Revista de Ciencias Biológicas y de la Salud http://biotecnia.unison.mx
Universidad de Sonora
ISSN: 1665-1456
1 Instituto Politecnico Nacional. CICATA-IPN Unidad Querétaro.
2 Tecnológico Nacional de México/ ITS Huichapán.
3 Universidad Autónoma de Tamaulipas. Unidad Académica de Trabajo Social y Ciencias para las Humanidades.
Propiedades de gelificación de carne de jaiba (Callinectes sapidus) adicionada con gelatina y transglutaminasa microbiana
Las proteínas de la carne de cangrejo generalmente se se- paran de su caparazón después de la cocción, lo que implica una agregación térmica tipo coágulo, que induce problemas relacionados con su capacidad de retención de agua, lo que limita sus alternativas de procesamiento posteriores. El ob- jetivo de este estudio fue determinar el efecto de la adición de gelatina y transglutaminasa microbiana (MTgasa) sobre las propiedades de geles obtenidos de carne de jaiba azul (Callinectes sapidus) previamente cocida. La carne de jaiba que se sometió a 3 ciclos de lavado-prensado con agua fría, utilizando una relación 3:1 agua-carne y se mezcló con 0 a 3
% de gelatina y 0.5 % de MTgasa, se embutió en tubos de ace- ro inoxidable y se cocieron a 90 ºC durante 15 min en agua caliente. Se determinaron las propiedades mecánicas (aná- lisis del perfil de textura, módulo de Young y tensión máxi- ma), color, agua extraíble e imágenes micrográficas (SEM). Los resultados mostraron que la gelatina interaccionó con las proteínas de la carne de jaiba y la MTgasa utilizó ambas proteínas como sustrato para formar una red estructurada. Las propiedades mecánicas del gel dependieron del nivel de gelatina añadido, con mejores resultados a menor cantidad. La cantidad de agua extraible se redujo mediante la adición de 3 % de gelatina.
Crab meat proteins are usually separated from shells after cooking, which induces a thermal coagulum-type aggrega- tion affecting the water-holding capacity and limiting further processing alternatives. This study aimed to evaluate the effect of adding gelatin and microbial transglutaminase (MT- gase) on the properties of gels obtained from cooked blue crab (Callinectes sapidus) meat. Crab meat was subjected to 3 washing-pressing cycles with cold water using a 3:1 (wa- ter:meat) ratio, mixed with 0 to 3 % gelatin and 0.5 % MTgase, stuffed into stainless steel tubes, and cooked by immersing in hot water at 90 ºC for 15 min. Mechanical properties (tex- ture profile analysis, Young modulus, and maximum stress), color, extractable water, and micrograph images (SEM) were
*Author for correspondence: Gonzalo Velazquez e-mail: gvelazquezd@ipn.mx
Received: April 23, 2024
Accepted: June 23, 2024
Published: August 15, 2024
obtained. Results showed that gelatin interacted with crab proteins, and MTgase used both proteins as substrates to form a structured network. The mechanical properties of gels depended on the level of gelatin added, with better results at a lower amount. The amount of extracted water was reduced by adding 3 % of gelatin.
Muscle protein gelling is a widely used technological process for developing different meat, poultry, and fish products. Dif- ferent conditions used in the process, such as temperature, pH, salt level, or additives, allow modifying the functional properties of the final products to develop or improve qual- ity parameters like texture, color, flavor, or stability (Ramírez et al., 2011).
Solubilization with salt and thermal denaturalization (unfolding) of the non-cooked muscle protein are required to form gel products (Uresti et al., 2005; Castro-Briones et al., 2009). However, meat extracted from crabs cannot follow such steps since these organisms are processed by high thermal treatment, inducing the denaturation and aggre- gation of proteins before being separated from the shell (Martínez et al., 2014). These steps hinder any further pro- cessing alternative for this important and abundant natural resource, with particular interest in the blue crab (Callinectes sapidus) of the Gulf of Mexico (Rodríguez-Castro et al., 2017; Morales-Azpetia et al., 2021), different than canning (Bouriga et al., 2023) or freezing (Ghribi et al., 2023) both with highly appreciated market for consumers. Different processes have been explored to solve this situation.
