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Food Hydrocolloids 25 (2011) 1842e1852

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Food Hydrocolloids
journal homepage: www.elsevier.com/locate/foodhyd

Food hydrocolloids as additives to improve the mechanical and functional properties of sh products: A review
Jos A. Ramrez a, Rocio M. Uresti a, Gonzalo Velazquez a, b, Manuel Vzquez c, *
a

Departamento de Tecnologa de Alimentos, Cuerpo Acadmico de Alimentos, UAM, Reynosa-Aztln, Universidad Autnoma de Tamaulipas, Apdo. Postal 1015, Reynosa, Tamaulipas 88700, Mexico b CICATA Quertaro, Cerro Blanco No. 141, Col. Colinas del Cimatario, Quertaro 76090, Mexico c Department of Analytical Chemistry, Faculty of Veterinary Science, University of Santiago de Compostela, Campus Lugo, 27002 Lugo, Spain

a r t i c l e i n f o
Article history: Received 27 October 2010 Accepted 24 May 2011 Keywords: Surimi Restructured products Starch Low salt Caseinate Transglutaminase Hydrocolloids Additives

a b s t r a c t
The restructuring process offers to sh processors the opportunity to obtain new products, taking advantage of both low-value sh species and remains from lleting and other processing operations. However, mechanical and functional properties of restructured products depend on the biochemical and physicochemical properties of muscle proteins, mainly myosin and actomyosin. In this regard, the biochemistry of sh muscle is different from that of mammals and birds. Therefore, sh products must be processed in a different way from red meat or poultry. The main sh products are surimi and restructured products. Fish products can be improved or modied by using hydrocolloids (carbohydrates and protein) as additives. In this review, the modern technology to obtain these products, the applications of hydrocolloids in sh products, and the implications of the increasing demand for healthy, low-salt sh products are discussed. 2011 Elsevier Ltd. All rights reserved.

1. Introduction The increasing demand for sh and sh products by consumers is affecting the shery resources worldwide, drastically reducing the stocks of many sh species such as ounder, cod, hake, and other shes. At the same time, there are several underutilised sh species due to their size, avour, odour, colour, or texture. In addition, some lleting by-products could be transformed into high-value products through restructuring technology. Both lowvalue species and lleting remains could be transformed into high-value products by surimi technology and restructuring technology. These technologies are used to obtain novel products using an array of additives to improve the mechanical and functional properties. However, several biochemical and physicochemical considerations regarding muscle proteins must be taken into account to obtain high-quality products. The restructuring process allows the acquisition of products with high commercial value. This process implies the milling of sh muscle, solubilisation of sh proteins with salt, formatting of sh paste and induction of the gelling phenomenon, usually by heat.

Several restructured sh products have been developed, including the following: vacuum-tumbling processing of trimmed salmonid sh with posterior canning and retorting; and tumbling of channel catsh using egg white as binder (Borderas & Prez-Mateos, 1996; Yetim & Ockerman, 1995a, 1995b; Zimmerman, Bissel, & McIntosh, 1998). The restructuring process allows for the commercialisation of some low-value sh species with higher prots: non-commercial sh species, smaller shes than commercial size (such as caught as shrimp by-catch), and trimmings from lleting of commercial sh species (Noriega-Rodrguez et al., 2009; Pacheco-Aguilar et al., 2010). 1.1. Biochemical considerations The biochemistry of sh muscle is different from that of mammals and birds. Consequently, sh products must be processed in a different way than red meat or poultry. The introduction of the surimi technology in occidental countries has allowed a better understanding of the biochemistry of sh muscles and the physicochemical behaviour of proteinaceous matrix when forming gels. Particular phenomena in sh products are modori and suwari. Modori is a deteriorative phenomenon affecting the gel structure (weakening) and takes place at temperatures near 60  C. It has

* Corresponding author. Tel.: 34 982822420; fax: 34 982254592. E-mail address: manuel.vazquez@usc.es (M. Vzquez). 0268-005X/$ e see front matter 2011 Elsevier Ltd. All rights reserved. doi:10.1016/j.foodhyd.2011.05.009

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been associated with the activity of endogenous serine and cysteine proteases in the muscle. To minimise this negative effect, surimi products must be heated as quickly as possible, being careful that the sh paste remains in the 50e70  C range. Usually, sh gels are obtained by water immersion (90  C for 20e30 min) of formatted sh paste (An, Peters, & Seymour, 1996; Ramrez, Garca-Carreo, Morales, & Snchez, 2002; Ramos-Martnez, Morales-Gonzlez, Ramrez, Garca-Carreo, & Montejano-Gaitn, 1999; Snchez, Ramrez, Morales, & Montejano, 1998). Suwari, or setting, is the gelling of muscle protein at temperatures in the 0e40  C range. This phenomenon is considered benecial because it improves the mechanical and functional properties of sh gels and is usually induced before heating the sh paste at 90  C for 30 min. Setting results from the activity of a calcium-dependent endogenous transglutaminase (TGase). This enzyme catalyses the formation of covalent bonds between adjacent proteins, improving gel structure. Transglutaminase catalyses an acyl-transfer reaction between g-carboxyamide groups of glutaminyl residues in proteins. When the primary amine is the 3-amino group of lysine and lysyl residues, 3-(g-glutamyl) lysine cross-linking takes place (Kumazawa, Seguro, Takamura, & Motoki, 1993). Adding calcium to restructured products improves their mechanical properties because calcium is a cofactor of endogenous transglutaminase. For example, adding 10e100 mM calcium chloride (CaCl2) induced the aggregation of actomyosin from Oreochromis niloticus incubated at 4 and 40  C. It was associated with the activity of endogenous transglutaminase, determined by the presence of protein aggregates (Yongsawatdigul & Sinsuwan, 2007). In addition, calcium improves proteinecalciumeprotein bonds in thermal-induced gels, increasing the mechanical properties of surimi gels. However, it is important to consider that the presence of proteinecalciumeprotein interactions has been reported as detrimental for protein stability during the frozen storage of surimi. Thus, calcium must be added during the solubilisation of sh pastes, just before inducing the setting (Lee & Park, 1998; Morales, Ramrez, Vivanco, & Vzquez, 2001). Although the setting depends on the optimal activity of the endogenous TGase, it is critical to consider the physicochemical properties of myosin and actomyosin, which are the substrates for the enzyme. Obtaining the optimal activity of TGase requires the muscle proteins to be denatured to expose the residual groups, allowing the covalent cross-linking of adjacent proteins. However, muscle proteins tend to aggregate quickly and show a short range of temperatures between the onset of denaturation and the beginning of aggregation. Additionally, muscle proteins from coldwater shes denature at lower temperatures than muscle proteins from warm-water shes. These differences should be considered to obtain restructured products. Fishes from cold water, e.g., Alaska Pollock, form stronger gels when solubilised pastes are incubated at 0  C for 12e24 h or at 25  C for 2 h before being heated to 90  C for 30 min. Conversely, sh species from tropical water, e.g., tilapia, form stronger gels when setting is induced at 40  C for 30 min. In this regard, gels from lizardsh (Saurida undosquamis), a warm-water sh species, showed better mechanical properties when incubated at 40  C for 30 min compared to 25  C for 2 h prior to heating at 90  C for 20 min. Gels from O. niloticus formed at 40  C for 30 min showed better mechanical properties than gels formed at 4  C for 2 h. The setting was induced by formation of higher molecular weight protein (HMP), which occurs more frequently at 40  C than at 4  C. This was induced by higher protein denaturation, measured by changes in surface hydrophobicity and loss of the alpha-helical structure. The low mechanical properties of gels induced by setting at 4  C was associated with a partial covalent cross-linking of adjacent proteins by the endogenous transglutaminase because the low temperature did not induce denaturation of native actomyosin,

