Characteristics of Sarcoplasmic Proteins and Their Interaction with Surimi and Kamaboko Gel

ABSTRACT:  This study examined the effect of adding common carp sarcoplasmic proteins (Sp- P) on the gel characteristics of threadfin bream surimi and kamaboko while maintaining constant moisture and myofibrillar levels. Based on the temperature sweep test, which is involved in heating of surimi gel from 10 to 80 °C to monitor the viscoelastic properties, at temperature range of 40 to 50 °C, the decrease level (depth of valley) in storage modulus (G') thermograph was in proportion to the concentration of added Sp- P. Storage modulus (G') showed greater elasticity after adding Sp- P compared with the control without Sp- P. Furthermore, the breaking force and distance and consequently gel strength of the resultant kamaboko were improved significantly ( P > 0.05). Thus, added Sp- P did not interfere with myofibrillar proteins during sol–gel transition phase but associated with textural quality enhancement of resultant kamaboko; however, addition of Sp- P from the dark muscle of the carp decreased the whiteness of the resultant surimi. Furthermore, according to the SEM micrographs, the gel strength could not be associated with either the number of polygonal structures/mm² or the area of the polygonal structures in the kamaboko gel microstructure.     

Participation of cysteine protease cathepsin L in the gel disintegration of red bulleye (Priacanthus macracanthus) surimi gel paste

BACKGROUND: Endogenous proteases, among them cysteine‐type proteases, are reported to contribute to gel disintegration, resulting in kamaboko of poor quality. Severe gel disintegration occurs in red bulleye surimi gel paste. The objective of this study was to clarify the participation of cysteine protease cathepsin L in the gel disintegration of red bulleye surimi. The surimi was made into kamaboko with and without cathepsin L inhibitors. To confirm its hydrolysis action, crude cathepsin L was also extracted and added to the surimi to make kamaboko. RESULTS: The gel strength of kamaboko obtained by both one‐step (50 °C, 2 h) and two‐step (50 °C, 2 h + 80 °C, 20 min) heating was very low in the absence of inhibitors. Protease inhibitors E‐64 and leupeptin were found to enhance the gel strength considerably. Sodium dodecyl sulfate polyacrylamide gel electrophoresis revealed that the hydrolysis of kamaboko was promoted by crude cathepsin L and inhibited by E‐64 and leupeptin. The gel strength of two‐step heated kamaboko was increased from 12 to 110 and 130 g cm^?2 by E‐64 and leupeptin respectively at a concentration of 0.2 g kg^?1 surimi. CONCLUSION: Endogenous cathepsin L of red bulleye surimi participates in gel disintegration during kamaboko processing. It does so by degrading the myosin heavy chain of actomyosin and consequently hindering the gelation of red bulleye surimi. Copyright © 2009 Society of Chemical Industry     

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.     

Characteristics of surimi and kamaboko from sardines

Sardines of varying freshness (1 to 3 days in ice) were manually or mechanically processed into fish mince and surimi using 1 to 3 washing steps. Standard kamaboko gels were prepared by grinding thawed surimi with 3% NaCl and 5% potato starch, stuffing into sausage casings, holding at 37°C for 30 min and cooking at 90°C for 50 min.
Three washing steps decreased the yield of washed fish mince (21-27 g per 100 g of whole fish), and the protein recovery (50-55% of that present in the unwashed mince), but caused efficient lipid removal (80%) leading to surimi containing only 0.2-1.4% lipid. The texture and colour of the final kamaboko were also improved.
The texture parameters (folding score, rigidity, elasticity index and gel strength) of kamaboko prepared from very fresh sardines were markedly enhanced by gel setting during incubation at 37°C for 30 min or 4°C for 24 hr. Incubation at 60°C for 30 min led to soft, coarse gels. Omitting potato starch or replacement by spray dried egg white had little effect on texture.
The texture of kamaboko prepared from less fresh sardines was less firm and elastic, did not improve when incubation was carried out at 37 or 4°C before cooking, and was softer and coarser after incubation at 60°C. Partial or total replacement of potato starch by egg white, soy protein isolate or bovine serum albumin markedly improved the texture. Egg white also increased the colour lightness.     