Baxter and Skonberg (2006) reported that cooked meat from Johan crab (Cancer borealis) could form gels using a 2-cycles washing-dewatering process, similar to the widely used technique to obtain surimi products. Similar behavior, but with weak gels, was obtained when cooked crab meat was centrifugated to remove the water-soluble protein fraction (tropomyosin being the most abundant extracted protein) (Baxter and Skonberg, 2008). Other processing techniques have been reported, such as a different cooking
Volumen XXVI
DOI: 10.18633/biotecnia.v26.2316
temperatures of crab meat in the range of 50 to 120 ºC, with better mechanical properties in gels obtained at higher precooking temperature (Martínez et al., 2014). microbial transglutaminase (MTgase) at 0.5 or 1.0 % has been reported as an alternative to reduce the washing-dewatered pressing cycles to just one, which still affects the characteristic flavor of the crab by removing the water-soluble fraction of meat (Hernández-Robledo et al., 2015; 2017). Gels with appropri- ate texture from cooked crab meat without removing the water-soluble fraction were obtained by mixing crab meat with MTgase at 60 ºC (Trejo-Díaz et al., 2021). However, all these methods using thermally induced gelling of crab meat result in gels with poor water holding capacity.
The objective of this work was to determine if gelatin combined with MTgase can improve the water holding ca- pacity of cooked crab meat proteins without affecting the mechanical properties of the gels.
The blue crab (Callinectes sapidus) was captured in Laguna Madre, Tamaulipas, transported, and processed at the facilities of the company “Integradora Pesquera Acuícola” located in San Fernando, Tamaulipas (México) within 24 h after caught. The crabs were cooked using a commercial autoclave and cooled with clean water. The crab meat was removed from shells, introduced into a plastic recipient, and transported on ice to the laboratory for further analysis.
Gelatin (GP 28, 290 bloom, Coloidales Duché, S.A DE CV. Ciudad de México, México) was purchased at a local market. The commercial microbial transglutaminase was Active TG-TI (Ajinomoto USA, Inc., Teaneck, NJ).
Cooked and minced crab meat was washed with water at a 3:1 (water: meat) ratio for 10 min at 4 ºC to dissolve soluble proteins, drained with a cotton fabric filter to remove the excess water containing the soluble compounds and stored in 250 g portions in polyethylene bags until analyzed.
Following the methodology reported by Hernández-Roble- do et al. (2017), the meat was mixed with gelatin (0, 0.5, 1, or 3 %) and MTgase (at 0 % as control or 0.5 %) using a food processor (Hamilton Beach Model 72860-MX, Glen Allen, VA, USA) for 3 min and stuffed into stainless steel tubes with cap in both extremes, closed, and immersed in hot water at 90 ºC for 30 min in a water bath with temperature control (Techne Tempette Junior TE-8J). After cooking, the tubes were im- mersed in ice water (0 ºC) and stored at 4 ºC until analyzed (less than 16 h).
A texturometer (Model TA Plus, Lloyd Instruments,
Ametek, UK) was used to perform the uniaxial compression test. Cylindrical gel samples (25 x 30 mm) were compressed to 75 % at 1 mm/s crosshead speed using a 50 mm aluminum probe (P50). The test was carried out at room temperature. Two compression cycles were used for texture profile anal- ysis (TPA). The hardness, cohesiveness, springiness, and chewiness parameters were calculated from the TPA curves. From the first compression cycle, stress-strain plots were obtained, and the Young modulus and maximum stress were calculated. Six replicates were analyzed for each treatment.
The L*, a*, b* CIELab color parameters of the samples were determined using a colorimeter (Bluemetric, model BLUE- HP200, SA de CV, Monterrey, Mexico) in four random points on each gel sample. From the measurements, a*, b*, L*, and the color attributes Hue* and Chroma* were calculated.
A 3 g sample from the crab meat gels was wrapped in 5 paper sheets of 6 cm x 6 cm, placed in 50 mL conical centrifuge tubes, and centrifuged at 15,000 rpm for 15 min (Rotofix 32 A. Hettich Zentrifugen, Tuttlingen, Germany) following the methodology reported by Hernández-Robledo et al. (2017). Subsequently, the final weight of the sample was registered. Four repetitions per treatment were performed. The EW was calculated using Equation 1.