and reacting residual groups were not exposed (Yongsawatdigul & Sinsuwan, 2007). Even species from habitats with similar temperatures (cold or warm waters) show different onset temperatures for the denaturation of muscle proteins. Muscle proteins from warm-water species, e.g., walleye pollock, white croaker, and threadn bream, showed species-specic properties, which resulted in different rheological properties. Optimum temperatures for shaping sh meat pastes were different depending on the temperature required to initiate protein denaturation (Fukushima, Okazaki, Fukuda, & Watabe, 2007). It has been reported that natural actomyosin from pacic whiting and threadn bream showed different properties on thermal transitions, measured by circular dichroism (CD) and differential scanning calorimetry (DSC). Pacic whiting actomyosin required a lower temperature to initiate its thermal transitions and showed higher unfolding of its tertiary structure, measured by surface hydrophobicity, alpha-helical content, and solubility induced by incubation at 25  C for 4 h and 40  C for 2 h. The higher degree of unfolding of the protein structure exposed more residual groups, allowing more covalent cross-linking of adjacent proteins by transglutaminase activity. Transglutaminase catalysed more cross-linking of pacic whiting myosin heavy chain than threadn bream myosin heavy chain (Hemung, Li-Chan, & Yongsawatdigul, 2008). Finally, the freshness of sh muscle is important. In similar process conditions, the mechanical properties of gels from lizardsh decreased with the freshness of sh muscle kept in ice over ten days (Benjakul, Phatcharat, Tammatinna, Visessanguan, & Kishimura, 2008). 1.2. Microbial transglutaminase Initially, the setting was considered a technological problem for surimi processing because the solubilised sh paste tended to gel during refrigerated storage. Once the benecial effect of inducing the setting was shown to improve the mechanical properties of gels, several studies were carried out to understand its origin. Finally, its enzymatic origin was understood, and several groups worked to nd how to produce transglutaminase by biotechnology techniques. Currently, a commercial calcium-independent microbial transglutaminase (MTG) is used to improve the mechanical and textural properties of several protein foods, including surimi and restructured sh products. This enzyme can be obtained from Streptoverticillium ladakanum or Streptoverticillium mobaraense (Jiang, Leu, & Tsai, 1998) and has been applied to increase the textural properties of surimi from the cold-water sh Alaska pollock, and several warm-water species, such as Southern blue whiting and white croaker (Asagami, Ogiwara, Wakameda, & Noguchi, 1995), striped mullet (Ramrez, Rodrguez-Sosa, Morales, & Vzquez, 2000) or silver carp (Ramrez, Santos, Morales, Morrisey, & Vzquez, 2000). MTG catalyses the same reaction as endogenous transglutaminase, but MTG shows lower deamidation afnity than the endogenous transglutaminase of sh or pig (Ohtsuka, Umezawa, Nio, & Kubota, 2001). Several studies have reported the optimal conditions for using MTG in surimi gels (Lee, Lanier, Hamann, & Knopp, 1997; Ramrez, Rodrguez-Sosa, et al., 2000; Ramrez, Santos, et al., 2000) and restructured sh products (Tllez-Luis, Uresti, Ramrez, & Vzquez, 2002; Uresti, Lpez-Arias, GonzlezCabriales, Ramrez, & Vzquez, 2003). Recent studies have reported that MTG induced more extensive cross-linking of myosin heavy chain proteins than endogenous sh transglutaminase, allowing the formation of gels with better mechanical properties than from Pacic whiting actomyosin (Hemung et al., 2008). Although better mechanical properties are obtained by increasing

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the amount of MTG, the optimal activity of the enzyme is reached when setting is obtained at temperature conditions that induce the denaturation of sh actomyosin. Although commercial applications for protein cross-linking are based on MTG, there is an interest to explore the use of several oxidative enzymes, including tyrosinases, laccases, and sulfhydryl oxidases as alternatives. However, the reaction mechanisms of these cross-linking enzymes differ, resulting in different technological properties. Therefore, the use of novel enzymes requires extensive knowledge of the complex structure of proteins to give each enzyme access to reactive groups and to avoid process conditions that affect the extent of cross-linking. This consideration is required to tailor proteins towards better functionality, such as improved gelling, emulsifying property or others (Buchert et al., 2010).

2. Surimi Surimi technology offers a great opportunity to transform different sh species into high commercial value products. Thus, the demand for surimi and kamaboko is increasing worldwide. However, surimi technology has several negative environmental impacts, which are necessary to minimise. One such impact is the over-exploitation of white sh stocks, which has compromised the supply of these species. Strategies for using alternative species and sheries by-catch, together with the maximum utilisation of sh, are being proposed (Jafarpour & Gorczyca, 2008; Martin-Sanchez, Navarro, Perez-Alvarez, & Kuri, 2009). Surimi is not a nal product; it is a wet concentrate of highquality myobrillar proteins, obtained by washing the minced sh meat with cold water several times. The washing operation removes the water-soluble sarcoplasmic proteins responsible for organoleptic properties and concentrates the water-insoluble myobrillar proteins, such as, myosin, actin, and the actomyosin complex (Ramrez, Martn-Polo, & Bandman, 2000). Although it is technically feasible to obtain surimi from any sh species, the functional properties are highly dependent on sh species, and surimi from many species shows low gelling capacity properties. Gelling and other functional properties of surimi depend on the overall effect of all proteins in the food system. Gelling is a functional property that involves three main steps in muscle protein systems: 1) solubilisation with 2e3% salt at pH close to 7 (pH of muscle in post-riguor mortem); 2) thermal denaturation of proteins (50e90  C), and 3) a consequent protein aggregation. These conditions allow the acquisition of an irreversible and opaque gel with different levels of rigidity and deformability, depending on the thermal treatment, sh species, and other parameters. The surimi industry in Japan usually evaluates the quality of surimi gels using the folding test where a small sample (less than 0.5 cm) is folded twice. In this simple test, high-quality surimi does not show any fracture. A torsion test has been proposed as an objective method to measure the mechanical properties of surimi gels, which could be applied to other gelling foods. This method allows the determination of shear stress and the shearing strain at failure (Fig. 1). Shear stress measures gel strength and correlates well with sensory hardness, TPA hardness, and TPA fracturability. This parameter can be improved by different processing conditions and additives. Shear strain measures the gel deformability and correlates well with cohesiveness and springiness (TPA). This parameter highly depends on the sh species and freshness; generally, it is not improved by process or additives. A surimi gel with a shear strain value higher than 2.2 is considered high quality and can be used for producing crab or shrimp analogues. Surimi

Fig. 1. Effect of shear stress and shear strain on the appearance of surimi and restructured product.

gels with strain values lower than 1.8 are considered low quality (Hamman & Lanier, 1987; Kim, Hamman, Lanier, & Wu, 1986). Most sh species from warm-water produce surimi gels with low to medium shear stress and low shear strain values. These gels are perceived as mushy (low stiffness and low cohesiveness) and have low commercial value (Luo, Kuwahara, Kaneniwa, Murata, & Yokoyama, 2001; Ramrez, Garca-Carreo, et al., 2002; Ramrez, Santos, et al., 2000). Fig. 1 shows the relationship between shear stress and shear strain and sensory textural perception. Several studies have been carried out to improve the mechanical and functional properties of surimi gels. The use of calcium improved the shear stress of surimi gels from several sh species, but had no effect on the shear strain. This behaviour is associated with the activity of residual endogenous transglutaminase after the washing cycles that are necessary to obtain surimi (Lee & Park, 1998; Morales et al., 2001). Several additives, including MTG and hydrocolloids, have been used to improve the mechanical properties of surimi gels (Ramrez, Rodrguez-Sosa, et al., 2000; Ramrez, Santos, et al., 2000). Recently, it has been reported that centrifugation, rather than decanting and ltering, improves the mechanical properties by more efciently removing the sarcoplasmic proteins. Other techniques explored whether various alterations improved the mechanical properties of surimi products, including modication of the pH and the use of alkaline treatments during washing (Jafarpour & Gorczyca, 2008). Surimi is also considered an ingredient in the establishment of many products. Recently, the use of surimi as a protein-based carrier in developing high omega-3 fatty acid-containing seafood products has been proposed because it allows for uniform dispersion and oxidative stability of omega-3 fatty acid oil in the highly cohesive gel system without the use of antioxidants (Tolasa, Lee, & Cakli, 2010). 3. Restructured products Although several methods of restructuring have been developed, the most common process includes cutting, tumbling, and massaging (with or without vacuum). This process uses salt to solubilise and extract myobrillar proteins, which form a sticky exudate responsible for binding all the products (Boyer, Joandel, Ouali, & Culioli, 1996; Ramrez, Martn-Polo, et al., 2000). Myobrillar proteins (particularly myosin) are responsible for the heat-induced aggregation involved in gelling and binding mechanisms (Boyer, Joandel, Roussilhes, Culioli, & Ouali, 1996). The

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level of salt used during massaging is important, as it determines the amount of exuded protein, which acts as a binding agent, leading to the protein aggregation. A different mechanism of temperature-induced aggregation has been reported for myosin, as inuenced by the ionic strength. At low ionic strength, myosin aggregation could be induced by side-to-side interactions, while at high ionic strength, the aggregation could be induced by head-tohead interactions, which implies a more structured system (Boyer, Joandel, Ouali, et al., 1996; Ramrez, Rodrguez-Sosa, et al., 2000). Restructured products can be obtained by combining abundant and low commercial value sh species. Striped mullet (Mugil cephalus), an abundant sh species caught in the north of the Gulf of Mexico with very low commercial value because of its dark meat and strong avour, was combined with Mexican ounder (Cyclopsetta chittendenni), an abundant sh species highly appreciated for its white esh and good taste, but with a small size and low commercial value when caught as shrimp by-catch in the north of the Gulf of Mexico. Although gels from both sh species alone showed good mechanical properties, gels obtained from the mixture had lower mechanical properties. When microbial transglutaminase was used as binder at 3 g/kg, the mechanical properties of the mixture (1:1) of striped mullet:Mexican ounder were improved, allowing for restructured products with mechanical, functional and sensorial properties appropriate for commercialisation (Ramrez, Del ngel, Uresti, Velzquez, & Vzquez, 2007). Other binding agents that have been reported include brinogen, thrombin, phosphate, isolated soy protein, sodium caseinate, waxy modied corn starch, carrageenan, oat our, modied food starch, kappa-carrageenan, and soy protein. The suggested mechanisms for these additives can be acting as llers or by interactions with the solubilised myosin as shown in Fig. 2 (Motzer, Carpenter, Reynolds, & Lyon, 1998; Shao, Avens, Schmidt, & Maga, 1999; Tsai, Unklesbay, Unklesbay, & Clarke, 1998).

