enhanced myosin heavy chain polymerization during suwari treatment for 15 and 30 min, resulting in the increase of breaking strength. The solubilization in 8 M urea and pepsin digestibility of these gels as well as angiotensin I‐converting enzyme (ACE) inhibitory activity of their pepsin digests were decreased with the increased levels of myosin heavy chain polymerization. These results suggest that myosin heavy chain polymerization affects not only rheological properties of thermal gels but also their functional properties for human health.     

Effect of soy protein isolate on gel properties of Alaska pollock and common carp surimi at different setting conditions

The effects of soy protein isolate (SPI) on the gel properties of different grade Alaska pollock and common carp surimi at different setting conditions were evaluated and compared. Breaking force and distance of gels decreased with increasing SPI concentrations in direct cook (85 °C for 30 min) and in cook after setting at 30 °C for 60 min conditions. The effect of SPI on gel strength of common carp surimi was less than in Alaska pollock surimi. The breaking force obtained for addition of 10% SPI to Alaska pollock surimi was higher than for surimi alone when cooked after incubation at 50 °C for 60 min. Addition of SPI decreased the whiteness and increased the yellowness of the gel. The gel structure showed that the addition of SPI modified the microstructure of the fish protein gel, thus resulting in surimi with different gelling properties. Copyright © 2004 Society of Chemical Industry     

Enhancement of the Gelation Properties of Surimi from Yellowtail Seabream (Parargyrops edita,Sparidae) with Chinese Oak Silkworm Pupa,Antheraea pernyi

In this study, the textural properties and micromechanism of yellowtail seabream (Parargyrops edita, Sparidae) surimi, with and without Chinese oak silkworm pupa homogenate (SPH), were investigated at different levels. The fresh, freeze‐dried, and oven‐dried SPH all showed a gel‐enhancing ability in suwari (40/90 °C) and modori (67/90 °C) gels, in a concentration‐dependent manner. Though the drying treatments can improve the storability of SPH, compared with fresh, the effect of the active substance was weakened. Suwari and modori gels added with 5%(w/w, whole product) fresh SPH had the increase in breaking force and deformation by 37.39% and 47.98%, and 85.14% and 78.49%, respectively, compared with the control gel (without SPH addition). The major myofibrillar protein, especially myosin heavy chain (MHC), was better retained by the addition of SPH. Compared the control group, a finer, denser, and more ordered 3‐dimensional gel network microstructure was obtained, and different Df (Fractal dimension) was analyzed by using the box count method. This was found in all samples from 2.838 to 2.864 for suwari gels and 2.795 to 2.857 for modori gels, respectively. Therefore, the modori of yellowtail seabream surimi, linked with endogenous proteases, could be retarded in the presence of SPH, leading to an increase in gel strength.     

Gel Forming Characteristics of Frozen Surimi from Chum Salmon in the Presence of Protease Inhibitors

When salted surimi paste of chum salmon was incubated at 20–60°C, a marked loss of the breaking strength of heat-induced gel occurred simultaneously with breakdown of myosin heavy chain, but this was effectively suppressed by addition of cysteine protease inhibitors or bovine plasma powder. In the presence of protease inhibitor, the surimi gels were formed at relatively low temperatures showing highest gel strength at incubations of 50 and 60°C. Chum salmon surimi showed no evidence of suwari and no myosin heavy chain cross-linking.     

