THE OBTAINING AND CHARACTERIZATION OF THE MECHANICALLY DEBONED CHICKEN MEAT MYOFIBRILLAR PROTEIN CONCENTRATES

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1 THE OBTAINING AND CHARACTERIZATION OF THE MECHANICALLY DEBONED CHICKEN MEAT MYOFIBRILLAR PROTEIN CONCENTRATES Aurelia IONESCU*, Iuliana APRODU*, Margareta Lăcrămioara ZARA*, Aida VASILE*, Gabriela GURĂU** * Galati Dunarea de Jos University, 111, Domneasca St., Galati, Aurelia.Ionescu@ugal.ro ** Emergency Hospital of Children Sf. Ioan of Galati Abstract The possibility to obtain myofibrillar proteins concentrate from the mechanically chicken meat by extraction with alkaline solutions and water washing and /or cooled soda chloride solution was studied. Also, the fish surimi paste hot gel properties in association with different ingredients were studied; these ingredients were currently used form the products fabrication on the basis of fish surimi. The starch, xanthan and protein concentrate from soy (beans) increased the viscosity of the soil on the basis of chicken meat surimi and improved the hot induced gels characteristics. Key words: chicken surimi, myofibrillar protein concentrate, rheological behavior, water holding capacity, setting, hot treatment water losses, rate and shear stress, apparent viscosity. Résumé La possibilité d obtenir le concentré de protéines myofibrillar de la viande des volailles sans os (mécanique) par l extraction avec des solutions alcalines et de se laver avec l eau et/ou la solution du chlorure du sodium refroidie, a été analysée. Aussi les propriétés de gélification thérmique de la pâte du surimi du poisson dans l association avec des différents ingrédients usés couramment à la fabrication des produits fondés sur la surimi pâte, ont été étudiées. L amidon, le xanthan et le concentré de protéines du soja (soya) augmentent les sols visqueux basés sur la surimi pâte des volailles et améliorent les caractéristiques des gels thérmiques induits. Rezumat S-a analizat posibilitatea de obţinere a concentratului de proteine miofibrilare din carnea de pasăre dezosată mecanic prin extracţie cu soluţii alcaline şi spălare cu apă şi/sau soluţie de clorură de sodiu răcite. De asemenea, au fost studiate proprietăţile de gelificare termică ale pastei de surimi de peşte în asociaţie cu diferite ingrediente, folosite în mod curent la fabricarea produselor pe bază de surimi de peşte. Amidonul, xanthanul şi concentratul proteic din soia măresc vâscozitatea solurilor pe bază de surimi de pasăre şi ameliorează caracteristicile gelurilor induse termic. 1. Introduction The increase of the food products of Bologna, Frankfurter type and other salamis based on chicken meat requires problems in connection with the capitalization of the mechanized or heavily hand deboned anatomical sections such as: necks, wings, turkey hen and chicken backs. In the countries were the chicken meat and the products based on the chicken meat as a main source of proteins of animal origin there are different occupations of their complex and complete capitalization. Thus, in Canada and America, the advanced technologies and performance installation in order to recovery the chicken meat from bones. The quality of the mechanically separated chicken meat is conditioned of the bird species, chick or turkey hen and the crushing grinding or spraying conditions and the conditions of their separation from the soft textures, too. 44