3.1. Low-salt restructured products The growing concern over the elevated consumption of sodium from processed products opens an opportunity for the food industry to offer low-salt products. Reduction of salt intake could prevent and control adverse blood pressure levels, and consumers are interested in alternative products with lower levels of salt (Narhinen et al., 1998). However, adding salt is necessary for obtaining restructured products with the appropriate mechanical and functional properties. As discussed previously, the techniques used to obtain restructured products require solubilisation and extraction of myobrillar proteins with salt to obtain sticky exudates, which are used to bind meat pieces. Decreasing the salt levels induces a reduction in the amount of solubilised and extracted protein, which affects the binding capacity. The use of transglutaminase as a binding agent in restructured products, containing low concentration or no salt, as well as raw products (uncooked), has been suggested because proteins extracted during massaging are also a good substrate for cross-linking reactions by MTG (Kuraishi et al., 1997). However, restructured products obtained by thermal-induced aggregation require at least 1% NaCl to promote cross-linking reactions, which improve the mechanical properties of restructured sh products. At this salt concentration, there were no differences in the mechanical properties of products obtained with 3 or 6 g/kg of the enzyme. MTG was able to induce protein cross-linking even in the absence of salt. However, protein aggregation was not enough to improve the overall functional and textural properties (Ramrez, Uresti, TllezLuis, & Vzquez, 2002). 3.2. Cold binding The heat-induced setting depends widely on the denaturation temperature of myosin, which induces the exposure of the buried g-carboxyamide groups of glutamyl residues and 3-amino group of

Non treated

Cooking

Good gel

Solubilized fish paste

Food hydrocolloids as additives

Cooking

Better gel

Protein structure showing intramolecular interactions Food hydrocolloids added as additives induce crosslinking and protein interactions Thermal induced denatured protein

Fig. 2. Suggested mechanism for induced changes in proteins due to hydrocolloids.

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lysine residues during MTG-induced cross-linking (Cofrades, Ayo, Serrano, Carballo, & Jimnez, 2006). However, MTG shows activity even in cold temperatures (under 4  C). This property is important when binding raw meat under refrigeration to produce restructured products. This practice is called cold binding and implies the aggregation of myobrillar proteins without the denaturation/ aggregation induced by heat. In cold binding, aggregation is due mostly to the MTG activity (Castro-Briones et al., 2009; Hemung et al., 2008). Cold binding using MTG alone or combined with others binders, such as carbohydrates or proteins, allows the use of sh llet trimmings and minced muscle to prepare restructured products that could be commercialised as raw material to produce sushi, cold smoked sh llets, carpaccios or marinated products. Furthermore, restructured raw products could be cooked as fresh sh llet or pieces of llet in several dishes (Moreno, Carballo, & Borderias, 2010). Uncooked restructured products were obtained with MTG under refrigeration or freezing conditions. The binding of 2-cm cubes of lean pork meat for 16 h of frozen-induced aggregation at 40  C required at least 30 g/kg NaCl and 1 g/kg MTG to obtain good mechanical properties. Products obtained with 10 g/kg NaCl and 1 g/kg MTG showed inappropriate mechanical properties (Kuraishi et al., 1997). Minimally processed raw restructured sh products with appropriated mechanical and functional properties were obtained from pieces or homogenised hake muscle after solubilisation with 15 g/kg sodium chloride, 10 g/kg MTG, and 7.5 g/ kg sodium caseinate. The soluble pastes were incubated for 24 h at 5  C to allow protein cross-linking (Moreno, Carballo, & Borderias, 2009). The cold binding technique allows the production of low-salt products (5e15 g/kg salt) by using MTG (5e10 g/kg) and storing the solubilised pastes at 5  C for 48 h at different pHs (Moreno et al., 2010). Although MTG improves the mechanical properties related with the gel strength, it has a minimal effect on shear strain. A minimal or negative effect on the water-holding capacity (WHC) has also been reported (Tllez-Luis, Ramrez, & Vzquez, 2004). Thus, the use of hydrocolloids to improve the WHC might be needed when restructured products are obtained using MTG. The compatibility among MTG and the hydrocolloids must be considered because sometimes the combined use leads to unstructured weaker products as is explained below. Other side to consider when using this enzyme is its high cost. Frequently, the sh products can require a minimal improvement in the mechanical properties which could be obtained just by adding some hydrocolloids instead of MTG. 4. Hydrocolloids as additives Polysaccharides and proteins are food hydrocolloids with an important role in the structure, stability and functional properties of several processed foods. Proteinecarbohydrate interactions determine the functional properties in foods where proteins are the major ingredients, such as meat and sh processed products. Different hydrocolloids have been proposed to improve the mechanical and functional properties of surimi and restructured sh gels (Gomez-Guilln, Borderias, & Montero, 1997; Lee, Wu, & Okada, 1992; Park, 2000; Ramrez, Barrera, Morales, & Vzquez, 2002). Fish proteins solubilised by salt and water form a continuous matrix. Some additives can be entrapped within this matrix, lling the gel and exerting their functional effects in the restructured products by a) inuencing the formation of the continuous surimi gel matrix during thermal-inducing gelation; b) modifying the viscosity, mobility and other properties of the liquid phase; c) inuencing texture and appearance of the gel, i.e., particle size,

distribution, rheological (textural) properties, and relative volume fraction of the gel (Lee et al., 1992). 4.1. Carbohydrates Gel-forming capability is important to obtain sh products, such as restructured products (from whole-minced pastes) or surimibased products (water-washed pastes). Carbohydrates, such as gums and starches, promote the formation of the continuous matrix by interacting with water and proteins in the sh paste. Some additives interact with proteins to form a more structured system, while others act as llers, binding water and modifying the viscosity of the system (Lee et al., 1992). It is also important to consider that adding carbohydrates into a formulation could modify the capacity of salt to solubilise myobrillar proteins, which would affect the mechanical and functional properties of gels. Furthermore, some carbohydrates are not compatible with the muscle proteins and have a disruptive effect in the gelling property. Several hydrocolloids, such as starch, carrageenan, and konjac, are typically used to improve the mechanical properties of surimi gels (Gomez-Guilln et al., 1997; Park, 2000). 4.1.1. Starch Starch is the most common ingredient used as ller in products based on surimi or sh. It increases rmness and gel strength (Lee, 1984; Lee et al., 1992; Susuki, 1981; Wu, Hamman, & Lanier, 1985; Wu, Lanier, & Hamman, 1985). Starch is used in the production of surimi products at 40e120 g/kg to control wetness, stickiness, and/ or thermal stability during storage and serving temperatures. Another important attribute of native and modied starches is their capacity to partially replace sh proteins while maintaining desired gel characteristics at a lower cost (Hunt, Getty, & Park, 2009). There is an increasing interest in identifying novel applications for both native and modied starches to improve the mechanical and functional properties of restructured and surimi products. Native wheat starch modied the rheological properties of kamaboko gels from sardine surimi without affecting the thermal transitions, as determined by DSC (Karayannakidis, Zotos, Petridis, & Taylor, 2008). Potato starch slightly improved the strength of surimi seafood gels treated with ohmic heating, but it had a detrimental effect on whiteness, as compared to wheat starch (Chai & Park, 2007). Adding pre-gelatinised starches to SA-grade surimi changed the mechanical properties by enhancing the stiffness of the gel while decreasing yield and breaking force (Yamamoto, Murakami, Nakachi, Nishino, & Nishikawa, 2007). Adding acetylated rice starch at 40e80 g/kg improved the freeze-thaw stability of surimi pastes, but reduced the gel strength and expressible moisture content of surimi gels. The effect of acetylated starch on rheological properties of surimi sols and gels seems to be related to the swelling capability of starch granules in the presence of limited water (Jung, Kim, & Yoo, 2007). Frozen storage affects the mechanical, functional and sensorial properties of sh meals, and the effect is higher when food is subjected to several freeze-thaw cycles during storage and commercialisation. A rubbery texture is generally associated with a loss in WHC and usually results in lower acceptability. Modied tapioca starch (hydroxypropylated distarch phosphate), added at 10 g/kg to bigeye snapper (Priacanthus tayenus) mince paste, reduced the negative changes caused by ve freeze-thaw cycles, improving the mechanical, functional, and overall properties of restructured products, as compared to products with no starch. Restructured products containing 10 g/kg modied starch showed a ner matrix with smaller strands at all freeze-thaw cycles used, observed by scanning electron microscopy (SEM), as compared with the control minced gel (Tuankriangkrai & Benjakul, 2010).