EW = (Wi-Wf /Wi) x 100 (Eq. 1)
Where:
EW = amount of extracted water. Wi = Initial weight.
Wf = Final weight.
The crab meat gels were freeze-dried and ground. A sample was fixed on an aluminum pin using conductive double-sid- ed tape and then observed in an ambient scanning electron microscope (Phenom Pro., Phenom-World BV, Eindhoven, The Netherlands).
Data were analyzed using a factorial ANOVA and the post hoc Tukey test was performed to evaluate the significant effects of the treatments. Results are presented as mean ± standard deviation, and differences were considered statistically sig- nificant at a p < 0.05. Also, multiple regression analysis was performed to model the response of the gel properties as a function of the percentage of gelatin and MTgase using a second-order polynomial equation (Design Expert® v10, Stat- Ease, Inc., Minneapolis, MN, USA). Coefficients of the terms in the polynomial equation were calculated and 3D plots were used to describe the behavior of the analyzed properties.
Table 1. Experimental design.
Factors Levels
Gelatin concentration 0, 0.5, 1 and 3 %
MTgase concentration 0 % and 0.5 %
The heating process allowed gelling the crab meat despite meat proteins were previously denatured and aggregated due to the processing conditions required to separate of the meat from the shell.
The correlation values obtained from the multiple regression analysis are shown in Table 2. Hardness, cohesiveness, and chewiness showed R2 and adjusted R2 values higher than 0.9, indicating that the model fits adequately to data and that the model could be appropriate for future data.
Young modulus maximum stress, and expressible water fitted appropriately to the model (R2 > 0.9). The differences between R² and adjusted R² values are lower than 0.2 indicat- ing that the terms included in the polynomial models allow describing the effect of the parameters on these properties.
The model obtained for springiness did not fit well at any of both parameters, indicating that his property was not a good indicator to observe changes in mechanical properties after adding gelatin. Springiness is not the same as elasticity, because this test may involve the fracture of the sample
affecting its capacity to return to its original form (Rahman et al., 2021). Young modulus, on the other hand, is associated with elasticity because it considers the compression values (stress and strain) involved in the linear region of the test im- plying only a small deformation (Lam et al., 2017) that does not fracture (macro or micro) the sample, thus its deforma- tion theoretically is reversible and the sample should return to its original shape.
The analysis of variance (ANOVA) for the fitting of the gelatin and MTgase effect on mechanical and extractable wa- ter is shown in Table 3. Models differ significantly (at p < 0.05) for changes induced in hardness, cohesiveness, chewiness, Young modulus, and maximum stress. Gelatin significantly affected these parameter (p < 0.05) except for expressible water. However, MTgase did not affect any parameter, and there was no significant effect on the interaction of gelatin and MTgase on any studied property. The quadratic term (A2) suggests that gelatin had a higher effect on the mechanical properties than in expressible water.
Figure 1 shows the changes in the texture profile analysis pa- rameter. The hardness of gels was not affected by the MTgase level (0 to 0.5 %); however, it was negatively affected by the addition of low levels of gelatin (less than 2 % as calculated for the model). Gelatin added at 3 % improved the hardness
Table 2. Coefficients of the regression model for hardness (N), cohesiveness, springiness, chewiness (N), Young modulus (MPa), maximum stress (MPa) and expressible water, of gels from crab meat added with gelatin and MTgase.
Factor | Hardness | Cohesiveness | Springiness | Chewiness (N) | Young modulus | Maximum | EW |
(N) | (MPa) | stress (MPa) | (%) | ||||
Gelatin | |||||||
Intercept | 11.77 | 0.2169 | 0.7402 | 0.6142 | 78.93 | 17.9 | 11.72 |
A-Gelatin | -8.19 | -0.0788 | -0.0022 | -4.14 | 36.9 | 9.06 | -9.47 |
B-MTgase | 3.39 | -0.0059 | 0.0144 | 0.7807 | 7.93 | 1.2 | 1.96 |
AB | -2.56 | -0.0163 | 0.0031 | -1.11 | 4.65 | 2.55 | 0.2864 |
A2 | 26.46 | 0.1092 | -0.0122 | 8.97 | 4.52 | 10.49 | 10.36 |
R2 | 0.9595 | 0.9658 | 0.435 | 0.9595 | 0.9356 | 0.9499 | 0.8933 |
Adjusted R2 | 0.9055 | 0.9203 | -0.3183 | 0.9055 | 0.8497 | 0.8832 | 0.7511 |
Table 3. Statistical significance (p-value) for hardness, cohesiveness, springiness, chewiness, Young modulus, maximum stress, and expressible water of gels from crab meat added with gelatin and MTgase obtained from the ANOVA of the regression model.