2 Concerning, the utilization of the mechanically separated chicken meat, the two risks of the security and public health are identified in the reference literature the high flour and calcium contents and the level of high lipids, which are proceeded from the backbone and back marrow, too. A high calcium level is injurious to the consumers who have a great capacity of calcium absorption, but a high flour level can lead to the flouroza which consists of the appearance of permanent brown, yellow or white spots on the teeth. Taking into account them, FSIS (Food Safety and Inspection Service) interdicts the utilization of the mechanically separated chicken meat paste in order to fabricate the products destined to the teen-ager, children under 2 years and suckling nourishment. From the beginning, the technology used to obtain the product of fish surimi with adequate functional properties the transposition of this technology was tried. This was done in order to remove undesirable components (fats, blood, water soluble substances or salt solutions) from the mechanically separated chicken meat, which reduces the period of keeping and the quantity of the paste admitted to be incorporated in different meat food. The gelatin properties have to be improved by washing; they have to be hot induced; they belong to the bird myofibrillar protein, important in order to establish the texture appearances of the products based on reshaped and minced meat; the cholesterol, calcium, flour levels substantially diminish. Research objectives To establish the obtaining technology of the myofibrillar proteins concentrates from the mechanically deboned chicken meat; The chemical physics characterization of CPDM and bird myofibrillar proteins concentrate; To study the functional properties of the respective protein concentrate. 2. Materials and methods The mechanically deboned chicken meat produced in USA was secured by the different factories of the meat preparations which use this product as an addition in different types of chicken sausages or in connection with the pork or beef meat. The chicken paste was frozen and kept in frozen state until the analysis performance. The defrosting was performed at +4 C over the night; each package has to be protected by an aluminium sheet to avoid the sunlight. In order to solve the experimental part the following analysis were performed: - chamber drying humidity at C until the constant mass in accordance with the method STAS 9065/3-1975; - total nitrogen. The determination of the total nitrogen content was performed by the Kjeldahl method (STAS 9065/4-1981). The global proteins were calculated by the multiplication the total nitrogen by the factor 6.25; - the grease content was determined by the SOXHLET method by the organic solvents extraction (STAS 9065/2-1973); - the ammonium was determined by the method indicated by STASS 9065/3-1974; - the free amino-acids were determined by the titrimetric phormol in accordance with the technology described by Ionescu (2000); - the nitrogen volatile bases were determined by the method described by Ionescu (1995); - the TBA index was determined by the method described Ionescu (1995); - the ph was potentiometer determined by the potentiometer of the type Wissenchaftlich Techniche Werstätten GmbH/WTW equipped with the thermometer and tube electrode 2.1. Rheological measurements The study of the pastes rheological properties based on chicken surimi was performed by using a rotary viscosimeter RHEOTEST 2 type, made in Germany (VEB-MEDINGE company). The pastes rheological behavior has been examined using a device that has a S 3 coaxial cylinder, which is indicated to be used for medium viscosity. 45

3 The quantity of the material included into the cylinder was 50 g and the work frequency was 50 Hz. The shear rate (γ) varied in the domain of s -1. The shear stress (τ r ) was calculated based on α values read on the apparatus gradual dial for the different values of shear rate, by the relation: τ r = z α (N/m 2 ) (1) where z is the apparatus constant for the second domain and cylinder, S 3, dyn./cm 2 times with the division x scale). The apparent viscosity was calculated with the relation: τ s η = 100 (Pa s.) (2) γ 3. Results and discussions The sensory characteristics and chemical composition of the mechanically deboned chicken meat are shown in the table 1. CPDM after defrosting was presented as a soft meat paste with a superficial layers grey and depth red homogenous thin structure. The presence of the bones, tendons and cartilages were not observed when it is touched. The chicken meat has presented an acid weak ph and a specific light odor of chicken fats. From the chemical viewpoint we remark the proteins and lipids high relatively contents, but the ash content is to be under 1%. Due to the high fats levels, in order to obtain the chicken myofibrillar protein substance we used the alkaline medium extraction technology together with the natrium bicarbonate solution of 0.50%, ph = 8.5; it is showed by the figure 1. The filtering of the alkaline solution and chicken meat homogenization was performed in order to remove the proteins of the conjunctive tissue. The solid portion was washed twice by the alkaline natrium bicarbonate solution of 0.25% with the adapted ph at the level 7.5 with the lactic acid solution of 60% (v/v) in order to recover the myofibrillar proteins driven by the residue. The filter has been centrifugal, then the solid residue was washed three times by means of the NaCl 0.2% solution in order to remove completely as possible as, the fats, the heminic pigments and the components of the cooled soda chloride solution soluble mechanically deboned chicken meat. Due to the strong hydratation of the chicken meat myofibrillar proteins, the cooled water is not to be indicated in order to wash the protein residue. Table.1. Chemical composition of the mechanically deboned chicken meat and chicken surimi and sensorial and physics characteristics Indicator CPDM Surimi from mechanically deboned chicken meat Humidity, Total nitrogen, Proteins, Grease, Ash, Non protein nitrogen, Aminic nitrogen, The nitrogen of the volatile nitrogen bases, TBA, mg malonaldehyde/kg ph Color Inside red, green, grey outside white Consistence Soft soft Odor Chicken grease odor Neutral 46