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Most frequently, starch is the rst choice for producing traditional sh burgers or sausages. However, there is a growing interest to obtain new products with different textures and sensorial attributes to offer meals that satisfy the expectations of meals that customers will enjoy eating. Using small amounts of proteins and non-starch hydrocolloids in the formulation could improve the quality of minced sh products, taking advantage of their multifaceted functionality as texture modiers. These formulations change the upper and lower bounds for the attributes of instrumental texture, increasing sensory acceptability (Kasapis, 2009). 4.1.2. Gums Gums are considered a good alternative for improving the mechanical properties of restructured products. They are readily available and they are not expensive. Most of them are compatible with sh muscle proteins, improve the yield without negative effect on texture. Usually, they do not affect signicantly the colour. The main effect is improving the WHC. Other important factor to consider when using gums is that although gums are carbohydrates they do not add calories and have the benecial effects of the bre on diet. Many consumers, especially those looking for healthy foods, could appreciate this effect. Carrageenan and konjac are highly compatible with sh muscle meals, but others gums have a negative effect on texture and some especial considerations must be taken into account. On this regard, locust bean and xanthan gum at a 0.25/0.75 ratio has been proposed to improve the mechanical properties of surimi gels from silver carp (Ramrez, Barrera, et al., 2002). Alginates weaken surimi gels when incorporated (Lee et al., 1992). However, alginates are commonly used for obtaining raw restructured sh products by the cold binding technique under chilling or freezing conditions. The effectiveness of sodium alginate as cold binder can be improved by adding a low concentration (1 g/ kg) of CaCl2, whereas a higher concentration (10 g/kg) reduces the binding capability of the alginate (Moreno et al., 2009, 2010). Konjac glucomannan (KGM) has been proposed to be an efcient cryoprotective agent for sh myobrillar proteins. This gum was able to decrease the muscle protein denaturation/aggregation from grass carp (Ctenopharyngodon idella) during storage at 18  C, improving the amount of salt-extractable protein and reducing the Ca2-ATPase activity, total sulphydryl groups, and active sulphydryl contents. Adding KGM at 10 g/kg showed the same cryoprotective effect as a conventional cryoprotectant (100 g/kg sucroseesorbitol, 1:1). Adding 15e20 g/kg KGM allowed an increase in water-holding capacity, breaking force, and deformation of surimi gels, although the whiteness decreased and the colour became darker (Xiong et al., 2009). 4.1.3. Pectins Pectins are classied as high methoxyl (HM) or low methoxyl (LM) pectins. Both types of pectins have been reported to not improve the mechanical and functional properties of surimi. Moreover, both pectins induced a disruptive effect during gelling. However, amidated LM (ALM) pectin is compatible with surimi gels and improves gelling properties. Results suggest that electrostatic proteinepectin interactions induced a disruptive effect when HM and LM pectin were added. Amidation could improve the polarity of LM pectin. Thus, hydrogen bonds between amidated LM pectin and protein could form a more compatible proteinecarbohydrate system (Barrera, Ramrez, Gonzlez-Cabriales, & Vzquez, 2002). Pectins are a complex family of polysaccharides characterised by their degree of esterication (DE), which varies with the age, location inside the plant tissue, extraction method, and neutral sugar content. Commercial HM pectins have a typical DE of 55e80%; HM pectins usually gel in the presence of sugar at low pH

conditions (Morris, 1998). The gels are formed by associations of chains by stacking the esteried homogalacturonic acid zones, resulting in a three-fold helical conguration governed by hydrogen bonding and hydrophobic interactions. In contrast, LM pectins may form gels in the presence of calcium over a wide range of pHs with or without sugar (Fu & Rao, 2001). Gels are normally formed at concentrations of 1 g/kg. Two types of LM pectins are produced commercially: (a) ordinary LM pectins, prepared by acid treatment in ethanol or isopropanol, and (b) amidated pectins, prepared with ammonia in alcoholic suspensions of pectin (Morris, 1998). The formation of proteinepolysaccharide complexes could improve the functional properties of proteins. Pectins are anionic hydrocolloids with different degrees of methoxylation. Therefore, pectins have a wide range of ionic charges. HM pectins interact with proteins above the isoelectric point, for instance, with lysozyme (Yang, Chen, & Chang, 2001) and bovine serum albumin (Ledward, 1994). HM pectins improved the gelling capacity and thermal stability of whey protein concentrate in the pH range of 4.6e8.5 when the protein concentrate was above 80 g/kg. Proteinepectin interactions improved solubility, emulsication, gelation, and foaming behaviour of whey protein concentrates (Mishra, Mann, & Joshi, 2001). Pectins have been used as cryoprotectants in surimi (Sych, Lacroix, Adambounou, & Castaigne, 1990; Ueng & Chu, 1996). The use of HM pectins decreases the shear stress and shear strain of surimi gels when added without calcium. This behaviour could be associated with the anionic property of both types of hydrocolloids, and consequently, the repulsive driving force results in a less structured system. In a system containing HM pectins, adding calcium chloride improved the shear stress of gels, reaching equal or higher values than control gels without calcium chloride. Shear strain was improved in all gels containing HM pectins and calcium, as compared to gels containing only HM pectins. However, neither gel showed a shear strain value equal to or higher than control gels. These results suggest that endogenous transglutaminase present in surimi induced the formation of stronger gels by covalent bonds and were not affected by the presence of HM pectin. Another possibility could be that this behaviour is indicative of a proteinecalciumepectin interaction because, as previously discussed, transglutaminase did not improve the shear strain of surimi gels. Despite this type of interaction, surimi gels containing HM pectins showed less mechanical properties than surimi control gels. LM pectin improved the hardness of surimi gels and decreased the shear strain and cohesiveness, but had no signicant effect on shear stress, springiness, or water-holding capacity. The mechanical properties of surimi gels containing LM pectin were not affected by adding calcium. This could be due to covalent bonded surimi gels masking or inhibiting the proteinecalciumepectin interactions, or because these interactions do not have a benecial effect on the mechanical properties of surimi gels. ALM pectin showed a benecial effect on the mechanical properties of surimi and restructured sh products, as compared to LM pectins (Barrera et al., 2002; Uresti et al., 2003). This behaviour could be associated with a different structure of ALM. The amidation of the LM pectin confers different physicochemical and functional properties, i.e., LM amidated pectins require less calcium than LM non-amidated pectins to form a gel. ALM pectins are reported to work better under acidic conditions (pH 3.2e3.6), while non-amidated LM pectin works in the pH range of 2.8e6.5. Hydrogen bonds between ALM pectin and myobrillar proteins could result in an improvement in the mechanical properties, specically hardness and breaking force, of sh gels when ALM pectins are added at 10 g/kg. The detrimental effect on mechanical properties associated with higher concentrations of ALM pectin

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(20e50 g/kg) could be caused by swelling of the hydrocolloid or changes in the native structure of muscle proteins by pectineprotein interactions, with the presence of both hydrogen bonds and electrostatic interactions. The swelling of pectin could promote a disruptive effect by competing for water molecules (a salting-out effect) or simply by interfering in gel formation. A different mechanism seems to take place in sh pastes and gels containing ALM pectins. Fish pastes with 10 or 20 g/kg of amidated LM pectin showed lower values for rmness and consistency compared to control pastes, but did not improve the WHC. This behaviour suggests the presence of proteinepectin interactions, decreasing the proteinewater and pectinewater interactions. Alternatively, the signicantly higher levels of rmness and consistency and WHC reported for solubilised sh pastes using 30 or 50 g/kg of ALM pectin may be associated with higher entrapment of water by amidated LM pectin (Fig. 3). Adding 10 g/kg ALM pectin improved the mechanical properties of restructured sh gels. However, higher levels of ALM pectin showed a disruptive effect on the system. These results suggest that during the gelling of the sh system containing ALM pectin, the proteinepectin interactions in sh pastes could be substituted by proteineprotein interactions, increasing pectinewater interactions (Uresti et al., 2003). 4.1.4. Fibre Modern human diet has evolved from diets high in fruits, vegetables, lean meats, and seafood to processed foods high in sodium and hydrogenated fats and low in bre. These diet changes have affected dietary parameters related to health, resulting in an increase in obesity and chronic disease, including cardiovascular disease (CVD), diabetes, and cancer (Jew, AbuMweis, & Jones, 2009). Dietary bre obtained from plants is considered a functional ingredient because it provides several health benets beyond bowel regularity. These benets may include digestive health, weight management, cardiovascular health, and general wellness. These facts have increased the interest of researchers and the food industry to offer healthy food products while preserving their sensorial acceptance (Viuda-Martos et al., 2010). Adding 10e30 g/kg of rice bran to frankfurter sausage did not affect its shelf life. Total viable cells, anaerobic, and psychrotrophic bacteria showed a low growth rate and longer lag time (Heo, Kim, Choi, Kim, & Paik, 2009). White and red grape dietary bre concentrate (GDF) is obtained from wine industry residues and is considered a potential functional ingredient for the enrichment of foods because of its high concentration of dietary bre with a high-soluble/insoluble dietary bre ratio and associated bioactive compounds. Adding 20e40 g/kg