Thermal stability of myofibrillar protein from Indian major carps

The characteristics and stability of natural actomyosin (NAM) from rohu (Labeo rohita), catla (Catla catla) and mrigal (Cirrhinus mrigala) were investigated. The total extractable actomyosin (AM) was higher (7.60 mg ml^?1) in the case of rohu compared with that from catla and mrigal (5 mg ml^?1). Although the specific AM ATPase activity was similar (0.43–0.5 µmol P min^?1 mg P^?1) among the three species, the total ATPase activity was lower in mrigal (25 µmol g^?1 meat) compared with the other species (37 µmol g^?1 meat). The inactivation rate constants (k_d) of AM Ca ATPase activity showed differences in the stabilities of actomyosin among these fish, the actomyosin from catla being least stable. The NAM from these species was stable up to 20 °C at pH 7.0. Catla AM became unstable at 30 °C, while rohu and mrigal AM could withstand up to 45 °C. The thermal denaturation with respect to solubility, turbidity, ATPase activity, sulphhydryl group and surface hydrophobicity showed noticeable changes at around these temperatures. Copyright © 2004 Society of Chemical Industry     

Gel‐forming ability of surimi from grass carp (Ctenopharyngodon idellus): influence of heat treatment and soy protein isolate

The effects of setting conditions and soy protein isolate (SPI) on textural properties of surimi produced from grass carp were investigated. Effects of setting temperature, setting time and protein concentration on the breaking force and distance were evaluated and compared utilizing response surface methodology. Models for breaking force and breaking distance of grass carp surimi were established. Protein concentration was the major factor affecting the gel strength of grass carp surimi. Breaking force and distance of grass carp surimi gels decreased with increase of protein ratio from SPI at 30 °C and 40 °C for 60 min setting and heating at 85 °C for 30 min, but the breaking force obtained for addition of 100 g kg^?1 SPI protein to grass carp surimi was higher than that for surimi alone at 60 °C for 60 min incubation and heating at 85 °C for 30 min. Copyright © 2005 Society of Chemical Industry     

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.     

Sardine Surimi Gels as Affected by Salt Concentration, Blending, Heat Treatment and Moisture

The effects of simultaneous modification of salt concentration, blending time, moisture content and heat treatment at different setting and cooking temperatures and time on characteristics of sardine (Surdina pilchardus) surimi gels was examined using a randomized incomplete block design. Maximum gel strength (GS) was obtained at highest salt concentrations and 78% moisture. Pre-setting was required to achieve acceptable gel quality. Highest GS values were found in gels set for 30–60 min at 35°C prior to heating at 90°C for 40 min. However, GS decreased after prolonged heating at 90°C. Gels set at 25, 35 and 40°C for 90 min had lower GS values when heated at 90°C for 40 min but were stable during further heating.     

Strength of Gels Prepared from Washed and Unwashed Minces of Hoki (Macruronus novaezelandiae) Stored in Ice

Washed and unwashed fish minces were prepared from hoki that had been stored in ice. Gels were formed from the minces, cooked at both 60°C and 90°C and assessed by puncture, torsion and a folding test method. The strength of the gels decreased as the fish were stored. However, after 10 days, the strength of gels made from hoki minces still compared favorably with gels made from other commercial fish species without storage. This suggests that manufacture of hoki surimi on-shore may be practical. Fish freshness as evaluated by sensory methods was closely related to the K value and gel strength. Hence K values might provide the basis of a raw material quality control system for an on-shore surimi plant.     

Thermal Gel Degradation (Modori) in Sardine Surimi Gels

Sardine (Sardina pilchardus) surimi gels set (50°C or 60°C), or set and cooked (50°C or 60°C + 90°C) for different times were studied in order to evaluate modori (thermal gel degradation). The texture data of the set gels were similar to data obtained previously in gels set at lower temperature that produced good kamaboko gels. However, in gels set at 50°C and 60°C modori occurred upon cooking. Microscopically the set gels exhibited globular aggregated structures that became more compact when modori occurred. Results suggested that at modori temperature protein-protein bonding caused massive protein coagulation preventing the formation of a fibrillar matrix upon cooking.     

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.     

