Acessibilidade / Reportar erro

Aging time of five muscles from carcass of Nellore young bulls

Maturação de cinco músculos da carcaça de novilhos da raça Nelore

ABSTRACT.

This trial aimed to assess the qualitative traits of five muscles of 14 Nellore bulls with 450 kg ± 30.7 kg BW, feedlot fed for 60 days. After slaughter and carcass chilling, samples of the Biceps femoris (BF), Longissimus (LD), Gluteus medius (GM), Semitendinosus (ST) and Trapezius thoracis (TT) muscles were collected, vacuum-packed and aged at 0 to 2 ºC for 1, 7 and 14 days and subsequently stored at -20ºC for chemical and quality analysis. The pH, shear force, water holding capacity, cooking losses, meat color and ether extract were evaluated in all aging times. Data were analyzed in a split-plot design using the PROC MIXED procedure of SAS. Aging affected quality traits and chemical properties of the meat, improving aspects, such as tenderness (p < 0.01) and lightness (p < 0.01). The Trapezius thoracis muscle has a higher color stability compared with the Longissimus muscle. Aging is not recommended for the ST muscle because the tenderness is not improved. The GM and BF muscles are tender on the first day, and the aging process is indicated for these cuts for adding value to the beef.

Keywords:
beef cattle; biceps femoris; longissimus; meat color; Nellore; tenderness.

RESUMO.

Foram estudadas as características qualitativas de cinco músculos, maturados ou não, de quatorze bovinos da raça Nelore com 450 kg ± 30,7 kg de peso corporal e confinados por 60 dias com dieta contendo 60% de concentrado e 40% de volumoso na MS. Após o abate e resfriamento das carcaças, amostras dos músculos: picanha, (Biceps femoris - BF), contrafilé (Longissimus - LD), alcatra (Gluteus medius - GM), lagarto (Semitendinosus - ST) e acém (Trapezius thoracis - TT) foram retirados, embalados à vácuo e maturados em câmara B.O.D (0 a 2oC) por um, sete e 14 dias e posteriormente armazenadas a -20oC para análises químicas e de qualidade. Os dados foram analisados em um delineamento em split-plot utilizando o procedimento PROC MIXED do SAS. A maturação influencia nas características qualitativas e químicas da carne bovina, melhorando aspectos como a maciez (p < 0,01) e a luminosidade (p < 0,01). O músculo Trapezius thoracis tem uma maior estabilidade de cor quando comparado com o músculo Longissimus. Não é recomendada a maturação do músculo ST em razão deste não apresentar melhora em sua maciez. Os músculos GM e BF apresentam-se macios logo no primeiro dia, sendo que o processo de maturação para estes cortes é indicado em razão de agregar valor à carne.

Palavras-chave:
bovinos; cor da carne; cortes cárneos; maciez; Nelore; pH

Introduction

Tenderness has been considered a major contributor to eating experience in beef (Guerrero, Valero, Campo & Sañudo, 2013Guerrero, A., Valero, M. V., Campo, M. M., & Sañudo, C. (2013). Some factors that affect ruminant meat quality: from the farm to the fork. Review. Acta Scientiarum. Animal Sciences35(4), 335-347.;Miller, Carr, Ramsey, Crockett & Hoover, 2001Miller, M. F., Carr, M. A., Ramsey, C. B., Crockett, K. L., & Hoover, L. C. (2001). Consumer thresholds for establishing the value of beef tenderness. Journal of Animal Science, 79(12), 3062-3068.). Aging meat in vacuum packaging at refrigerated temperatures provides purveyors with a way to increase tenderness (Guelker et al., 2013Guelker, M., Haneklaus, A., Brooks, J., Carr, C., Delmore, R., Griffin, D., ... & Johnson, D. (2013). National Beef Tenderness Survey-2010: Warner-Bratzler shear force values and sensory panel ratings for beef steaks from United States retail and food service establishments. Journal of Animal Science, 91(2), 1005-1014.;Voges et al., 2007Voges, K., Mason, C., Brooks, J., Delmore, R., Griffin, D., Hale, D., ... Maddock, R. (2007). National beef tenderness survey-2006: Assessment of Warner-Bratzler shear and sensory panel ratings for beef from US retail and foodservice establishments. Meat Science, 77(3), 357-364.).

The predominant type of fiber in the musculature of animals has a direct influence on the qualitative traits of the meat, affecting the texture, shear force, color, juiciness, pH, and yield (Aberle, Forrest, Gerrand, Mills & Hedrick, 2001Aberle, E. D., Forrest, J. C., Gerrand, D. E., Mills, E. W., & Hedrick, H. B. (2001). Principles of Meat Science (4 ed.).;Maggioni et al., 2012Maggioni, D., Prado, I. N., Zawadzki, F., Valero, M. V., Marques, J. A., Bridi, A. M., ... Abrahão, J. J. S. (2012). Grupos genéticos e graus de acabamento sobre qualidade da carne de bovinos. Semina: Ciências Agrárias, 33(1), 391-402.), because these are related to factors such as the muscle contraction state, degradation of the myofibril, intramuscular fat and diameter of muscle fibers. This affects the meat tenderness directly and indirectly.

Some muscles have a greater physical activity than others, and, as a consequence, they have a large proportion of red fibers among the white fibers (Kirchofer, Calkins & Gwartne, 2002Kirchofer, K. S., Calkins, C. R., & Gwartney, B. L. (2002). Fiber-type composition of muscles of the beef chuck and round. Journal of Animal Science, 80(11), 2872-2878.). Myoglobin stores and transports oxygen in the muscles, such that the concentration of myoglobin increases as the oxygen requirement of the muscle is increased, and the levels of these pigments are higher in the most active muscles (Mancini & Hunt, 2005Mancini, R. A., & Hunt, M. C. (2005). Current research in meat color. Meat Science, 71(1), 100-121.).