4 Mechanically deboned chicken meat Homogenization, 5 min., ratio 1/3 NaHCO 3, 0.5%, ph = 8.5, 2 0 C Repose at +4 0 C, 10 minutes Filtering through the nylon sieve Solid residue Filtered Washing (2 repeated washings) ratio 1/3 NaHCO 3, 0.25%, ph = 7.5, 2 0 C Supernatant I Centrifugal, 3600 rpm., 15 minutes, 0 0 C Filtering Filtered Solid residue Residue I Repeated washings (2), ratio 1/3, homogenization 5 minutes NaCl, 0.2%, 2 0 C Supernatant II (III) Centrifugal, 3600 rpm., 15 minutes, 0 0 C Residue II (III) Washing, ratio 1/5, homogenization 5 minutes NaCl, 0.2%, 2 0 C Supernatant IV Centrifugal, 3600 rpm., 15 minutes, 0 0 C Residue IV Supernatant Centrifugal, 3600 rpm., 15 minutes, 0 0 C Myofibrillar protein concentrates (chicken surimi) Figure 1. Technological scheme of the chicken surimi mechanically deboned chicken meat myofibrillar proteins substance obtaining 47

5 The physics and chemical and sensorial characteristics of the damp and protein bird myofibrillar concentrate are registered in the table 1, too. The chicken surimi had a high water content due to the good water retain and hydratation capacity of the chicken myofibrillar proteins. The protein content is situated at the level of 11.56%; the fats content of the ash was of 0.49%. The soda from the chloride solution used for the myofibrillar protein residue washing is included in the ash composition, too. The color pigments have been removed during the repeated washings and extraction; the finished is of white color. The substances which react to the 2-tiobarbituric acid, so that the part from these components is connected by the covalent connections with the myofibrillar proteins, could not be entirely removed by the applied technology. These covalent connections with the myofibrillar proteins can be broken in acid medium and during the hot treatment, too; these covalent connections with the myofibrillar proteins finally can react to the 2-tiobarbituric in order to form a colored compound, too. It devolves that it is necessary to use a very fresh CPDM only in order to obtain the chicken myofibrillar protein concentrate. The recovering efficiency of the myofibrillar proteins was of 65.8% Rheological behaviour of the bird myofibrillar proteins concentrates The rheological study of the bird myofibrillar proteins concentrate consisted of its apparent viscosity and shear stress determination at the different shear rates (the s -1 domain). Within our experiment the surimi soil was thermostat for 10 minutes at the temperature of 20 C, after that the Rheotest 2 measurements were performed at the controlled temperature. The typical rheograms of the cruel meat batters bird surimi batters presented in figures 2 and 3 show this has a behavior similar to a pseudoplastic body. Characteristically to the pseudoplastic nonnewtonian behavior dependent on the dispersed proteins structure, the fluidity phenomenon is present. 35 Proteic dispersion on basis of the chicken Rank 3 Eqn 8010 [Power] y=a+bx c r 2 = DF Adj r 2 = FitStdErr= Fstat= a= b= c= Shear stress, N/m Figure 2. Shear stress rheogram shear rate 48

6 Proteic dispersion on basis of the chicken Rank 1 Eqn 8010 [Power] y=a+bx c 8 r 2 = DF Adj r 2 = FitStdErr= Fstat= a= b= c= Apparent viscosity, Pa.s Figure 3. Apparent viscosity rheogram shear rate The apparent viscosity continuously has diminished, but the shear stress developed on the whole domain of the shear rates. The flowing curves indicate a maximum viscosity at the smallest shear rate and a strict viscosity falling in first ten days of the shear rate. At the same time, it observed that the surimi batters present behavior to the Newtonian a flowing in the extreme domains of the required parameters. The system s linear behavior mainly consisting myosin, actin and actomyosin to which it is observed that the friction diminishes due to the modifications of the protein structure which from the surimi batters. These changes could consist of breaking of some bound between the polypeptidic chains or of the alignment of proteic molecules, together with the increasing of the shear rate. They could also consist of in the interactions between the flowing elements and the dispersion medium (water in which the sodium tripolyphosphate and the salt are soluble). The surimi batters proved to be a thixotropic system, because at the share flowing at manifested reversible time dependence and a viscosity isotherm decreasing. The time dependence was connected to the rates by whose means the myofibrillar bird meat protein has suffered destruction or remaking events. The presence of the hysteresis loop (figures 4 and 5) shows that the destruction rate was more that the restructure rate. Apparent viscosity, Pa.s ascendancy descendancy Figure 4. The variation of the shear stress depending on the shear rate The apparent viscosities and the shear stress had smaller shear values on the upward branch of the shear rate in relation to the values of downward branch for the same level of the shear rate The influence of some ingredients on the rheological behavior of the chicken myofibrillar protein concentrates Within this work we studied the role of some active hydrodynamic biopolymers (xanthan and starch) and of other ingredients on the 49