Original article: Gel properties of red tilapia surimi: effects of setting condition,fish freshness and frozen storage

This study aimed to determine effects of setting condition, fish freshness and storage time of frozen surimi on properties of red tilapia surimi gel. To investigate the effect of setting condition, a combination of eight setting temperatures (35–70 °C) and four setting times (30–120 min) was used. Maximum breaking force, deformation and gel strength were obtained after the gel had been set at 40 °C for 90 or 120 min. Setting at 65 °C resulted in the lowest obtained gel strength, because of proteolytic degradation of myosin heavy chain. Increasing storage time of raw fish material in ice caused a significant decrease in gel strength of the resultant surimi gel (P < 0.05). Gels produced from surimi kept in frozen storage for up to 9 months also exhibited reduced gel strength, with a concomitant increase in the expressible drip, with increasing storage time (P < 0.05).     

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.     

Microstructure of suwari and kamaboko sardine surimi gels

In a previous work it was suggested that the texture of kamaboko (set and cooked) gels made from sardine surimi under varying setting conditions was predetermined by the specific matrix forming in each suwari (set) gel. This paper describes the microstructure of the networks formed in suwari and kamaboko gels set at 25, 35 and 40 °C for 30 or 60 min as examined by scanning electron microscopy (SEM). Cooking conditions for kamaboko gels were fixed at 90 °C for 30 min; other preparation conditions were invariable. At low magnification (≤×500) the gel matrixes were compact, with practically no differences among lots. At higher magnification (×20 000), the suwari gel matrixes formed at low temperature consisted of globules. At higher temperatures the globules joined up to form fibrillar structures (fibres) and zones of disordered globule aggregation (coagula); at longer setting times, lateral bonding of the fibres became apparent. Kamaboko gels produced from unstructured globular matrixes exhibited only a few fibrillar zones and large areas of coagula. Where there was already an incipient fibrous formation, these developed into individual fibres or bundles of fibres that correlated with the best texture characteristics. Suwari gels with extensive lateral bonded fibres gave rise to kamaboko gels with a highly compact appearance under SEM; this correlated with a decline in texture values. These different structures suggest that the protein–protein bonds in the suwari networks have different levels of stability to heat, and these levels determine whether or not the proteins can subsequently be reorganised when the kamaboko gel forms. © 1999 Society of Chemical Industry     

High Pressure Effects on Gelation of Surimi and Turkey Breast Muscle Enhanced by Microbial Transglutaminase

High pressure effects on the strength (stress) and elasticity/deformability (strain) of surimi and turkey breast meat gels containing microbial transglutaminase (TGase) were evaluated. Pressurization of muscle proteins at 4°C prior to incubation at 25°C or 40°C (setting) increased gel strength 2–3 fold in uncooked surimi gels, but not in uncooked turkey gels. However, pressurization at 40°C or 50°C prior to setting increased the strength of turkey gels. Similar effects of prior pressurization, but of lesser magnitude, occurred in gels formed by directly or subsequently (following setting) cooking at 90°C. SDS-PAGE confirmed that myosin crosslinking occurred due to TGase activity during the setting treatment, which had survived prior pressure treatment. High pressure rendered protein substrates more accessible to TGase thereby enhancing intermolecular cross-link formation and gel strength.     

Effect of preheating temperature on the microstructure of walleye pollack surimi gels under the inhibition of the polymerisation and degradation of myosin heavy chain

BACKGROUND: The physical attribute of heat‐induced gel texture is highly dependent on the microstructure of the gel. In this study the microstructures of walleye pollack surimi gels preheated at various temperatures with and without inhibitors (ethylenediamine‐N,N,N′,N′‐tetraacetic acid, iodoacetamide and leupeptin) were observed with a natural scanning electron microscope. RESULTS: Without inhibitors, gels preheated at 30 °C showed a fine and uniform network structure together with the highest polymerisation of myosin heavy chain (MHC) and the highest gel strength. At 60 °C, gels exhibited a broken, disrupted and loose cluster‐like structure together with the highest degradation of MHC and the lowest gel strength. Under the inhibition of polymerisation and degradation of MHC a fine network was observed up to 40 °C during preheating. However, after a second step of heating at 80 °C the microstructures were disrupted and resembled each other regardless of the preheating temperature. CONCLUSION: Heat‐induced gel formation is related to the polymerisation and degradation of MHC and the microstructure of the gel during preheating. Gelation occurred during setting even under the inhibitory condition, and the formation of covalent bonding by transglutaminase is not essential to the formation of a three‐dimensional network during setting but is essential to the gel strength enhancement effect of setting by subsequent heating at 80 °C. Copyright © 2010 Society of Chemical Industry     