Muscles of the forequarter, which perform long periods of physical activity and have a short rest period, have high levels of red fibers (Kirchofer et al., 2002Kirchofer, K. S., Calkins, C. R., & Gwartney, B. L. (2002). Fiber-type composition of muscles of the beef chuck and round. Journal of Animal Science, 80(11), 2872-2878.), as they require much oxygen for their metabolism. The oxidative metabolism requires a well-developed circulatory system and a high concentration of mitochondria and myoglobin. In contrast, muscles that perform fast movements or twitches require a longer rest period. These tissues are rich in white fibers, which, depending in an anaerobic metabolism to obtain energy and need more muscle glycogen in relation to myoglobin. Given the lower concentration of myoglobin, these muscles are less red and thus named 'white' tissues (Cezar & Sousa, 2007Cezar, M., & Sousa, W. (2007). Carcaças ovinas e caprinas: obtenção, avaliação e classificação. Uberaba, MG: Editora Agropecuária Tropical.). Consequently, there are differences when compared meat color of muscles from the fore- and hindquarter regions of the animals.

Muscles rich in slow-twitch, red(oxidative) muscle fibers are characterized by the presence of myoglobin and lipids, and low glycogen content (Hunt & Hedrick, 1977Hunt, M. C., & Hedrick, H. B. (1977). Profile of fiber types and related properties of five bovine muscles. Journal of Food Science, 42(2), 513-517.). As a consequence, metabolism is mostly oxidative and with low lactic acid production, which results in a higher final pH. Muscles consisting mostly of fast-twitch, white muscle fibers (glycolytic) have a high glycogen content and a typically glycolytic metabolism, with a very active degradation of glycogen to lactic acid, promoting lower final pH values (Savell, Muelle, & Baird, 2005Savell, J. W., Mueller, S. L., & Baird, B. E. (2005). The chilling of carcasses. Meat Science 70(3), 449-459.).

Fast-twitch muscles (white fibers) have a greater ATPase activity and this should yield tender meat due to the lower activity of calpastatin (Geesink, Kuchay, Chishti & Koohmaraie, 2006Geesink, G. H., Kuchay, S., Chishti, A. H., & Koohmaraie, M. (2006). μ-Calpain is essential for postmortem proteolysis of muscle proteins. Journal of Animal Science84(10), 2834-2840.), because of the negative correlation between the calpastatin activity and the myofibrillar ATPase activity (Geesink, Taylor, Bekhit & Bickerstaffe, 2001Geesink, G. H., Taylor, R. G., Bekhit, A. E. D., & Bickerstaffe, R. (2001). Evidence against the non-enzymatic calcium theory of tenderization. Meat Science59(4), 417-422.). Therefore, a greater proportion of oxidative fibers reflect in lower activity of calpains, due to a larger amount of calpastatin, resulting in lower muscle degradation and originating a less tender meat (Koohmaraie, 1996Koohmaraie, M. (1996). Biochemical factors regulating the toughening and tenderization processes of meat. Meat Science, 43, 193-201.).

Nevertheless, in order to increase the overall value of the carcass, it is necessary to study these muscles, which will demystify some aspects and provide an increased consistency of products, promoting a more effective commercialization as well as guidance in the use of processing technologies, as in the case of aging (Macedo et al., 2008Macedo, L. M., Prado, I. M., Prado, J. M., Rotta, P. P., Prado, R. M., Souza, N. E., & Prado, I. N. (2008). Chemical composition and fatty acids profile of five carcass cuts of crossbred heifers finished in feedlot. Semina: Ciências Agrárias29(3), 597-608.;Tschirhart-Hoelscher, Taylor, Bekhit & Bickerstaffe, 2006Tschirhart-Hoelscher, T. E., Baird, B. E., King, D. A., McKenna, D. R. & Savell, J. W. (2006). Physical, chemical, and histological characteristics of 18 lamb muscles. Meat Science, 73(1), 48-54.). Aging allows for a significant improvement in tenderness, and this procedure can be advantageous from the qualitative point of view, especially when it comes to animals with a greater Bos indicus genetic composition (Maggioni et al., 2012Maggioni, D., Prado, I. N., Zawadzki, F., Valero, M. V., Marques, J. A., Bridi, A. M., ... Abrahão, J. J. S. (2012). Grupos genéticos e graus de acabamento sobre qualidade da carne de bovinos. Semina: Ciências Agrárias, 33(1), 391-402.;Wheeler, Cundiff & Koch, 1994Wheeler, T. L., Cundiff, L. V., & Koch, R. M. (1994). Effect of marbling degree on beef palatability in Bos taurus and Bos indicus cattle. Journal of Animal Science, 72(12), 3145-3151.).

It is there for interesting to improve and differentiate meat cuts, mainly in relation to its qualitative aspects, as several market studies have shown that consumers have paid a higher value in meat products which have according to their preferences. Thus, this study aimed to evaluate the effects of different aging times on the quality traits of five muscles of Nellore young bulls.

Material and methods

The trial was carried out at the São Paulo State University (UNESP, Jaboticabal, São Paulo State, Brazil), following the humane animal care and handling procedures, according to the guidelines of the São Paulo State University (UNESP, Brazil). Fourteen Nellore young bulls with average initial body weight of 450 ± 30.7 kg and age of 15 months were used. Initially, cattle were weighed, identified and housed in individual pens with trough and drinkers. Cattle were subjected to seven days of adaptation to experimental installations and diets. After this period, the animals were fed for 60 days. Diets were formulated according toValadares Filho (2006Valadares Filho, S. C. (2006). Tabelas brasileiras de composição de alimentos para bovinos (Vol. 1). Viçosa, MG: UFV.) and offered in the concentrate level of 40:60. Corn silage was used as the exclusive roughage and concentrate was composed of ground corn, soybean meal, urea/ammonium sulfate and mineral mixture (Table 1).