(N)
Factor Hardness
Cohesiveness Springiness Chewiness
(N)
Gelatin
Young modulus (MPa)
Maximum stress (MPa)
EW (%)
Model | 0.0199* | 0.0155* | 0.7018 | 0.0199* | 0.0393* | 0.0272* | 0.0815 |
A-Gelatin | 0.0206* | 0.0037* | 0.881 | 0.0089* | 0.0091* | 0.0116* | 0.0187* |
B-MTgase | 0.0946 | 0.4810 | 0.2551 | 0.2333 | 0.1908 | 0.4133 | 0.3009 |
AB | 0.2420 | 0.1753 | 0.8265 | 0.1904 | 0.4871 | 0.2045 | 0.8933 |
A2 | 0.0054* | 0.0106* | 0.6784 | 0.0071* | 0.7356 | 0.0491* | 0.0843 |
*Indicates statistical significance.
of gels, but it was not enough to recover the initial param- eters of samples obtained without this hydrocolloid (Figure 1A).
Cohesiveness (Figure 1B) and chewiness (Figure 1D) showed a similar behavior to hardness, with an initial de- crease as affected by the addition of 2 % gelatin and a slight increase when added at 3 %. As mentioned previously, when modeling was discussed, an interaction between MTgase and gelatin was not observed. Crab gels showed relatively high values of springiness (72 %), and this parameter was not affected by the addition of MTgase, gelatin, or their combina- tion (Figure 1C).
Small changes in mechanical properties of crab meat gels, when 0.6 % MTgase was added and cooked directly at 90 ºC (by immersion in hot water), were reported previously. However, better mechanical properties were found when gels from crab meat containing MTgase were incubated at 40 ºC for 30 min. This behavior was associated with side-to- side protein aggregations promoted by covalent bondings of adjacent proteins as a result of MTgase activity during
incubation at 40 ºC (Martínez et al., 2014).
The disruptive effect of gelatin on the mechanical prop- erties was also observed in gels obtained from Alaska pollock surimi (Hernández-Briones et al., 2009).
Young modulus (Figure 2A) and maximum stress (Figure 2B) showed a different behavior than TPA parameters. These mechanical properties increased when both MTgase and gelatin were added, and showed a combined effect when added at their maximum level (0.5 % and 3 %, respectively). Differences between both mechanical parameters are asso- ciated with the basis of each test. TPA simulates the textural perception in the mouth while a meal is being chewed, while Young modulus and maximum stress, as mentioned previ- ously, are fundamental tests (Rahman et al., 2021).
C
A
The percentage of water extracted was reduced by 20 % by adding up to 1.5 % gelatin (Figure 3). Gelatin is a hydrocolloid that is characterized by the ability to trap water, which can help crab meat gel to improve its water-holding capacity
B
D
Figure 1. Effect of MTgase and gelatin on the TPA parameter values of crab meat gels.
B
Figure 2. Effect of MTgase and gelatin on Young modulus (A) and maximum stress (B) of crab meat gels.
and thus, decrease the amount of water it can lose. However, previous studies (Martinez et al., 2014) with blue crab meat gels, the addition of transglutaminase (6 g/kg), incubated at 40 °C and cooked at 90 °C, showed lower percentages of wa- ter extracted than gels without enzyme. In this study, adding MTgase did not affect the amount of extracted water alone or combined with gelatin, even though gelatin also acts as a substrate for the enzyme (Haug et al., 2004). Studies on add- ing MTgase and gelatin to surimi gels reported a decrease in water loss (Hernández-Briones et al., 2009; Kaewudom et al., 2013).
The effect of gelatin addition on color attributes of crab meat gels is shown in Table 4. No significant differences (p ≤ 0.05) were observed in these parameters as a function of the level of gelatin or MTgase, indicating that, regardless of the con-
Figure 3. Effect of MTgase and gelatin on the amount of expressible water of crab meat gels.