GDF to minced sh muscle from horse mackerel (Trachurus trachurus) improved water and oil retention, lipid stabilisation, and cooking yield during frozen storage at 20  C for six months. Although GDF showed a good dispersion in the protein matrix according to scanning electronic microscopy (SEM), the matrix was more discontinuous compared to control samples and was associated with an increase in aggregation of myobrillar proteins during frozen storage. Samples containing 20 g/kg GDF scored highest in overall acceptance compared to control samples (Sanchez-Alonso & Borderias, 2008; Sanchez-Alonso, Solas, & Borderias, 2007). The use of wheat bre in surimi as a healthy ingredient at 30 and 60 g/kg with different particle sizes decreased the strength, cohesiveness, and water binding capacity of surimi gels and was associated with the formation of a non-homogeneous protein net observed by SEM. The concentration and particle sizes of bre did not change the appearance but affected the texture of the gel. Fibre with large particle sizes protected surimi from the loss of gel strength and hardness during freezing (Sanchez-Alonso, HajiMaleki, & Borderias, 2006). Adding bre into minced hake (Merluccius merluccius) and horse mackerel (T. trachurus) muscle increased the WHC when water was not added to maintain the moisture constant, but even in these conditions, rigidity and cohesiveness were lower for products containing bre than control samples (Sanchez-Alonso, Haji-Maleki, & Borderias, 2007). Chicory root inulin, a soluble bre, has been used as an additive in restructured sh products with a detriment to mechanical properties, specically hardness. This negative effect can be avoided by adding 20 g/kg carrageenan, but it was not compatible with MTG (Cardoso, Mendes, & Nunes, 2007a, 2007b, 2008; Cardoso, Mendes, Pedro, & Nunes, 2008; Cardoso, Mendes, Vaz-Pires, & Nunes, 2009). Pea bre can be added to minced sh and surimi up to 40 g/kg to obtain restructured products without modifying the textural and functional properties. It was compatible with up to 20 g/kg carrageenan, allowing increased hardness of restructured hake products. Pea bre was compatible with MTG at 1 g/kg or above, and it improved the textural properties of surimi gels from Atlantic mackerel (Scomber scombrus) and chub mackerel (Scomber japonicus) (Cardoso et al., 2007a, 2007b, 2009; Cardoso, Mendes, & Nunes, 2008). 4.1.5. Others Adding 10 g/kg chitosan to kamaboko gels from grass carp (Ctenopharyngodon idella) allowed an increase in hardness, springiness, cohesiveness, chewiness, adhesiveness, whiteness, WHC, and TBA while decreasing peroxide value and bacterial growth. The preservative function was related to the molecular weight of chitosan. Relatively low molecular weight chitosan showed a higher antioxidant capacity than high molecular weight chitosan. However, a mixture of 300 and 10 kDa chitosan exhibited the highest antibacterial activity (Mao & Wu, 2007; Wu & Mao, 2009). 4.2. Proteins 4.2.1. Effect of proteins on restructured products Whey protein concentrate (WPC) at 10e30 g/kg inhibited the autolytic modori phenomenon, associated with the activity of endogenous proteases activated at 60 and 65  C in surimi from bigeye snapper (P. tayenus), goatsh (Mulloidichthys vanicolensis), threadn bream (Nemipterus bleekeri), and lizardsh (Saurida tumbil). Adding WPC decreased the amount of hydrolysed protein, as demonstrated by the decrease in trichloroacetic acid-soluble peptide content, the higher level of myosin heavy chain and the better mechanical and functional properties of the surimi gels.

Fig. 3. Effect of the ALM pectin concentration on the rmness (close circles) and consistency (open circles) of solubilised sh pastes. Bars show standard deviation. Adapted from Uresti et al. (2003).

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However, WPC at 30 g/kg affected the colour attributes, decreasing the whiteness of gels (Rawdkuen & Benjakul, 2008). Adding WPC in combination with calcium chloride (50 mmol/kg) improved the mechanical and functional properties of surimi gels from goatsh (M. vanicolensis) obtained by incubating surimi paste at 40  C before cooking (Benjakul, Yarnpakdee, Visessanguan, & Phatcharat, 2010). Beef plasma protein (BPP) added at 10e30 g/kg improved the mechanical properties of red tilapia surimi gels obtained by setting at 40  C for 90 min followed by heating at 90  C for 30 min. However, the whiteness of gels decreased when the concentration of BPP was increased (Duangmal & Taluengphol, 2010). Similar results were obtained by adding BPP to surimi gels from arabesque greenling (Pleurogrammus azonus) and walleye pollock (Theragra chalcogramma). The mechanical properties of these surimi gels increased when 10e30 g/kg BPP was added to solubilised pastes and incubated at 25  C for up to 15 h before cooking at 90  C for 30 min (Kato et al., 2010). Soy protein isolate (SPI) modied the textural properties of surimi gels from silver carp (Hypophthalmichthys molitrix) and grass carp (C. idella). SPI negatively affected the mechanical properties of surimi gels obtained by setting sh pastes at 30 and 40  C for 60 min before heating at 85  C for 30 min. The mechanical properties decreased when the protein concentration increased (100e400 g/kg). However, adding 100 g/kg SPI improved the mechanical properties of surimi gels obtained by incubating sh pastes at 50  C for 60 min before heating at 85  C for 30 min (Luo, Shen, & Pan, 2006; Luo, Shen, Pan, & Bu, 2008). Egg white (EW) added at 10e30 g/kg improved the mechanical properties of red tilapia surimi gels obtained by setting at 40  C for 90 min followed by heating at 90  C for 30 min, as well as for surimi gels from arabesque greenling (P. azonus) and walleye pollock (T. chalcogramma), incubated at 25  C for up to 15 h before cooking at 90  C for 30 min (Duangmal & Taluengphol, 2010; Kato et al., 2010). Special dried egg white showed a larger effect on the mechanical properties of surimi gels from Pacic whiting (Merluccius productus) and Alaska pollock (T. chalcogramma), as compared to regular dried egg white and liquid egg white. Adding egg white with cryoprotectants before freezing for 12 months was less efcient at improving the mechanical properties of surimi gels than adding 20e30 g/kg egg white during chopping of solubilised pastes (Hunt, Park, & Handa, 2009). Sarcoplasmic protein can be obtained from washing operations during surimi processing. This muscle fraction contains substantial transglutaminase activity, which could be used for catalysing the protein cross-linking of myobrillar proteins, improving the mechanical properties of surimi gels. MTG could be concentrated by ultraltration using a 30 kDa membrane, increasing the total activity without affecting the specic activity. Adding tilapia (O. niloticus) sarcoplasmic proteins increased the mechanical properties of lizardsh surimi gels when produced by setting at 37  C for 1 h before cooking (Yongsawatdigul & Piyadhammaviboon, 2007). Adding common carp (Cyprinus carpio) sarcoplasmic proteins (Sp-P) improved the mechanical properties of gels from threadn bream surimi at constant moisture and myobrillar levels. Although adding Sp-P did not interfere with myobrillar proteins during the solegel transition phase, this did enhance the textural quality of kamaboko. However, the addition of Sp-P from the dark muscle of the carp decreased the whiteness of the surimi (Jafarpour & Gorczyca, 2009). Soluble proteins from surimi wash water (SWW) can be insolubilised by complexing with chitosanealginate, allowing its recovery and the reduction of suspended organic matter in water discharged from surimi processing plants. Adding 10e30 g/kg of pacic whiting SWW recovered with chitosanealginate (chiealg

SWW) into Alaska pollock (T. chalcogramma) grade FA surimi pastes allowed for the improvement in the mechanical properties of surimi gels, but decreased the WHC and slightly increased the redness, an undesirable effect in the production of Alaska pollock grade FA surimi (Velazquez et al., 2007). Pacic whiting SWW recovered with chitosanealginate at 10 g/kg slightly improved the mechanical properties of grade A Pacic whiting surimi gels with a minimal effect on colour. Higher concentrations resulted in quality deterioration, poor mechanical properties, and changes in colour. Myoglobin, a sarcoplasmic protein, extracted from Pacic sardine decreased the mechanical properties of Pacic whiting surimi gels when added at 2 g/kg. However, it showed a synergistic effect when added at 10 g/kg together with 10 g/kg of beef plasma protein, increasing surimi gel strength (Park & Park, 2007). Myoglobin from tuna was able to bound tuna and sardine myosin proteins as a function of storage time at 4  C for up to 24 h, inducing a higher oxidation of oxymyoglobin and loss in the Ca2-ATPase activity of myosin (Chaijan, Benjakul, Visessanguan, & Faustman, 2007). Fish gelatin is a commercially available food additive obtained after hydrolysis of collagen from sh. Fish gelatin had a disruptive effect on the mechanical properties of grade A or FA surimi gels (Alaska pollock) when added at 15 g/kg in solubilised surimi pastes, incubated at 40  C for 30 min followed by cooking at 90  C for 15 min. However, sh gelatin had no effect on the mechanical properties when added at 5e10 g/kg. The same effect was observed in the expressible water (Fig. 4) when only 15 g/kg gave a statistical difference (Hernandez-Briones, Velazquez, Vazquez, & Ramirez, 2009). Insoluble proteins recovered by centrifugation from Pacic whiting surimi wash water, consisting mainly of myobrillar proteins, were added at 10e50 g/kg into Alaska pollock grade FA surimi. The insoluble proteins increased the mechanical properties of surimi gels, but affected WHC and caused slight changes in colour attributes (Ramrez, Velazquez, Lopez-Echevarria, & Torres, 2007; Velazquez et al., 2008). 4.2.2. Effects of proteins in low-salt restructured products A decrease in salt concentration has a negative effect on protein extractability and solubility, resulting in poor mechanical properties. The protein solubilised and extracted during blending also serves as a substrate for cross-linking reactions by endogenous and microbial transglutaminase (Andrs-Bello, Garca-Segovia, Ramrez, & Martnez-Monz, in press; Sun, 2009). The effect of adding 10 g/kg of whey protein concentrate (WPC) and 10 g/kg of sodium caseinate (Na-caseinate) was studied in