Table 1
Diet composition.

After 60 days of feeding, animals were slaughtered at a commercial abattoir with 598 ± 41.7 kg of shrunk body weight. Pre-harvest handling was in accordance with good animal welfare practices, and slaughtering procedures followed the Sanitary and Industrial Inspection Regulation for Animal Origin Products.

After the slaughter, carcasses were weighed and then refrigerated at 0°C for approximately 24h. After the postmortem chill period, samples of the following muscles were removed from the left carcasses: Biceps femoris (BF), Gluteus medius (GM), Longissimus (LD), Semitendinosus (ST) and Trapezius thoracis (TT). Three samples were taken from each muscle to evaluate the variable of meat quality in its respective time.

The samples were aged for 7 or 14 days between 0 and 2oC and subsequently stored at -20oC for analysis. The pH, shear force, water holding capacity, cooking losses, meat color and ether extract were evaluated in all aging times.

Warner-Bratzler shear force (WBSF) steaks were thawed at 4°C for 24h and oven-broiled in an electric oven (Ltedesco) preheated at 175°C. Internal steak temperatures were monitored by 20-gauge copper-constantan thermocouples placed in the approximate geometric center of each steak and attached to a digital monitor. When internal steak temperature reached 35°C, the steak was turned over and allowed to reach an internal temperature of 71°C before removal from the oven. Cooked WBSF steaks were cooled for 24h at 4°C (AMSA, 1995AMSA. (1995). Research guidelines for cookery, sensory evaluation and instrumental tenderness measurements of fresh meat. In AMSA. (Ed.), American Meat Science Association (p. 48). Savoy, IL: National Livestock and Meat Board.). Eight round cores (1.27 cm diameter) were taken from each steak parallel to the long axis of the muscle fibers (AMSA, 1995AMSA. (1995). Research guidelines for cookery, sensory evaluation and instrumental tenderness measurements of fresh meat. In AMSA. (Ed.), American Meat Science Association (p. 48). Savoy, IL: National Livestock and Meat Board.). Each core was sheared once through the center, perpendicular to the fiber direction by a Warner-Bratzler shear machine (Brookfield Texture Analyser). Cook loss (CL) was evaluated on the steaks that were also used for WBSF measurement. Total CL was calculated as the difference between the weight of the steaks before and after oven-broiling.

The determination of meat and fat color was performed as described byHouben, Van Dijk, Eikelenboom and Hoving-Bolink (2000Houben, J. H., Van Dijk, A., Eikelenboom, G., & Hoving-Bolink, A. H. (2000). Effect of dietary vitamin E supplementation, fat level and packaging on colour stability and lipid oxidation in minced beef. Meat Science, 55(3), 331-336.), using a Hunterlab colorimeter to evaluate the lightness (L*), redness (a*), and yellowness (b*). Color aspects were assessed by the CIE L*a*b*color system using 0°/45°. Thirty minutes before the assessment, cross sections were made at the samples surface to expose themyoglobin to oxygen, as described byAbularach, Rocha, and Felíc (1998Abularach, M. L. S., Rocha, C. E., & Felício, P. E. (1998). Características de qualidade do contrafilé (M. L. dorsi) de touros jovens da raça Nelore. Ciência e Tecnologia de Alimentos18(2), 205-210.), the same steps were made for the fat color measurement. After this, the color was measured at three different points and average values calculated. The colorimeter was calibrated before analyzing the samples against white and black standards.

After evaluating each steak's color, approximately 2 g was collected to determine the water holding capacity (WHC). This value is the difference between the weights of the sample before and after being subjected to a pressure of 10 kg for 5 min. (Hamm, 1986).

The ultimate pH was measured on the aged muscles of each animal using a pH-meter with automatic endpoint and buffer cognition as well as temperature compensation equipped with a penetrating electrode (Model SG2 - ELK, Seven Go(tm), Mettler Toledo International Inc.). The pH-meter was calibrated before use to pH 7.0 and 4.01. The pH was measured at approximately 4 cm deep on the muscles.

For proximate analysis, the epimysium was removed from the samples before lyophilization for 48h. Samples were then ground and analyzed for ether extract (EE; Method 920.85) (AOAC, 2005AOAC-Association Official Analytical Chemist. (2005) Official Methods of Analysis (18th ed.). Gaitherburg, Maryland, USA: AOAC.) in order to determine the chemical composition of each aged samples.

Data were analyzed in a split-plot design using PROC MIXED procedure ofSAS (2004)SAS. (2004). SAS/STAT User guide, Version 9.1.2. Cary, NC, USA: SAS Institute Inc.. The model tested the fixed effects of muscle, aging time and their interaction. Muscle (animal) was included in the model as a random effect. When no significant, interaction was removed from the model. The means squares were generated for the main effects and significant interactions were separated (p < 0.05) using the Tukey's test.

Results and discussion

No interactions were detected between aging times and muscles (Table 2) for pH, L* and EE; thus, the results were discussed separately. The pH of TT muscle was higher (p = 0.04) than in other muscles. In the present study, the aging reduced the pH values in relation to the beef evaluated at the time 1, where in the pH dropped on day 7 (5.2) and increased again on day 14 (5.7), but with a lower value in relation to day 1 (5.7).