Contribution of sarcoplasmic proteins to myofibrillar proteins gelation

Surimi, a refined protein extract, is produced by solubilizing myofibrillar proteins during the comminuting and salting stages of manufacturing. The resulting paste gels on heating to produce kamaboko or a range of analog shellfish such as crab claw, filament sticks, fish mushroom, and so on. The myosin molecule is the major myofibrillar protein in gelation. It is believed that washing steps during the traditional surimi process play an important role in enhancing the gel properties of the resultant kamaboko by removing water-soluble (sarcoplasmic, Sp-P) proteins. By contrast, some researchers claim that retaining Sp-P or adding it into the surimi gel network not only does not interfere with the action of myofibrillar proteins during the sol-gel transition step but also improves the gel characteristics of the resultant kamaboko. It seems that retention of Sp-P or their addition into raw surimi does enhance the textural properties of kamaboko gel perhaps by functioning as a proteinase inhibitor, particularly against trypsin and trypsin-like proteinases but this depends on the type of applied surimi process. Among different types of Sp-P, it has been claimed that some proteins such as endogenous transglutaminase (TGase) play a more important role than other Sp-P in bond formation, by catalyzing the cross-linking of myosin heavy chain (MHC) molecules during low-temperature setting of surimi, resulting a more elastic kamaboko gel.     

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.     

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.     

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     

The properties of surimi and kamaboko gels from nine British species of fish

This paper describes the preparation and properties of surimi and derived kamaboko gels from a range of British-caught species of teleost (or bony) fish including white fish (fillets, trimmings and skeletons), fatty fish and an elasmobranch (or cartilaginous) fish. The data include yields, moisture and fat contents, water-binding capacities, pH values and Hunter L,a,b colour values as well as sensory and instrumentally measured indices of texture.
Cod, haddock and whiting fillets and trimmings of haddock and whiting yielded surimi and derived gels with functional properties most closely approaching those of the Alaska pollack surimi used as a standard. Saithe gave a gel which was firm and elastic but which had a low water-binding capacity and was dark in colour. The fatty fish yielded surimi with some potentially useful functional properties but colour and water-binding capacity were inferior to pollack surimi.     

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.     

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.     

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.     

典型加工条件下鱼糜肌原纤维蛋白品质变化规律及调控方法研究进展

鱼糜制品（鱼丸、鱼糕、蟹肉棒等）因为其健康营养、方便快捷等特点而深受消费者欢迎，具有广阔的市场前景。鱼糜制品是基于鱼糜肌原纤维蛋白的胶凝性能所形成的弹性凝胶体，其加工工序包括斩拌、加热、添加外源物等。因此，鱼糜肌原纤维蛋白在典型加工条件下发生结构以及功能特性的变化会影响鱼糜制品的品质。本文主要综述了鱼糜肌原纤维蛋白在物理场（加热、斩拌）、化学场（pH值、离子强度）、生物场（酶、微生物）等典型加工条件下的结构及功能特性变化规律及调控方法，以期为进一步发展鱼糜制品加工业提供理论依据。     

New Approach to Improve the Quality of Minced Fish Products from Freeze-Thawed Cod and Mackerel

To improve the quality of minced fish products, various reductants, e.g. mercaptoethanol, cysteine, tannic acid, sodium bisulfite, and ascorbic acid were used in surimi process. It was found that 0.08–0.10% mercaptoethanol, cysteine, and sodium bisulfite were the most effective in recovering the reactive -SH group, and increasing the actomyosin extractability and quality of kamaboko from frozen cod and mackerel. The addition of reducing agents during surimi processing recovered the reactive SH group and subsequently increased the gelation of freeze-thawed fish meat. This suggests that the formation of disulfide bond is of importance in gelation of minced fish products. The addition of oxidants during processing into final product from the surimi with reducing agents made the gel-strength of product higher than that of samples without oxidants. This proves the importance of disulfide bond in gelation of minced fish products.     