7 rheological properties of the semisolid paste chicken surimi. Thus, the series of the protein dispersion were performed; they are registered in the table 2; their shear flowing behavior was studied, too. They contribute to the myofibrillar protein solubility and the improvement of the surimi meat batters functional properties, too. 450 The relations between the shear stress, apparent viscosity and shear rate are shown in the figure 6 and figure 7 The performed proteic dispersions have presented the different pseudoplasticity depending on their components. The smallest viscosity was established at the system based on tripolyphosphate and salt addition surimi, the substances currently added to the surimi meat batters. Shear stress, N/m ascendancy descendancy Figure 5. The variation of the apparent viscosity depending on the shear rate Table 2. The components of the chicken myofibrillar proteins dispersions based on chicken surimi The sample nature Surimi, g Salt, Tripolyphosphate, Xanthan, Starch, Dampro, 1. Witness Xanthan sample Maize starch sample The sample of Damprosoy (beans) proteic concentrate addition Shear tension, N/m Apparent viscosity, Pa.s Chicken surimi Chicken surimi+nacl+xanthan+tpp Chicken surimi+nacl+xanthan+tpp+dampro Chicken surimi+nacl+xanthan+tpp+starch corn Shear rate, s Chicken surimi Chicken surimi + NaCl + xanthan + TPP Chicken surimi + NaCl + xanthan + TPP + Dampro Chicken + NaCl + xanthan + TPP + Starch corn Figure 6. The influence of the different ingredients and of the shear rate on the shear stress at the dispersions on the basis of the chicken surimi Figure 7. The influence of the different ingredients and of the shear rate on the apparent viscosity in case of the dispersions on the basis of the chicken surimi 50

8 The xanthan and starch maize combination close by another s ingredients has determined the most important increasing of the system s viscosity, therefore at opposites the biggest resistance to the flowing and shear an can determinate the forming of a protein gel with the firmest texture. Xanthan maize starch and soy protein concentrate in the chicken surimi; cruel meat batters took action as a strengthen agents. During the starch addition sample some irregularities in the evolution of apparent viscosity and of the shear stress (tangent stress) were observed. Those could be explained by the proteins structure and the macromolecules arrangement in the flowing direction depending on the shear rate followed by the partial remarking at a given moment of the protein structures and by the maize starch interference which is included in the system s water proteins competition. At the big shear rates, the apparent viscosity remains actually constant; it indicates that the biopolymers molecules orientation is complete, but the viscosity after that obtained the maximum value, remains constant. The rheological measurements constitute at present the base of the texture prediction of the different food products as gels, meat batters or emulsions The study of the chicken myofibrillar proteins gel properties The myofibrillar proteins wet concentrate was studied from the viewpoint of their capacity to produce gels at the hot treatment. Therefore, we studied the influence of the protein concentration and the presence of some additions on the forming capacity of the tridimensional networks by the chicken proteins. In order to characterize the formed protein gels we used as indicators the water holding capacity, the gel viscosity and the keeping stability. The gels are colloidal dispersions obtained from two components characterized at least by the deformation and the fluidity absence. The myofibrillar proteins at the concentrations more 5% form lineal filaments and special small aggregates in the presence of the salt. By their interaction of these filaments, the tridimensional relations are formed; these retain water molecules of the formed structure myosin is a main protein responsible to gel; F- actin improves the myosin gel properties, this protein having weak gel properties. The actomyosin gel properties are connected to the myosin molecule heavy chain from the actomyosin complex composition. In order to study the chicken myofibrillar proteins gel properties, the surimi samples established with cryoprotection substances and salt addition were homogenized during three minutes, but after the equilibration of the temperature at 25 0 C were differently kept at these temperature 1 hour, respectively 2 hours. For the gels which were formed after cooling setting, the expressed water percent was established as a measure of the system s capacity in order to retain the water under centrifugal conditions and after the application of a thermal treatment, too (table 3). The myofibrillar chicken proteins form the tridimensional networks more firm at the hot treatment if the pregelation is to be performed at the temperature of 25 C. At the temperature of 45 C during the setting are possible structure modifications that affect the water holding water capacity. Table 3. The influence of the temperature on the obtained water percentage Gel temperature, The obtained water percentage C Centrifugal At the thermal treatment* * The chemical treatment has performed of the samples slow heating with a rate about 2 C/minut until the reaching inside the temperature of 90 C, maintaining this level at the temperature during ten minutes. 51