The control of pH is important, as it is related to color, tenderness and WHC of the meat (Valero et al., 2014Valero, M. V., Torrecilhas, J. A., Zawadzki, F., Bonafé, E. G., Madrona, G. S., Prado, R. M., ... Prado, I. N. (2014). Propolis or cashew and castor oils effects on composition of Longissimus muscle of crossbred bulls finished in feedlot. Chilean Journal of Agricultural and Research74(4), 445-451. doi:10.4067/S0718-58392014000400011;Zawadzki et al., 2011Zawadzki, F., Prado, I. N., Marques, J. A., Zeoula, L. M., Prado, R. M., Fugita, C. A., ... & Maggioni , D.(2011). Sodium monensin or propolis extract in the diet of Nellore bulls finished in feedlot: chemical composition and fatty acid profile of Longissimus muscle. Semina: Ciências Agrárias, 32(4), 1627-1636.). Muscle pH usually decreases from 7.0 after slaughter to approximately 5.3 to 5.8 after chilling, such that the pH drop during the chilling occurs between 6 and 12 h and is completed in 18 to 40 h after slaughter (Savell et al., 2005Savell, J. W., Mueller, S. L., & Baird, B. E. (2005). The chilling of carcasses. Meat Science 70(3), 449-459.). According toLuchiari Filho (2000Luchiari Filho, A. (2000). Pecuária da carne bovina (1 ed.). São Paulo, SP: LinBife.), a decrease in pH is due to the use of reserves of glycogen and its transformation into lactic acid by anaerobic glycolysis. Therefore, on day 1, the pH was at normal levels, which is in agreement with the meat-packing-industry standards, given that in Brazil meat packing plants export only meat with pH lower than 5.8 (Fernandes et al., 2008Fernandes, A. R. M., Sampaio, A. A. M., Henrique, W., Oliveira, E. A., Tullio, R. R., & Perecin, D. (2008). Características da carcaça e da carne de bovinos sob diferentes dietas, em confinamento. Arquivo Brasileiro de Medicina Veterinaria e Zootecnia60(1), 139-147.).

Vacuum-packaging delays the growth of aerobic putrefactive bacteria and also promotes the growth of lactic bacteria, which in turn produce antimicrobial substances (Puga, Contreras & Turnbull, 1999Puga, D. M. U., Contreras, C. J. C., & Turnbull, M. R. (1999). An evaluation of tenderization of forequarter bovine meat (Triceps brachii) through methods of ageing and injection with acetic and lactic acids. Food Science and Technology19(1), 88-96.). Hence, although microbial growth was not evaluated in the present study, it can be inferred that the lower pH observed on days 7 and 14 was due to the growth of lactic bacteria and production of acid substances, which contributed to the increased growth in the meat environment.

The difference in pH observed for the muscles (p = 0.04) in the present study can be related to the amount of glycogen. Muscles from the forequarter, e.g., TT, which perform long periods of physical activity and have a short rest period, have a greater proportion of red fibers and are characterized by the presence of myoglobin and lipids, but low glycogen levels (Hunt & Hedrick, 1977Hunt, M. C., & Hedrick, H. B. (1977). Profile of fiber types and related properties of five bovine muscles. Journal of Food Science, 42(2), 513-517.). Thus, their metabolism is preferentially oxidative and with low lactic-acid production, which explains why the TT muscle in our study showed a higher pH. Muscles that are composed mainly of white muscle fibers (LD, GM, ST and BF), however, have high glycogen content and a typically glycolytic metabolism, with a highly active degradation of glycogen to lactic acid, promoting lower pH levels (Savell et al., 2005Savell, J. W., Mueller, S. L., & Baird, B. E. (2005). The chilling of carcasses. Meat Science 70(3), 449-459.).

Higher L* values were observed at 7 and 14 days, differing from day 1, which showed a lower value

(p < 0.01). Among the muscles, ST showed greater L* than LD, GM, BF and TT (p < 0.01).

Aging increases the meat L*, resulting in brighter meats (Mancini & Hunt, 2005Mancini, R. A., & Hunt, M. C. (2005). Current research in meat color. Meat Science, 71(1), 100-121.). According toPereira, Sobral, Leme and Silva (2008Pereira, A. S. C., Sobral, P. J. A., Leme, P. R., & Silva, S. L. (2008). Physical and chemical characteristics of frozen ground beef and aged beef meat from Bos indicus steers supplemented with α-tocopherol acetate. Italian Journal of Food Science ,20(3), 419-425.), an explanation for the increase in L* with aging is the presence of a greater amount of liquid on the surfaces, and hence the greater moisture and higher values for this trait in the aged meat.

Protein degradation in the aging period is directly related to the pH, which changes the light dispersion properties and consequently affects the L* values (Kadim et al., 2013Kadim, I. T., Al-Karousi, A., Mahgoub, O., Al-Marzooqi, W., Khalaf, S. K., Al-Maqbali, R. S., ... Raiymbek, G. (2013). Chemical composition, quality and histochemical characteristics of individual dromedary camel (Camelus dromedarius) muscles. Meat Science, 93(3), 564-571.), and lower pH values will allow for greater meat L*. With higher muscle pH, proteins are able to bind more strongly to water, yielding less free water. When the proteins bind to more water, the muscle fibers are swollen, leaving less space between muscle fibers (Page, Wulf & Schwotzer, 2001Page, J. K., Wulf, D. M., & Schwotzer, T. R. (2001). A survey of beef muscle color and pH. Journal of Animal Science, 79(3), 678-687.). Therefore, meats with a higher pH will be darker in color because there is less free water to reflect light (Mancini & Hunt, 2005Mancini, R. A., & Hunt, M. C. (2005). Current research in meat color. Meat Science, 71(1), 100-121.). Therefore, due to the lower pH found with the aging time, some muscles showed lower WHC, which made it possible to increase the luminosity index with the aging time.

