Effect of reducing agents on physicochemical properties and gel-forming ability of surimi produced from frozen fish

Effects of different reducing agents (cysteine, ascorbic acid and sodium bisulfite) at various levels on physicochemical properties of protein, transglutaminase activity and gel properties of surimi produced from frozen croaker, lizardfish, threadfin bream and bigeye snapper were studied. Addition of cysteine resulted in the highest increase in the breaking force and the deformation of surimi gels, compared with other reducing agents. The optimum levels of cysteine were 0.05, 0.1, 0.05 and 0.1% (w/w) for surimi from frozen croaker, lizardfish, threadfin bream and bigeye snapper, respectively. Surimi from frozen croaker with cysteine added showed a similar breaking force and deformation to that produced from fresh fish. With addition of cysteine, an increase in sulfhydryl content with a concomitant decrease in disulfide bond content was generally observed. Ca²⁺ ATPase activity also increased, indicating the renaturation of the myosin molecule. T_max of peak 1 (myosin peak) of all surimi sols in the presence of cysteine was shifted to higher temperature. The increased transglutaminase activity was observed with addition of cysteine. Therefore, reducing agents, especially cysteine, recovered the denatured muscle proteins and activated the transglutaminase in the muscle, leading to the increased gel-forming ability of surimi produced from frozen fish.     

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.     

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.     

Characteristics and gel properties of muscles from sardine (Sardinella gibbosa) and mackerel (Rastrelliger kanagurta) caught in Thailand

Dark and ordinary muscle from sardine (Sardinella gibbosa) and mackerel (Rastrelliger kanagurta) were characterized. Lipid and myoglobin contents were higher in dark muscle than in ordinary muscle of both species, and higher contents of both constituents were found in sardine muscle than mackerel muscle. The extractable myoglobin contents in sardine dark and ordinary muscle were 14.27 and 2.18 mg/g, while mackerel dark and ordinary muscle contained 4.88 and 1.37 mg myoglobin/g sample, respectively. Alkali-soluble protein and stroma contents were greater in dark muscle than ordinary muscle. Mackerel muscle comprised a higher content of non-protein nitrogenous compounds than sardine muscle. The effect of washing conditions on the myoglobin extractability was investigated. A large amount of myoglobin was removed in the first washing cycle and only a small amount was removed in the second washing cycle. The highest removal of myoglobin from sardine (32.10–46.55%) and from mackerel muscle (103.20–313.66%) was achieved when the mince was washed with 0.2% NaCl and 0.5% NaCl, respectively. Washing media showed the marked effect on the color, expressible drip and textural properties of sardine and mackerel mince gels. The breaking force of directly heated and kamaboko gels from both sardine and mackerel mince washed with NaCl solution was higher than that of unwashed mince and water washed mince. However, no difference in deformation was observed. Washing also resulted in increased whiteness and lowered expressible moisture. In general, sardine surimi showed the superior gel-forming ability and whiteness to mackerel surimi.     

Monoclonal antibody-based enzyme immunoassay for detection of porcine plasma in fish surimi

Detection of porcine plasma using indirect ELISA was developed using mAb B4E1 for the prevention of their usage in human food that creates religious and health conflicts. The immunoassay has a CV < 20% and did not cross-react to other meat and non-meat proteins. The sensitivity of the assay is 0.25% (w/w) of porcine plasma in spiked raw and cooked fish surimi. The assay did not produce a false positive result for any of the commercial fish surimi tested that were not contain porcine plasma. Determination of a 60-kDa antigenic protein of porcine blood using Western blot confirmed its presence in the plasma fraction of the porcine blood. Further proteomic analysis involving liquid chromatography–tandem mass spectrometry (LC-MS/MS) revealed the 60-kDa protein to be porcine serum albumin.     

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.     

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.     