Gel Properties of Surimi from Bighead Carp (Aristichthys nobilis): Influence of Setting and Soy Protein Isolate

ABSTRACT: The effects of setting conditions and soy protein isolate (SPI) on textural properties and microstructures of surimi produced from bighead carp were investigated. The incubation conditions of bighead carp surimi affected the breaking force and distance. The optimum setting conditions were 35 °C to 40 °C for 60 min. When the surimi was cooked after 50 °C incubation for 30 to 120 min, the breaking force and distance were inferior to that of no incubation. The gel structure showed that the incubation conditions affected the bighead carp surimi gel microstructures, thus producing surimi with different gelling properties. Breaking force and distance of surimi gels decreased when the protein ratio of SPI was increased in the total protein at 30 °C and 40 °C for 60 min setting and heating at 85 °C for 30 min, but the breaking force obtained for 90% surimi protein plus 10% SPI protein was higher than surimi alone at 50 °C for 60 min incubation and heating at 85 °C for 30 min.     

Combined Effect of High Hydrostatic Pressure and Lysine or Cystine Addition in Low-Grade Surimi Gelation with Low Salt Content

The aim of this study was to reduce the sodium chloride (NaCl) level in surimi-based products by adding lysine or cystine in combination with high hydrostatic pressure (HHP). For experiments, Alaska pollock surimi was used to prepare gels in a factorial design (3?×?3?×?2) using three additive levels (no additive, lysine, and cystine), three NaCl levels (0, 0.3, and 3 %), and two HHP levels (0 and 300 MPa/10 min/10 °C). After blending, the pastes, consisting of surimi, additives, and different levels of salt, were stuffed into casings, high pressure treated, and stored at 5 °C for 24 h (suwari gel). Subsequently, samples were heated at 90 °C for 30 min (kamaboko-type gel). To assess the degree of protein denaturation prior to gelation at 90 °C, suwari gels were analyzed by differential scanning calorimetry to determine myosin denaturation enthalpy. Kamaboko-type gels were characterized by lightness properties, water binding capacity, and mechanical properties (by puncture test). Results showed that the pressure treatment at 300 MPa and/or the addition of lysine or cystine (0 and 0.1 %) to low-sodium-chloride samples (0 and 0.3 %) resulted in gels with similar quality characteristics to those with the regular 3 % sodium chloride addition, most likely due to the protein unfolding induced by both HHP treatment and the additives used.     

NONDISULFIDE COVALENT CROSS-LINKING OF MYOSIN HEAVY CHAIN IN “SETTING” OF ALASKA POLLOCK AND ATLANTIC CROAKER SURIMI1

ABSTRACT Myosin heavy chain (MHC) content of cooked gels of pollock and croaker surimi decreased during preincubation (“setting”) at temperatures ranging from 4–50C. Decreases in MHC content were attributed to either nondisulfide covalent cross-linking or proteolysis. Depending upon which process dominated at a given temperature, formation of stronger or weaker gels occurred, respectively. Maximum production of cross-linked polymers occurred at the optimum setting temperatures, i.e., at 25C for pollock surimi and 40C for croaker surimi. Subsequent cooking of these set gels at 90C decreased the amount of cross-linked polymers formed at the optimum setting temperature. Addition of free lysine-HCl inhibited formation of cross-linked polymers of MHC during setting and the increase in cooked gel strength for both species. This supports published evidence that cross-linking of MHC during setting may be of the ε-amino-(γ-glutamyl) lysine I type, mediated by a transglutaminase enzyme.