A higher L* value was found in the ST muscle, which can be explained by its anatomical position, with a more external location and a denser and more visible connective tissue, due to its function in the animal, with lower iron levels and consequently greater luminosity (Mancini & Hunt, 2005Mancini, R. A., & Hunt, M. C. (2005). Current research in meat color. Meat Science, 71(1), 100-121.).

The lowest EE value was observed on day 14 in relation to the other aging times (p = 0.03). The highest EE value for the muscles was obtained in BF, and muscles LD and TT did not differ from BF and GM. The ST muscle showed the lowest value, not differing from GM (p = 0.05) (Table 2).

The lipid content is influenced by several factors such as sex, breed, feeding, and the anatomical location of the beef cut (Moreira et al., 2003Moreira, F. B., Souza, N. E., Matsushita, M., Prado, I. N., & Nascimento, W. G. (2003). Evaluation of carcass characteristics and meat chemical composition of Bos indicus and Bos indicus x Bos taurus crossbred steers finished in pasture systems. Brazilian Archives of Biology and Technology46(4), 609-616.;Prado et al., 2011Prado, I. N., Abrahão, J. J. S., Zawadzki, F., Valero, M. V., Marques, J. A., Ito, R. H., & Perotto, D. (2011). Composição química e perfil de ácidos graxos do músculo Longissimus de bovinos de diferentes grupos genéticos alimentados com silagem de sorgo ou cana-de-açúcar e terminados com 3, 4 ou 4, 8 mm de espessura de gordura de cobertura. Semina: Ciências Agrárias, 32(4), 1461-1476.;Prado et al., 2008Prado, I. N., Aricetti, J. A., Rotta, P. P., Prado, R. M., Perotto, D., Visentainer, J. V., & Matsushita, M. (2008). Carcass characteristics, chemical composition and fatty acid profile of the Longissimus muscle of bulls (Bos taurus indicus vs. Bos taurus taurus) finished in pasture systems. Asian-Australasian Journal of Animal Sciences21(10), 1449-1457.;Rotta et al., 2009aRotta, P. P., Prado, I. N., Prado, R. M., Moletta, J. L., Silva, R. R., & Perotto, D. (2009a). Carcass characteristics and chemical composition of the Longissimus muscle of Nellore, Caracu and Holstein-friesian bulls finished in a feedlot. Asian-Australasian Journal of Animal Sciences22(4), 598-604.;2009bRotta, P. P., Prado, R. M., Prado, I. N., Valero, M. V., Visentainer, J. V., & Silva, R. R. (2009b). The effects of genetic groups, nutrition, finishing systems and gender of Brazilian cattle on carcass characteristics and beef composition and appearance: a review. Asian-Australasian Journal of Animal Sciences22(12), 1718-1734.). According toRotta et al. (2009b)Rotta, P. P., Prado, R. M., Prado, I. N., Valero, M. V., Visentainer, J. V., & Silva, R. R. (2009b). The effects of genetic groups, nutrition, finishing systems and gender of Brazilian cattle on carcass characteristics and beef composition and appearance: a review. Asian-Australasian Journal of Animal Sciences22(12), 1718-1734., the beef intramuscular fat content is 3 to 5%.Nevertheless, the percentage of total lipids observed in the different cuts analyzed varied from 4.41%, in ST, to 6.17% in BF. Evidence shows that the minimum content of lipids necessary to obtain a tender and juicy beef is 2.9-3.0% (Campion, Crouse & Dikeman, 1975Campion, D. R., Crouse, J. D., & Dikeman, M. E. (1975). Predictive value of USDA beef quality grade factors for cooked meat palatability. Journal of Food Science40(6), 1225-1228.). However, even though the EE values found in the present study are within the range considered appropriate, the cuts such as the LD, ST and TT muscles showed high shear forces on the first day. This may be related to the composition of the muscle fibers as well as the number of thermostable collagen crosslink.

The WHC, a* and b* intensities, CL, and WBSF variables showed an interaction between muscles and aging time (Table 3). The highest values for a* were obtained by BF and LD on day 14, and the lowest was found in ST at 7 days of aging (p < 0.01).

In general, increasing the postmortem aging time decreases the color stability of fresh meat. There have been several studies that have looked at how aging meat in vacuum packaging affects instrumental color values.

A study conducted byLeisner, Greer, Dilts and Stiles, (1995Leisner, J. J., Greer, G. G., Dilts, B. D., & Stiles, M. E. (1995). Effect of growth of selected lactic acid bacteria on storage life of beef stored under vacuum and in air. International Journal of Food Microbiology26(2), 231-243.) found that increasing beef postmortem aging time in vacuum packaging decreased a* values (redness) when placed into a simulated retail display. In lamb loins, similar results were shown as increasing aging time in vacuum packaging from 14 days to 63 days increased discoloration and decreased a* values (Kim, Luc & Rosenvold, 2013Kim, Y. H. B., Luc, G., & Rosenvold, K. (2013). Pre rigor processing, ageing and freezing on tenderness and colour stability of lamb loins. Meat Science, 95(2), 412-418.).Lee, Apple, Yancey Sawye & Johnson, (2008Lee, M. S., Apple, J. K., Yancey, J. W. S., Sawyer, J. T., & Johnson, Z. B. (2008). Influence of vacuum-aging period on bloom development of the beef gluteus medius from top sirloin butts. Meat Science, 80(3), 592-598.) found that beef Gluteus medius steaks from top sirloin butts aged in vacuum packaging for 7 and 14 days had increased chroma values, a* values, b* values, and oxymyoglobin percentages compared to steaks from top sirloin butts aged in vacuum packaging for 28 and 35 days.