Effect of oxidised phenolic compounds on the gel property of mackerel (Rastrelliger kanagurta) surimi

The effects of different oxidised phenolic compounds (ferulic acid, OFA; tannic acid, OTA; catechin, OCT and caffeic acid, OCF) at different levels (0-0.60% of protein content) on the properties of gels from mackerel (Rastrelliger kanagurta) surimi were investigated. Gels with addition of 0.40% OFA, 0.50% OTA, 0.50% OCF or 0.10% OCT had increases in breaking force by 45%, 115%, 46.1% and 70.3% and in deformation by 12.2, 27.5, 28.1 and 28.4%, respectively, compared with the control (without addition of oxidised phenolics). Lowered expressible moisture content without any change in the whiteness of resulting gels was found. Slightly lower myosin heavy chain (MHC) band intensity of gels added with oxidised phenolics at the optimal level was noticeable compared with that of the control. A sensory evaluation study indicated that addition of oxidised phenolic compounds had no negative impact on the colour and taste of the resulting gels (P > 0.05). Gels with addition of all oxidised phenolics had a finer matrix with smaller strands.     

Effect of oxidised tannic acid on the gel properties of mackerel (Rastrelliger kanagurta) mince and surimi prepared by different washing processes

Effect of oxidised tannic acid (OTA) at different levels (0, 0.25, 0.50 and 0.75% of protein content) on the gel properties of mackerel (Rastrelliger kanagurta) mince and surimi prepared by different washing processes was investigated. Breaking force and deformation of gels varied with washing processes and concentrations of OTA. The gel of alkaline-saline washing process surimi (ASWPS) added with 0.25% OTA had the increases in breaking force and deformation by 166.2 and 45.9%, respectively, compared with that of conventional washing process surimi (CWPS) without OTA addition. Those increases were associated with the lowered expressible moisture content. Electrophoretic studies revealed that the greater polymerisation was found in ASWPS added with 0.25% OTA. Slight retention of myosin heavy chain (MHC) with lowered trichloroacetic acid (TCA) soluble peptide contents was observed in ASWPS gel added with 0.25% OTA, suggesting the decreased degradation induced by indigenous proteases. The microstructure of ASWPS gels became more ordered, compact and denser with the addition of 0.25% OTA. The use of OTA in conjunction with alkaline-saline washing process could improve the properties of gel from mackerel surimi without adverse effect on sensory properties.     

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.     

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.     

鱼种和亲水胶体对鱼糜制品凝胶性质的影响

考察了添加复合亲水胶体对鲢鱼、带鱼、金线鱼等鱼糜制品凝胶特性的影响。结果发现,添加亲水胶体后,带鱼鱼糜制品凝胶强度从58.38 g·cm提高至107.27 g·cm,金线鱼鱼糜制品从328.68 g·cm下降至137.55 g·cm,但鲢鱼鱼糜制品没有明显变化。另一方面,添加亲水胶体后鱼糜制品的硬度、粘结性、咀嚼性等发生下降,但水分含量、持水性、蒸煮吸水率均有显著提高。而且,添加亲水胶体后带鱼鱼糜制品中肌球蛋白重链的降解受到一定的抑制。SEM结果发现亲水胶体可以填充到带鱼和鲢鱼鱼糜制品中,但在金线鱼鱼糜凝胶结构中容易形成胶体块状,导致凝胶强度下降。      

Cold storage of porcine plasma treated with microbial transglutaminase under high pressure. Effects on its heat-induced gel properties

The objective of this work was to study the heat-induced gelling properties, at acid pH, of porcine plasma previously treated with microbial transglutaminase (MTGase) under high pressure (HP), when kept under refrigeration conditions for different times (setting time). The results indicated that, although the cross-linking activity of MTGase was enhanced under pressure, consequently, improving the thermal gel texture, the most significant effects, particularly on gel hardness, were obtained by keeping the treated plasma solutions under refrigeration for at least 2 h before gelation. On the whole, under such conditions, increases of approximately 60% of this textural parameter, calculated on the basis of the values corresponding to the heat-induced non-treated plasma gels at pH 5.5, were achieved. However, from the SDS–PAGE profiles, it can be suggested that mechanisms other than polymerisation by MTGase explain the beneficial effects of the treated plasma cold storage on gel texture. In contrast, the setting time had no effects on the water-holding capacity of heat-induced plasma gels at acid pH value, although this gel property was slightly enhanced by submitting porcine plasma solutions to the combined treatment (MTGase plus HP), with improvements being in accordance with the better-structured network of these heat-induced plasma gels.     