9 All the gels performed on the basis of the chicken surimi meat without setting with protein concentration between % and values of ph more 7.0 have presented a good holding water capacity after the application of a hot medium treatment until 70 C, maintaining this temperature in the hot center during 10 minutes. The gels after the cooling and over night keeping at 4 C did not present the syneresis event. The starch maize addition gels have presented a cohesive structure and elasticity in comparison with those without starch addition. The acts are a simple reinforcement agent of the myofibrillar proteins gel; it does not interact with the protein matrix; it does not affect its forming too, because the after filling produces after the myofibrillar protein gels. The global soy (beans) proteins tend to reduce the gel cohesive structure on basis of chicken surimi meat. The gel elasticity and reinforcement until 70 C were mainly reduced in comparison with those of the gels thermally induced until 90 C. 4. Conclusions The applied technology in order to obtain the myofibrillar protein concentrate from the mechanically deboned chicken meat led to proteins recovering efficiency of 65.8% and the good separation of the undesired substances (lipids, sarcoplasmatic protein non nitrogen and nitrogen extractable substances); Chicken surimi meat has distinct functional properties it remarks especially by a good water holding capacity and good features in order to form the gels during the thermal treatment; Hydrocolloids of xanthan and starch type improved the texture proprieties of the myofibrillar proteins concentrate when the protein gels are formed; The reinforcement of the gels on the basis of the chicken surimi is depend on the temperature and the gel period and the temperature, too, used form the hot inducing of the protein gel. 5. Bibliography Anne, B. Smyth et al. (1997). Heat-induced gelation properties of surimi from mechanically separated chicken. J. Food Science, 62, 2, 326. AOAC, (1990). Official Methods of Analysis, 15 th ed. Association of Official Analytical Chemists, Washington, D C. Burge, L., D. JR, et al. (1984). Rheological properties of comminuted meat batters and the relationship to constituent interactions. J. Food Technology, 19, 719. Chong, M, Lee et al. (1992). Ingredient and formulation for surimi-based product. In: Surimi technology, Lanier Trye şi Chong M. Lee, edited de Marcel Dekker, New York, 273. Hongsprabhas, P. et al. (1999). Use of cold-set whey protein gelation to improve poultry meat batters. Poultry Science 78, Ionescu, A., Resmeriţă, D. et al. (2001). The influence of some ions, temperature and shear rate upon rheological properties of the xanhtan and carrageenan soluţions. In: The Annals of University Dunărea de Jos of Galaţi, fascicle VI, ISSN , Food Technology, 7. Lanier, T.C., (1986). Functional properties of surimi. Food Technology, 40,3, 107. Lee,C.M. et al. (1992). Ingredient and formulation technology for surimi-based food products. In: Surimi Technology, T. C. Lainer and C. M. Lee (Ed.). Marcel Dekker, Inc., New York. Lee, G.H. et al. (1997). Covalent Cross-linking effects on Thermo-Rheological Profiles of fish protein gels. J. Food Science, 62,1, 25. McDonald et al. (1991). Carbohydrates as cryoprotectants for meats and surimi. Food Technology, 45, 3, 150. Park, J.W. (1994). Functional protein additives in surimi gels. J. Food Science, 59, 525. Toledo, R. et al. (1997). Relationship between composition, stability and rheological properties of comminuted raw meat batters. J. Food Science, 42,725. Won, B. Yoon et al. (1997). Surimi-Starch Interactions based on mixture design and regressions models. J. Food Science, 62, 3,