The difference in beef color may be related to the type of muscle fiber (Hood, 1980Hood, D. E. (1980). Factors affecting the rate of metmyoglobin accumulation in pre-packaged beef. Meat Science, 4(4), 247-265.). Red fibers (oxidatives) will have higher concentrations of mitochondria that typically compete with myoglobin for oxygen consumption, reducing the oxymyoglobin layer and giving a darker appearance to the muscle (Monin, 1991Monin, G. (1991). Facteurs biologiques des qualités de la viande bovine. Production Animales4(2), 151-160.,1998Monin, G. (1998). Recent methods for predicting quality of whole meat. Meat Science, 49(1), S231-S243.).

These results suggest that the muscles classified as red would have a faster discoloration rate and an increase in metmyoglobin production under aerobic exposure. However, the present study hypothesized that vacuum-packed muscles from the forequarter show a similar discoloration rate to muscles from the hindquarter, because when the oxygen is removed, the process of discoloration is slowed down. Thus, the TT, a red-fiber muscle which showed constant a* values, and this fact may be related to the anaerobic condition imposed to the muscle. Therefore, there will be less competition between mitochondria and myoglobin for oxygen, so a* will be kept at normal values.

Table 2
pH, lightness(L*) and ether extract (EE) from beef aged of Nellore young bulls finished in feedlot.

Table 3
Interaction between muscles and aging times for the meat quality traits of Nellore young bulls.

For the b* intensity, the highest value was found in the ST muscle on day 14, followed by days 7 and 1. The lowest values were obtained for the BF muscle on days 1 and 7 (Table 3). All muscles showed high b* values throughout the aging time (p = 0.03). Aged muscles show a greater yellow intensity, as observed in all studied muscles, which is attributed to storage and temperature. At higher temperatures, there is an acceleration in the pigment oxidation rate and an increase in the oxidizing reaction inside the tissue (Faustman & Cassens, 1990Faustman, C., & Cassens, R. G. (1990). The biochemical basis for discoloration in fresh meat: a review. Journal of Muscle Foods1(3), 217-243.), due to the reduced antioxidant defense and increased lipid oxidation rate resulting from the activity of free radicals (Renerre, 2004Renerre, M. (2004). La couleur de la viande et sa mesure. INRA1, 63-68.), which may also increase the oxidation of myofibrillar proteins (Rowe, Maddock, Lonergan & Huff-Lonergan, 2004Rowe, L. J., Maddock, K. R., Lonergan, S. M., & Huff-Lonergan, E. (2004). Oxidative environments decrease tenderization of beef steaks through inactivation of μ-calpain. Journal of Animal Science, 82(11), 3254-3266.).

The LD, GM, BF and TT muscles showed their greatest WHC on day one. Intermediate values were obtained for LD on day 14; GM on day 7; BF on days 7 and 14; and ST on days 1 and 14. The lowest values were found for LD on day 7; GM on day 14; ST on day 7; and TT on days 7 and 14 (Table 3).

A significant difference could be observed in the WHC for the ST and LD muscles on day 7, and then this value increased significantly on day 14. During the conversion of muscle to meat, lactic acid accumulates in the tissue, thus reducing meat pH. Once the pH has reached the isoelectric point of the main proteins, especially myosin, the protein net charge is zero, meaning that the number of positive and negative charges in the proteins is essentially the same (Huff-Lonergan & Lonergan, 2005Huff-Lonergan, E., & Lonergan, S. M. (2005). Mechanisms of water-holding capacity of meat: The role of postmortem biochemical and structural changes. Meat Science, 71(1), 194-204.).

According toLawrie (1977Lawrie, R. A. (1977). Meat: Current developments and future status. Meat Science, 1(1), 1-13.), the formation of lactic acid and the consequent drop in pH are responsible for the reduced WHC of meat during the application of forces such as cutting and heating; and at pH of 5.2 to 5.3 (IEP of the muscle proteins, with balance of positive and negative charges), the meat has a lower WHC. This fact was observed on day 7, when there was a decrease in pH, thereby reducing the WHC in the ST and LD muscles.

The TT muscle reduced its WHC with aging. This muscle is rich in red fibers, having a higher pH in relation to the other muscles. At a higher pH, the WHC is higher; thus, in the evaluation of WHC, it will lose more water than the other muscles. This can be related to the anatomical position of this muscle, which is a section from the forequarter, the others being from the hindquarter. Reduction in WHC is not desirable from the commercial aspect, because it will affect the juiciness of beef, making it drier (Huff-Lonergan & Lonergan, 2005Huff-Lonergan, E., & Lonergan, S. M. (2005). Mechanisms of water-holding capacity of meat: The role of postmortem biochemical and structural changes. Meat Science, 71(1), 194-204.).

The shear force evaluation demonstrated that the ST muscle exhibited the highest values at all aging times (p < 0.01). Thus, for this muscle, aging did not affect the tenderness until 14 days. According toShackelford et al. (1991Shackelford, S. D., Morgan, J. B., Cross, H. R., & Savell, J. W. (1991). Idedntification of threshold levels for Warner-Bratzler shear force in beef top poils steakes. Journal of Muscle Foods, 2(4), 289-296.), values up to 4.5 characterize a tender beef. Therefore, the GM and BF muscles can be considered as tender on the first day of evaluation, so the aging is not justified.