A
centration of gelatin or the enzyme, the gels had similar color attributes. Gelatin is a translucent food additive (Siccha and Lock, 1992) and therefore, adding this protein does not affect the color of gels.
Microstructure SEM images of crab meat proteins containing different levels of gelatin or MTgase are shown in Figure 4. Control gels (without MTgase) containing 1 % of gelatin (Figure 1C) were more fibrous, less compact and denser than gels containing 0.5 % or 0.3 % of gelatin (Figure 1A and 1E). These images agree with the results obtained for hardness, cohesiveness, and chewiness, all of which were negatively affected by adding 1 % MTgase but increased slightly by add- ing 3 % gelatin and had a lower amount of extracted water (higher water holding capacity).
Gels containing MTgase and gelatin seemed denser than control gels, suggesting a better interaction among adjacent proteins by the enzyme effect. Gels containing only 0.5 % gelatin and 0.5 % MTgase seemed more fibrous (Figure 1b) than gels containing 1 % gelatin, which showed lower TPA attributes (except springiness) (Figure 1). Gels containing 3 % gelatin and 0.5 % MTgase were denser and more fibrous than gels with 1 % gelatin, and showed better TPA parameters (Figure 1).
It is important to consider that gelatin is a recognized substrate for MTgase (Haug et al., 2004), and it has been reported to negatively affect the mechanical properties of surimi gels (Hernández-Briones et al., 2009; Kaewudom et al., 2013), especially at levels equal or higher than 1.5 %. However, in this study, adding gelatin improved the texture fundamental properties (Young modulus and maximum stress). Additionally, TPA parameters (except springiness) were improved by adding 3 % of gelatin, even after the neg- ative effect caused by adding 1 % (Figure 1).
Figure 4. Effect of MTgase and gelatin on SEM micrographs of crabmeat gels.
Table 5. Color parameters of crabmeat gels with MTgase and hydrocolloids.
MTgase | Gelatin L* C* H* | |||
(%) | (%) | |||
Control | ||||
0 | 0 | 73.73 ± 1.18a | 8.40 ± 0.88a | 105.27 ± 1.43a |
0.5 | 0 | 71.16 ± 0.98a | 8.18 ± 0.62a | 103.77 ± 2.12a |
Gelatin | ||||
0.5 | 73.21 ± 0.66a | 8.57 ± 0.50a | 105.01 ± 1.66a | |
0 | 1 | 72.57 ± 0.78a | 8.83 ± 0.48a | 104.47 ± 1.64a |
3 | 74.00 ± 1.81a | 10.213 ± 1.09a | 101.39 ± 1.12a | |
0.5 | 72.00 ± 0.72a | 8.76 ± 0.68a | 104.36 ± 1.95a | |
0.5 | 1 | 72.362 ± 1.17a | 7.51 ± 2.80a | 102.77 ± 2.32a |
3 | 70.862 ± 2.02a | 8.28 ± 0.50a | 102.6 ± 1.17a | |
a,b Different letters indicate statistical difference (P < 0.05) among treatments (MTgase level for control or % gelatin for each level of MTgase).
Volume XXVI
Thermally denatured muscle proteins form an opaque and not reversible gel. Gelatin proteins are different as they interact during cooling to form a reversible translucid gel af- ter being thermally denatured. Both of them are recognized as a substrate for MTgase. Meat crab proteins have been reported as a unique and different kind of proteins, which, after being denatured and aggregated by thermal process- ing, keep the ability of gelling again (Martínez-Robledo et al., 2014), suggesting a partially reversible gel. SEM images indicate that gelatin, a protein that forms reversible gels, was able to interact with muscle crab proteins, and both were an appropriate substrate for MTgase, forming a structural network where crab meat proteins-gelatin interactions took place.
Cooked crab meat proteins formed a tridimensional ordered structure with good mechanical attributes after applying a thermal denaturation-aggregation process. Adding MTgase and gelatin improved the fundamental mechanical prop- erties. However, TPA parameters were negatively affected by the addition of 1 % gelatin, although they were slightly improved by adding 3 % gelatin. Results indicate that both proteins interacted, forming the network that stabilized the gels.
No potential conflict of interest was reported by the author(s).
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