Fig. 4. Effect of sh gelatin on expressible water content of surimi gels. Different letters indicate signicant differences between treatments (P 0.05). Adapted from Hernandez-Briones et al. (2009).

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J.A. Ramrez et al. / Food Hydrocolloids 25 (2011) 1842e1852 Cardoso, C., Mendes, R., & Nunes, M. L. (2007b). Effect of transglutaminase and carrageenan on restructured sh products containing dietary bres. International Journal of Food Science and Technology, 42, 1257e1264. Cardoso, C., Mendes, R., & Nunes, M. L. (2008). Development of a healthy low-fat sh sausage containing dietary bre. International Journal of Food Science and Technology, 43, 276e283. Cardoso, C., Mendes, R., Pedro, S., & Nunes, M. L. (2008). Quality changes during storage of sh sausages containing dietary ber. Journal of Aquatic Food Product Technology, 17, 73e95. Cardoso, C., Mendes, R., Vaz-Pires, P., & Nunes, M. L. (2009). Effect of dietary bre and MTG on the quality of mackerel surimi gels. Journal of the Science of Food and Agriculture, 89, 1648e1658. Castro-Briones, M., Caldern, G. N., Velazquez, G., Salud-Rubio, M., Vzquez, M., & Ramrez, J. A. (2009). Mechanical and functional properties of restructured beef products obtained with microbial transglutaminase using pre-heating and cold binding treatments. Meat Science, 83, 229e238. Chai, P. P., & Park, J. W. (2007). Physical properties of sh proteins cooked with starches or protein additives under ohmic heating. Journal of Food Quality, 30, 783e796. Chaijan, M., Benjakul, S., Visessanguan, W., & Faustman, C. (2007). Interaction between sh myoglobin and myosin in vitro. Food Chemistry, 103, 1168e1175. Cofrades, S., Ayo, J., Serrano, A., Carballo, J., & Jimnez, C. F. (2006). Walnut, microbial transglutaminase and chilling storage time effects on salt-free beef batter characteristics. European Food Research Technology, 222, 458e466. Duangmal, K., & Taluengphol, A. (2010). Effect of protein additives, sodium ascorbate, and microbial transglutaminase on the texture and colour of red tilapia surimi gel. International Journal of Food Science and Technology, 45, 48e55. Fu, J. T., & Rao, M. A. (2001). Rheology and structure development during gelation of low-methoxyl pectin gels: the effect of sucrose. Food Hydrocolloids, 15, 93e100. Fukushima, H., Okazaki, E., Fukuda, Y., & Watabe, S. (2007). Rheological properties of selected sh paste at selected temperature pertaining to shaping of surimibased products. Journal of Food Engineering, 81, 492e499. Gomez-Guilln, C., Borderias, A. J., & Montero, P. (1997). Thermal gelation properties of two different composition sardine (Sardina pilchardus) muscles with addition of non-muscle and hydrocolloids. Food Chemistry, 58, 81e87. Hamman, D. D., & Lanier, T. C. (1987). Instrumental methods for predicting seafood sensory texture quality. In D. E. Kramer, & J. Liston (Eds.), Seafood quality determination (pp. 123e136). Amsterdam, Netherlands: Elsevier Science Publishers BV. Hemung, B. O., Li-Chan, E. C. Y., & Yongsawatdigul, J. (2008). Thermal stability of sh natural actomyosin affects reactivity to cross-linking by microbial and sh transglutaminases. Food Chemistry, 111, 439e446. Heo, C., Kim, H. W., Choi, Y. S., Kim, C. J., & Paik, H. D. (2009). Shelf-life estimation of frankfurter sausage containing dietary ber from rice bran using predictive modeling. Korean Journal for Food Science of Animal Resources, 29, 47e54. Hernandez-Briones, A., Velazquez, G., Vazquez, M., & Ramirez, J. A. (2009). Effects of adding sh gelatin on Alaska pollock surimi gels. Food Hydrocolloids, 23, 2446e2449. Hunt, A., Getty, K. J. K., & Park, J. W. (2009). Roles of starch in surimi seafood: a review. Food Reviews International, 25, 299e312. Hunt, A., Park, J. W., & Handa, A. (2009). Effect of various types of egg white on characteristics and gelation of sh myobrillar proteins. Journal of Food Science, 74, C683eC692. Jafarpour, A., & Gorczyca, E. M. (2009). Characteristics of sarcoplasmic proteins and their interaction with surimi and kamaboko gel. Journal of Food Science, 74, N16eN22. Jafarpour, A., & Gorczyca, E. M. (2008). Alternative techniques for producing a quality surimi and kamaboko from common carp (Cyprinus carpio). Journal of Food Science, 73, E415eE424. Jew, S., AbuMweis, S. S., & Jones, P. J. H. (2009). Evolution of the human diet: linking our ancestral diet to modern functional foods as a means of chronic disease prevention. Journal of Medicinal Food, 12, 925e934. Jiang, S. T., Leu, S. Z., & Tsai, G. J. (1998). Cross-linking of mackerel surimi actomyosin by microbial transglutaminase and ultraviolet irradiation. Journal of Agricultural and Food Chemistry, 46, 5278e5282. Jung, Y. H., Kim, W. W., & Yoo, B. (2007). Effect of acetylated rice starch on rheological properties of surimi sol and gel. Food Science and Biotechnology, 16, 817e821. Karayannakidis, P. D., Zotos, A., Petridis, D., & Taylor, K. D. A. (2008). The effect of washing, microbial transglutaminase, salts and starch addition on the functional properties of sardine (Sardina pilchardus) kamaboko gels. Food Science and Technology International, 14, 167e177. Kasapis, S. (2009). Developing minced sh products of improved eating quality: an interplay of instrumental and sensory texture. International Journal of Food Properties, 12, 11e26. Kato, N., Suzuki, Y., Kunimoto, M., Kitakami, S., Murakami, Y., & Arai, K. (2010). Comparison of effects of plasma and albumen powders on the physical property of heated gels formed from salt-ground of three species sh frozen surimi. Journal of the Japanese Society for Food Science and Technology e Nippon Shokuhin Kagaku Kogaku Kaishi, 57, 26e31. Kim, B. Y., Hamman, D. E., Lanier, T. C., & Wu, M. C. (1986). Effects of freeze-thaw abuse on the viscosity and gel-forming properties of surimi from two species. Journal of Food Science, 51(4), 951e956.