Stolowski et al. (2006Stolowski, G. D., Baird, B. E., Miller, R. K., Savell, J. W., Sams, A. R., Taylor, J. F., ... Smith, S. B. (2006). Factors influencing the variation in tenderness of seven major beef muscles from three Angus and Brahman breed crosses. Meat Science, 73(3), 475-483.) grouped muscles regarding their sensitivity to aging, and observed that the GM and LD muscles have a slow response; ST has a low response, and BF does not respond to aging. The non-significant improvement in texture in the BF muscle may be related to the low calpain values (Koohmaraie, Seideman, Schollmeyer, Dutson & Babiker, 1988Koohmaraie, M., Seideman, S. C., Schollmeyer, J. E., Dutson, T. R., & Babiker, A. S. (1988). Factors associated with the tenderness of three bovine muscles. Journal of Food Science, 53(2), 407-410.), as well as the high collagen level (Hildrum et al., 2009Hildrum, K. I., Rødbotten, R., Høy, M., Berg, J., Narum, B., & Wold, J. P. (2009). Classification of different bovine muscles according to sensory characteristics and Warner Bratzler shear force. Meat Science83(2), 302-307.).

The lowest SF was verified in the TT muscle when subjected to aging for 14 days. In agreement withShackelford, Morgan, Cross and Savell (1991Shackelford, S. D., Morgan, J. B., Cross, H. R., & Savell, J. W. (1991). Idedntification of threshold levels for Warner-Bratzler shear force in beef top poils steakes. Journal of Muscle Foods, 2(4), 289-296.), several studies demonstrate the influence of pH on the activity of cathepsins and calpains, which are proteolytic enzymes, suggesting that the observed differences in pH may be partially responsible for the differences in tenderness. The muscle from the forequarter utilized in the study, showed higher pH and tenderness in relation to the muscles from the hindquarter. The variation in tenderness may also be attributed to the connective tissue (McCormick, 1994McCormick, R. J. (1994). The flexibility of the collagen compartment of muscle. Meat Science, 36(1), 79-91.). The same author also stated that muscles with little connective tissue resulted in tender meat as compared with those with a higher level of connective tissue. Muscles with a higher proportion of white fibers present a higher amount of connective tissue (Melton, Dikeman, Tuma & Kropf , 1974Melton, C. C., Dikeman, M., Tuma, H. J., & Schalles, R. R. (1974). Histological relationships of muscle biopsies to bovine meat quality and carcass composition. Journal of Animal Science, 38(1), 24-31.,1975Melton, C. C., Dikeman, M. E., Tuma, H. J., & Kropf, D. H. (1975). Histochemical relationships of muscle biopsies with bovine muscle quality and composition. Journal of Animal Science, 40(3), 451-456.); thus, the TT muscle is considered to be a muscle with a greater proportion of red fibers, which provides a lower level of connective tissue.

For the LD muscle, a decrease in SF was observed from day 1 to 14, and the same trend was detected for TT. Therefore, aging was effective for the tenderness of these two muscles (Table 3).

When different muscles are aged, the main objective is to evaluate the aging efficiency as a technique to improve the texture of muscles from the forequarter considered as tougher, and consequently of lower economic value, aiming to standardize them with tender muscles as well as add value to products that already have an acceptable tenderness.

In fact, most aging effects occur until the 14 days postmortem, in which the shear force is reduced, and maximum tenderness was found at 14 days (Miller, et al., 2001Miller, M. F., Carr, M. A., Ramsey, C. B., Crockett, K. L., & Hoover, L. C. (2001). Consumer thresholds for establishing the value of beef tenderness. Journal of Animal Science, 79(12), 3062-3068.). However, studies have shown that seven days of aging are sufficient to eliminate genetic differences reflected in the tenderness of meat from Zebu animals (Maggioni et al., 2012Maggioni, D., Prado, I. N., Zawadzki, F., Valero, M. V., Marques, J. A., Bridi, A. M., ... Abrahão, J. J. S. (2012). Grupos genéticos e graus de acabamento sobre qualidade da carne de bovinos. Semina: Ciências Agrárias, 33(1), 391-402.;Morales et al., 2003Morales, D. C., Chardulo, L. A. L., Silveira, A. C., Oliveira, H. N., Arrigoni, M. B., Martins, C. L., & Cervieri, R. C. (2003). Avaliação da qualidade da carne de bovinos de diferentes grupos genéticos. Acta Scientiarum. Animal Sciences, 25(1), 171-175.), which was observed in the present study for the LD muscle.

Bianchini et al. (2007Bianchini, W., Silveira, A. C., Jorge, A. M., Arrigoni, M. D. B., Martins, C. L., Rodrigues, É., ... Andrighetto, C. (2007). Efeito do grupo genético sobre as características de carcaça e maciez da carne fresca e maturada de bovinos superprecoces. Revista Brasileira de Zootecnia36(6), 2109-2117.) reported no differences in beef shear force of Longissimus dorsi between 7 and 14 days of aging; however, this variable was reduced as compared with day zero. This demonstrates that aging can improve beef tenderness.

Higher CL values were registered for the ST muscle on day 7, and the BF and TT muscles on day 7 did not differ from ST. The lowest values were found for LD on day 7, GM on days 1 and 7, BF on day 1 and TT on day 14. Comparing day 1 with 14, there was no significant difference in CL for the LD, ST and TT muscles (p < 0.01). This effect is desirable, because when these muscles are aged for 14 days, CL will not be impaired (Table 3). This fact is desirable for aging, because it means that CL will not be affected if the cut is aged for 14 days, so the meat juiciness will be preserved.

The ST muscle obtained higher CL on day 14, and this effect can be compared to the high shear-force values. According toOliveira et al. (2012Oliveira, E. A., Sampaio, A. A. M., Henrique, W., Pivaro, T. M., Rosa, B. L., Fernandes, A. R. M., & Andrade, A. T. (2012). Quality traits and lipid composition of meat from Nellore young bulls fed with different oils either protected or unprotected from rumen degradation. Meat Science, 90(1), 28-35.), CL values can be influenced by WHC, which is considered a very important trait for consumption, where in low values are related to a lower nutritional value, resulting in drier and less tender meat.