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).     

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.     

不同种类淀粉对罗非鱼鱼糜凝胶品质的影响

为了改善淡水鱼鱼糜制品的品质,以冷冻罗非鱼鱼糜为原料,分别添加4%木薯原淀粉、3种木薯变性淀粉（磷酸酯淀粉、羟丙基淀粉和乙酰化二淀粉磷酸酯）及复配木薯变性淀粉（乙酰化二淀粉磷酸酯与羟丙基淀粉质量比为3∶2）,考察淀粉添加对鱼糜凝胶质构、流变学特性、持水性及水分分布和微观结构等的影响,探讨不同种类淀粉对鱼糜凝胶品质的改善。结果表明,与对照组相比,添加5种淀粉均会显著降低罗非鱼鱼糜凝胶的白度（P<0.05）,但其凝胶强度、硬度和咀嚼性显著增大,凝胶持水性显著提高（P<0.05）,蒸煮损失率显著下降（P<0.05）,结合水含量显著增加（P<0.05）,凝胶微观结构更加均匀致密,且添加了复配木薯变性淀粉的凝胶质构特性最好,持水性最高。低场核磁共振成像和光学显微镜观察结果显示,不同种类的淀粉均能有效锁住鱼糜凝胶基质中的水分;升温过程中淀粉吸水膨胀,在鱼糜凝胶网络结构中起浓缩和填充作用;添加了复配木薯变性淀粉的鱼糜凝胶结构最致密均匀。因此,添加复配木薯变性淀粉可以有效改善罗非鱼鱼糜制品的品质,为淡水鱼鱼糜制品的开发提供了理论支撑。     

Rheological characteristics of suwari and kamaboko gels made of surimi from Indian major carps

The gel strength, compressibility and folding characteristic of suwari (set) and kamaboko (set and cooked) gels prepared from rohu ( Labeo rohita ), catla ( Catla catla ) and mrigal ( Cirrhinus mrigala ) surimi were examined to understand the occurrence of suwari and modori phenomena in surimi from major freshwater carps. Suwari setting of gels did not take place at lower temperatures. Suwari gels showed good gel strength at 50 °C for rohu and at 60 °C for catla and mrigal after 30 min setting time. Incubation for 60 min decreased the gel strength at 60 °C for rohu and catla. Setting at 25 °C followed by cooking at 90 °C increased the gel strength. Increased setting temperature, however, decreased the gel strength of cooked gels. Gel strength and compressibility data were supported by folding characteristics. © 2002 Society of Chemical Industry     

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.     

添加微细鲽鱼鱼骨泥对金线鱼鱼糜凝胶品质的影响

以鲽鱼骨为研究对象,首先采用湿法超微粉碎技术将其加工成微细骨泥,再将其添加到金线鱼鱼糜制品中开发高钙鱼糜制品,从鱼糜溶胶pH值、肌原纤维蛋白Ca2＋-ATP酶活力、凝胶强度、质构、持水性、色泽、凝胶溶解度、微观结构方面探讨添加不同质量分数（2.5%～12.5%）鱼骨泥对鱼糜制品凝胶品质的影响。结果显示：添加微细鱼骨泥不影响鱼糜正常凝胶的pH值;较低质量分数（不超过5.0%）时,鱼骨泥中的Ca2＋可以激活鱼糜溶胶中肌原纤维蛋白的ATP酶,显著提升Ca2＋-ATP酶活力;鱼糜凝胶的凝胶强度、质构、持水性、色泽指标均在添加质量分数5.0%鱼骨泥时达到最高值,而凝胶溶解度达到最低值。十二烷基硫酸钠-聚丙烯酰胺凝胶电泳分析和扫描电子显微镜观察结果表明,添加质量分数2.5%～5.0%鱼骨泥一定程度上促进了肌球蛋白重链（myosin heavy chain,MHC）的交联,可以促进鱼糜凝胶形成致密均匀的网状结构,过量添加则会影响MHC交联和凝胶网络致密性。