Qualification and quantification of fish protein in prepared surimi crabstick

ABSTRACT:  Species identification and protein quantification in surimi crabstick were achieved using sodium dodecyl-sulfate polyacrylamide gel electrophoresis (SDS-PAGE). When the Lowry and Kjeldahl protein determination methods were compared, the former showed more consistent results. Densitometric scanning of the gels was used for quantification of total fish protein as well as total egg white protein. The lower molecular weight proteins, 30 kDa and lower, proved to be the most useful in fish species identification as well as egg white protein addition. Using a combination of the myosin heavy chain band and the species-specific myosin light chain (Alaska pollock: 22.5 kDa; Pacific whiting: 24.4 kDa) proved the most accurate in calculating fish protein content of the crabstick sample, while for those samples that contained egg white, quantification was accomplished from the densitometric analysis of the overlapping bands of actin (45 kDa) from fish and ovalbumin from egg white. Lysozyme (14.3 kDa) proved to be a unique protein band in determining the presence of egg white when the content of dried egg white was equal to or exceeded 0.5% of the total weight of the final crabstick.     

Effect of select parameters on the properties of edible film from water-soluble fish proteins in surimi wash-water

Edible film from water-soluble fish proteins were developed by casting film solution on leveled trays and effects of pH (9.5, 10.0 and 10.5), heating temperature (60, 70 and 80 °C), and heating time (10, 20 and 30 min) of the film solution on various film properties were determined using Response Surface Methodology (RSM). The impact of pH and heating temperature of film solution was more significant, overall, on the film's properties than heating time. Contour plots of tensile strength and elongation at break was highest at pH of 10.0 at 70 °C (2.75-3.02 MPa) but low in elongation at break (6.35-9.16%), while water vapor permeability and oxygen permeability were at their lowest (58.55-65.96 g mm/m² d kPa and 351.33-624.18 cm³ μm/m² d kPa). There was a direct correlation between the films’ and proteins’ solubility on one hand, and heating temperature of film solution on the other, which reversed with change in pH of film solution. Film color was darker and more yellowish with increase in the pH of film solution.     

Effects of oxidative modification on gel properties of isolated porcine myofibrillar protein by peroxyl radicals

AAPH-derived (2,2′-azobis (2-amidinopropane) dihydrochloride) peroxyl radicals were selected as representative free radicals of lipid peroxidation to investigate the effects of oxidative modifications on isolated porcine myofibrillar protein structures as well as their rheological and gelling properties. Incubation of myofibrillar protein with increasing concentrations of AAPH resulted in a gradual increase (p < 0.05) in carbonyl content and SH → S–S conversion. Results from SDS-PAGE indicated that medium (~ 1 mM) and relatively high (> 3 mM) concentrations of AAPH induced aggregation of myosin and denaturation of myosin, troponin and tropomyosin, respectively. These structural changes resulted in changes on gelation of myofibrillar protein. Low level protein oxidation (AAPH ≤ 0.5 mM) had no remarkable effect (p > 0.05) on the viscoelastic pattern of myofibrillar protein gelation. Moderate oxidative modification (AAPH ~ 1 mM) enhanced the water-holding capacity (WHC) and texture properties of gels, while further oxidation (AAPH > 3 mM) significantly reduced the gel quality.     

Behaviour of connective tissue in fish surimi on fractionation by sieving

The surimis prepared from the three fish species, red barracuda Sphyraena pinguis, yellow sea bream Dentex tumifrons, and spotted shark Mustelus manazo, were fractionated by sieving through a 30-mesh stainless steel sieve. Chemical analyses revealed significant differences in the collagen content among the residual fraction on the sieve (fraction A), the passed fraction (fraction C), and the original surimi before sieving (fraction B): the fractions A and B showed values 10–20 and 5–10 times higher than those of the fraction C, respectively, for all the species examined. Histological observation indicated the richness of the thick connective tissues derived from myocommata in fractions A and B, while thick connective tissue was hardly observed in fraction C. These results suggested that the present fractionation method may have an effect of reducing the collagen content to about 10–20% of the original value, and that a large part of collagen in fish surimi exists in the relatively thick connective tissue, probably derived from myocommata.     

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.     

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