restructured products from silver carp (H. molitrix) at three salt concentrations (0, 10, and 20 g/kg). Dairy protein additives were added alone or in combination with MTgase at 3 g/kg. The mechanical properties and WHC of restructured products decreased when the salt concentration decreased. Sodium caseinate was more efcient than WPC in improving the mechanical properties of restructured products at each level of salt studied, as compared to control samples. The WHC was not improved by adding any of the dairy proteins. In the low-salt (10 g/kg NaCl) product, higher values of hardness were obtained by adding MTG and dairy proteins than by adding only MTG, suggesting a positive interaction between meat proteins, dairy proteins, and MTG. The last required the addition of salt to sh paste to improve the mechanical properties. Unsalted and low-salt restructured products supplemented with NA-caseinate or WPC and MTG showed better mechanical properties and WHC than control products obtained only with MTG. In products containing 20 g/kg NaCl, samples containing only MTG showed equal or better mechanical properties than samples containing MTG and dairy proteins (Uresti, Tllez-Luis, Ramrez, & Vzquez, 2004). WPC added at 10 g/kg showed a small effect in improving the mechanical properties of regular and low-salt restructured products from Mexican ounder (C. chittendenni) (Ramrez, Del ngel, Velzquez, & Vzquez, 2006). 5. Conclusions The applications for food hydrocolloids in sh products offer new opportunities to develop novel products based on surimi or restructured product technology. These products can include the new low-salt requirements for healthy food. Acknowledgements The authors are grateful to Xunta de Galicia (Spain) for the nancial support of this work (Project 10TAL402001PR) and the FEDER founds of the European Union. References
An, H., Peters, M. Y., & Seymour, T. A. (1996). Roles of endogenous enzymes in surimi gelation. Trends in Food Science and Technology, 7, 321e327. Andrs-Bello, A., Garca-Segovia, P., Ramrez, J. A., & Martnez-Monz, J. Production of cold-setting restructured sh products from gilthead sea bream (Sparus aurata) using microbial transglutaminase and regular and low-salt level. CyTA e Journal of Food, in press. doi:10.1080/19476337.2010.485701. Asagami, T., Ogiwara, M., Wakameda, A., & Noguchi, S. F. (1995). Effect of microbial transglutaminase on the quality of frozen surimi made from various kinds of sh species. Fish Science, 61, 267e272. Barrera, A. M., Ramrez, J. A., Gonzlez-Cabriales, J. J., & Vzquez, M. (2002). Effect of pectins on the gelling properties of surimi from silver carp. Food Hydrocolloids, 16, 441e447. Benjakul, S., Phatcharat, S., Tammatinna, A., Visessanguan, W., & Kishimura, H. (2008). Improvement of gelling properties of lizardsh mince as inuenced by microbial transglutaminase and sh freshness. Journal of Food Science, 73, S239eS246. Benjakul, S., Yarnpakdee, S., Visessanguan, W., & Phatcharat, S. (2010). Combination effects of whey protein concentrate and calcium chloride on the properties of goatsh surimi gel. Journal of Texture Studies, 41, 341e357. Borderas, A. J., & Prez-Mateos, M. (1996). Productos pesqueros reestructurados. Alimentaria, 269, 53e62. Boyer, C., Joandel, S., Ouali, A., & Culioli, J. (1996). Ionic strength effects on heatinduced gelation of myobrils and myosin from fast- and slow-twitch rabbit muscles. Journal of Food Science, 61, 1143e1148. Boyer, C., Joandel, S., Roussilhes, V., Culioli, J., & Ouali, A. (1996). Heat-induced gelation of myobrillar proteins and myosin from fast- and slow-twitch rabbit muscles. Journal of Food Science, 61, 1138e1142, 1164. Buchert, J., Ercili-Cura, D., Ma, H., Gasparetti, C., Monogioudi, E., Faccio, G., et al. (2010). Crosslinking food proteins for improved functionality. Annual Reviews of Food Science and Technology, 1, 113e138. Cardoso, C., Mendes, R., & Nunes, M. L. (2007a). Dietary bers effect on the textural properties of sh heat-induced gels. Journal of Aquatic Food Product Technology, 16, 19e30.

Author's personal copy

J.A. Ramrez et al. / Food Hydrocolloids 25 (2011) 1842e1852 Kumazawa, Y., Seguro, K., Takamura, M., & Motoki, M. (1993). Formation of 3-(gglutamyl) lysine cross-link in cured horse mackerel meat induced by drying. Journal of Food Science, 58, 1062e1064, 1083. Kuraishi, C., Sakamoto, J., Yamazaki, K., Susa, Y., Kuhara, C., & Soeda, T. (1997). Production of restructured meat using microbial transglutaminase without salt or cooking. Journal of Food Science, 62, 488e490. Ledward, D. A. (1994). Proteinepolysaccharide interactions. In N. S. Hettiarachchy, & G. R. Ziegler (Eds.), Protein functionality in food systems IFT basic symposium series. New York: Marcel Dekker, Inc. Lee, C. M. (1984). Surimi process technology. Food Technology, 38, 69e80. Lee, C. M., Wu, M. M., & Okada, M. (1992). Ingredient and formulation technology for surimi-based products. In T. C. Lanier, & C. M. Lee (Eds.), Surimi technology (pp. 273e302). New York: Marcel Dekker. Lee, H. G., Lanier, T. C., Hamann, D. D., & Knopp, J. A. (1997). Transglutaminase effects on low temperature gelation of sh protein sols. Journal of Food Science, 62, 20e24. Lee, H. G., & Park, J. W. (1998). Calcium compounds to improve gel functionality of Pacic whiting and Alaska pollock surimi. Journal of Food Science, 53, 969e974. Luo, Y. K., Kuwahara, R., Kaneniwa, M., Murata, Y., & Yokoyama, M. (2001). Comparison of gel properties of surimi from Alaska pollock and three freshwater sh species: effects of thermal processing and protein concentration. Journal of Food Science, 66, 548e554. Luo, Y. K., Shen, H. X., & Pan, D. D. (2006). Gel-forming ability of surimi from grass carp (Ctenopharyngodon idellus): inuence of heat treatment and soy protein isolate. Journal of the Science of Food and Agriculture, 86, 687e693. Luo, Y. K., Shen, H. X., Pan, D. D., & Bu, G. H. (2008). Gel properties of surimi from silver carp (Hypophthalmichthys molitrix) as affected by heat treatment and soy protein isolate. Food Hydrocolloids, 22, 1513e1519. Mao, L. C., & Wu, T. (2007). Gelling properties and lipid oxidation of kamaboko gels from grass carp (Ctenopharyngodon idellus) inuenced by chitosan. Journal of Food Engineering, 82, 128e134. Martin-Sanchez, A. M., Navarro, C., Perez-Alvarez, J. A., & Kuri, V. (2009). Alternatives for efcient and sustainable production of surimi: a review. Comprehensive Reviews in Food Science and Food Safety, 8, 359e374. Mishra, S., Mann, B., & Joshi, B. K. (2001). Functional improvement of whey protein concentrate on interaction with pectin. Food Hydrocolloids, 15, 9e16. Morales, O. G., Ramrez, J. A., Vivanco, D. I., & Vzquez, M. (2001). Surimi of sh species from the Gulf of Mxico: evaluation of the setting phenomenon. Food Chemistry, 75, 43e48. Moreno, H. M., Carballo, J., & Borderias, A. J. (2009). Study of two different cold restructuring processes using two different qualities of hake (Merluccius capensis) muscle, with addition of microbial transglutaminase. Journal of the Science of Food and Agriculture, 89, 1346e1351. Moreno, H. M., Carballo, J., & Borderias, J. (2010). Gelation of sh muscle using microbial transglutaminase and the effect of sodium chloride and pH levels. Journal of Muscle Foods, 21, 433e450. Morris, V. J. (1998). Gelation of polysaccharides. In S. E. Hill, D. A. Ledward, & J. R. Mithell (Eds.), Functional properties of food macromolecules (pp. 143e226). Gaithersburg, MD: Aspen Publishers. Motzer, E. A., Carpenter, J. A., Reynolds, E., & Lyon, C. E. (1998). Quality of restructured hams manufactured with PSE pork as affected by water binders. Journal of Food Science, 63, 1007e1011. Narhinen, M., Nissinen, A., Penttila, P. L., Somonen, O., Cernerud, I., & Puska, P. (1998). Salt content labeling of foods in supermarkets in Finland. Agricultural and Food Science in Finland, 7, 447e453. Noriega-Rodrguez, J. A., Ortega-Garca, J., Angulo-Guerrero, O., Garca, H. S., Medina-Jurez, L. A., & Gmez-Meza, N. (2009). Oil production from sardine (Sardinops sagax caerulea). CyTA e Journal of Food, 7, 173e179. Ohtsuka, T., Umezawa, Y., Nio, N., & Kubota, K. (2001). Comparison of deamidation activity of transglutaminases. Journal of Food Science, 66, 25e29. Pacheco-Aguilar, R., Ocano-Higuera, V. M., Ezquerra-Brauer, J. M., Castillo-Yaez, F. J., Garca-Snchez, G., & Marquez-Rios, E. (2010). Partial characterization of 50 nucleotidase from giant squid (Dosidicus gigas) mantle. CyTA e Journal of Food, 7, 173e179. Park, J. D., & Park, J. W. (2007). Extraction of sardine myoglobin and its effect on gelation properties of pacic whiting surimi. Journal of Food Science, 72, C202eC207. Park, J. W. (2000). Ingredient technology and formulation development. In J. W. Park (Ed.), Surimi and surimi seafood (pp. 343e391). New York, NY: Marcel Dekker. Ramrez, J., Uresti, R., Tllez-Luis, S., & Vzquez, M. (2002). Using salt and microbial transglutaminase as binding agents in restructured sh products resembling hams. Journal of Food Science, 67, 1778e1784. Ramrez, J. A., Barrera, M., Morales, O. G., & Vzquez, M. (2002). Effect of xanthan gum and locust bean gums on the gelling properties of myobrillar protein. Food Hydrocolloids, 16, 11e16. Ramrez, J. A., Del ngel, A., Uresti, R. M., Velzquez, G., & Vzquez, M. (2007). Low-salt restructured sh products using low-value sh species from the Gulf of Mexico. International Journal of Food Science and Technology, 42, 1039e1045. Ramrez, J. A., Del ngel, A., Velzquez, G., & Vzquez, M. (2006). Production of lowsalt restructured sh products from Mexican ounder (Cyclopsetta chittendeni) using microbial transglutaminase or whey protein concentrate as binders. European Food Research and Technology, 223, 341e345.

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Ramrez, J. A., Garca-Carreo, F. L., Morales, O. G., & Snchez, A. (2002). Inhibition of modori-associated proteinases by legume seed extracts in surimi production. Journal of Food Science, 67, 578e581. Ramrez, J. A., Martn-Polo, M. O., & Bandman, E. (2000). Fish myosin aggregation as affected by freezing and initial physical state. Journal of Food Science, 65, 556e560. Ramrez, J. A., Rodrguez-Sosa, R., Morales, O. G., & Vzquez, M. (2000). Surimi gels from striped mullet (Mugil cephalus) employing microbial transglutaminase. Food Chemistry, 70, 443e449. Ramrez, J. A., Santos, I. A., Morales, O. G., Morrisey, M. T., & Vzquez, M. (2000). Application of microbial transglutaminase to improve mechanical properties of surimi from silver carp. Ciencia y Tecnologa Alimentaria, 3, 21e28. Ramrez, J. A., Velazquez, G., Lopez-Echevarria, G., & Torres, J. A. (2007). Effect of adding insoluble solids from surimi wash water on the functional and mechanical properties of Pacic whiting grade A surimi. Bioresource Technology, 98, 2148e2153. Ramos-Martnez, E., Morales-Gonzlez, O. M., Ramrez, J. A., Garca-Carreo, F. L., & Montejano-Gaitn, J. G. (1999). Determination of the modori phenomenon and its origin in surimi of ve sh species from the Gulf of Mexico. Food Science and Technology International, 5, 397e405. Rawdkuen, S., & Benjakul, S. (2008). Whey protein concentrate: autolysis inhibition and effects on the gel properties of surimi prepared from tropical sh. Food Chemistry, 106, 1077e1084. Snchez, A., Ramrez, J. A., Morales, O. G., & Montejano, J. G. (1998). Deteccin de inhibidores de proteasas en extractos de leguminosas y su efecto sobre proteasas endgenas del msculo de pescado. Ciencia y Tecnologa Alimentaria, 2, 12e19. Sanchez-Alonso, I., & Borderias, A. J. (2008). Technological effect of red grape antioxidant dietary bre added to minced sh muscle. International Journal of Food Science and Technology, 43, 1009e1018. Sanchez-Alonso, I., Haji-Maleki, R., & Borderias, A. J. (2006). Effect of wheat bre in frozen stored sh muscular gels. European Food Research and Technology, 223, 571e576. Sanchez-Alonso, I., Haji-Maleki, R., & Borderias, A. J. (2007). Wheat ber as a functional ingredient in restructured sh products. Food Chemistry, 100, 1037e1043. Sanchez-Alonso, I., Solas, M. T., & Borderias, A. J. (2007). Physical study of minced sh muscle with a white-grape by-product added as an ingredient. Journal of Food Science, 72, E94eE101. Shao, C. H., Avens, J. S., Schmidt, G. R., & Maga, J. A. (1999). Functional, sensory, and microbiological properties of restructured beef and emu steaks. Journal of Food Science, 64, 1052e1054. Sun, X. D. (2009). Utilization of restructuring technology in the production of meat products: a review. CyTA e Journal of Food, 7, 153e162. Susuki, T. (1981). Fish and krill protein processing technology. London: Applied Science Publishers Ltd. Sych, J., Lacroix, C., Adambounou, L. T., & Castaigne, F. (1990). Cryoprotective effects of some materials on cod-surimi proteins during frozen storage. Journal of Food Science, 55, 1222e1227. Tllez-Luis, S. J., Ramrez, J. A., & Vzquez, M. (2004). Application in restructured sh products of transglutaminase obtained by Streptoverticillium ladakanum in media made from hydrolysates of sorghum straw. Journal of Food Science, 69(1), M1eM5. Tllez-Luis, S. J., Uresti, R. M., Ramrez, J. A., & Vzquez, M. (2002). Low-salt restructured sh products using microbial transglutaminase. Journal of the Science of Food and Agriculture, 82, 953e959. Tolasa, S., Lee, C. M., & Cakli, S. (2010). Physical and oxidative stabilization of omega3 fatty acids in surimi gels. Journal of Food Science, 75, C305eC310. Tsai, S. J., Unklesbay, N., Unklesbay, K., & Clarke, A. (1998). Thermal properties of restructured beef products at different isothermal temperatures. Journal of Food Science, 63, 481e484. Tuankriangkrai, S., & Benjakul, S. (2010). Effect of modied tapioca starch on the stability of sh mince gels subjected to multiple freeze-thawing. Journal of Muscle Foods, 21, 399e416. Ueng, Y. E., & Chu, Y. J. (1996). Effect of dietary bers on cold resistance of surimi. Food Science (Taiwan), 23, 266e275. Uresti, R. M., Lpez-Arias, N., Gonzlez-Cabriales, J. J., Ramrez, J. A., & Vzquez, M. (2003). Use of amidated low methoxyl pectin to produce sh restructured products. Food Hydrocolloids, 17(2), 171e176. Uresti, R. M., Tllez-Luis, S. J., Ramrez, J. A., & Vzquez, M. (2004). Use of dairy proteins and microbial transglutaminase to obtain low- salt sh products from lleting waste from silver carp (Hypophthalmichthys molitrix). Food Chemistry, 86, 257e262. Velazquez, G., Miranda-Luna, P., Lpez-Echevarra, G., Vzquez, M., Torres, J. A., & Ramrez, J. A. (2007). Effect of recovered soluble proteins from Pacic whiting surimi wash water on the functional and mechanical properties of Alaska pollock surimi grade FA. Ciencia y Tecnologa Alimentaria, 5, 340e345. Velazquez, G., Miranda-Luna, P., Lpez-Echevarra, G., Vzquez, M., Torres, J. A., & Ramrez, J. A. (2008). Effect of Pacic whiting wash water proteins on Alaska pollock surimi gels. Journal of Textural Studies, 39, 296e308. Viuda-Martos, M., Lopez-Marcos, M. C., Fernandez-Lopez, J., Sendra, E., LopezVargas, J. H., & Perez-Alvarez, J. A. (2010). Role of ber in cardiovascular diseases: a review. Comprehensive Reviews in Food Science and Food Safety, 9, 240e258.

Author's personal copy

1852

J.A. Ramrez et al. / Food Hydrocolloids 25 (2011) 1842e1852 Yang, C. C., Chen, C. C., & Chang, H. M. (2001). Separation of egg white lysozyme by anionic polysaccharides. Journal of Food Science, 63, 962e965. Yetim, H., & Ockerman, W. (1995a). The effects of egg white, tumbling, and storage time on proximate composition and protein fractions of restructured sh product. Journal of Aquatic Food Product Technology, 4, 65e77. Yetim, H., & Ockerman, W. (1995b). The inuence of egg white and tumbling on proximate composition and protein fractions of fresh catsh muscle. Journal of Aquatic Food Product Technology, 3, 25e39. Yongsawatdigul, J., & Piyadhammaviboon, P. (2007). Gel-enhancing effect and protein cross-linking ability of tilapia sarcoplasmic proteins. Journal of the Science of Food and Agriculture, 87, 2810e2816. Yongsawatdigul, J., & Sinsuwan, S. (2007). Aggregation and conformational changes of tilapia actomyosin as affected by calcium ion during setting. Food Hydrocolloids, 21, 359e367. Zimmerman, P. A., Bissel, H. M., IV, & McIntosh, G. S. (1998). Arctic Alaska Seafoods Inc., issued on December 8, 1998. Method of processing salmonoid sh. U.S. patent 5,846,594.

Wu, M. C., Hamman, D. D., & Lanier, T. C. (1985). Rheological and colorimetric investigations on starchesh protein systems during thermal processing. Journal of Texture Studies, 16, 53e74. Wu, M. C., Lanier, T. C., & Hamman, D. D. (1985). Rigidity and viscosity changes of croaker actomyosin during thermal gelation. Journal of Food Science, 50, 14e19, 25. Wu, T., & Mao, L. C. (2009). Application of chitosan to maintain the quality of kamaboko gels made from grass carp (Ctenopharyngodon idellus) during storage. Journal of Food Processing and Preservation, 33, 218e230. Xiong, G. Q., Cheng, W., Ye, L. X., Du, X., Zhou, M., Lin, R. T., et al. (2009). Effects of konjac glucomannan on physicochemical properties of myobrillar protein and surimi gels from grass carp (Ctenopharyngodon idella). Food Chemistry, 116, 413e418. Yamamoto, H., Murakami, M., Nakachi, S., Nishino, Y., & Nishikawa, A. (2007). Effect of addition of rice starch on the stress-strain characteristics of heat-induced gel of frozen sh-meat (Surimi). Journal of the Japanese Society for Food Science and Technology e Nippon Shokuhin Kagaku Kogaku Kaishi, 54, 138e141.