Conclusion

Aging affects the qualitative and chemical properties of beef, improving aspects of tenderness and lightness.

The Trapezius thoracis muscle has a higher color stability as compared with the Longissimus muscle, and it can be aged in vacuum-package for 14 days without changes in the redness (a*).

Aging is not recommended for the Semitendinosus, because it does not improve its tenderness. The Gluteus medius and Biceps femoris are tender on the first day, and the aging process is indicated for these cuts to add value to the beef.

Acknowledgements

We thank the Universidade Estadual Paulista Júlio de Mesquita Filho for sponsoring the experiment.

References

  • Aberle, E. D., Forrest, J. C., Gerrand, D. E., Mills, E. W., & Hedrick, H. B. (2001). Principles of Meat Science (4 ed.).
  • Abularach, M. L. S., Rocha, C. E., & Felício, P. E. (1998). Características de qualidade do contrafilé (M. L. dorsi) de touros jovens da raça Nelore. Ciência e Tecnologia de Alimentos18(2), 205-210.
  • AMSA. (1995). Research guidelines for cookery, sensory evaluation and instrumental tenderness measurements of fresh meat. In AMSA. (Ed.), American Meat Science Association (p. 48). Savoy, IL: National Livestock and Meat Board.
  • AOAC-Association Official Analytical Chemist. (2005) Official Methods of Analysis (18th ed.). Gaitherburg, Maryland, USA: AOAC.
  • Bianchini, W., Silveira, A. C., Jorge, A. M., Arrigoni, M. D. B., Martins, C. L., Rodrigues, É., ... Andrighetto, C. (2007). Efeito do grupo genético sobre as características de carcaça e maciez da carne fresca e maturada de bovinos superprecoces. Revista Brasileira de Zootecnia36(6), 2109-2117.
  • Campion, D. R., Crouse, J. D., & Dikeman, M. E. (1975). Predictive value of USDA beef quality grade factors for cooked meat palatability. Journal of Food Science40(6), 1225-1228.
  • Cezar, M., & Sousa, W. (2007). Carcaças ovinas e caprinas: obtenção, avaliação e classificação. Uberaba, MG: Editora Agropecuária Tropical.
  • Faustman, C., & Cassens, R. G. (1990). The biochemical basis for discoloration in fresh meat: a review. Journal of Muscle Foods1(3), 217-243.
  • Fernandes, A. R. M., Sampaio, A. A. M., Henrique, W., Oliveira, E. A., Tullio, R. R., & Perecin, D. (2008). Características da carcaça e da carne de bovinos sob diferentes dietas, em confinamento. Arquivo Brasileiro de Medicina Veterinaria e Zootecnia60(1), 139-147.
  • Geesink, G. H., Taylor, R. G., Bekhit, A. E. D., & Bickerstaffe, R. (2001). Evidence against the non-enzymatic calcium theory of tenderization. Meat Science59(4), 417-422.
  • Geesink, G. H., Kuchay, S., Chishti, A. H., & Koohmaraie, M. (2006). μ-Calpain is essential for postmortem proteolysis of muscle proteins. Journal of Animal Science84(10), 2834-2840.
  • Guelker, M., Haneklaus, A., Brooks, J., Carr, C., Delmore, R., Griffin, D., ... & Johnson, D. (2013). National Beef Tenderness Survey-2010: Warner-Bratzler shear force values and sensory panel ratings for beef steaks from United States retail and food service establishments. Journal of Animal Science, 91(2), 1005-1014.
  • Guerrero, A., Valero, M. V., Campo, M. M., & Sañudo, C. (2013). Some factors that affect ruminant meat quality: from the farm to the fork. Review. Acta Scientiarum. Animal Sciences35(4), 335-347.
  • Hildrum, K. I., Rødbotten, R., Høy, M., Berg, J., Narum, B., & Wold, J. P. (2009). Classification of different bovine muscles according to sensory characteristics and Warner Bratzler shear force. Meat Science83(2), 302-307.
  • Hood, D. E. (1980). Factors affecting the rate of metmyoglobin accumulation in pre-packaged beef. Meat Science, 4(4), 247-265.
  • Houben, J. H., Van Dijk, A., Eikelenboom, G., & Hoving-Bolink, A. H. (2000). Effect of dietary vitamin E supplementation, fat level and packaging on colour stability and lipid oxidation in minced beef. Meat Science, 55(3), 331-336.
  • Huff-Lonergan, E., & Lonergan, S. M. (2005). Mechanisms of water-holding capacity of meat: The role of postmortem biochemical and structural changes. Meat Science, 71(1), 194-204.
  • Hunt, M. C., & Hedrick, H. B. (1977). Profile of fiber types and related properties of five bovine muscles. Journal of Food Science, 42(2), 513-517.
  • Kadim, I. T., Al-Karousi, A., Mahgoub, O., Al-Marzooqi, W., Khalaf, S. K., Al-Maqbali, R. S., ... Raiymbek, G. (2013). Chemical composition, quality and histochemical characteristics of individual dromedary camel (Camelus dromedarius) muscles. Meat Science, 93(3), 564-571.
  • Kim, Y. H. B., Luc, G., & Rosenvold, K. (2013). Pre rigor processing, ageing and freezing on tenderness and colour stability of lamb loins. Meat Science, 95(2), 412-418.
  • Kirchofer, K. S., Calkins, C. R., & Gwartney, B. L. (2002). Fiber-type composition of muscles of the beef chuck and round. Journal of Animal Science, 80(11), 2872-2878.
  • Koohmaraie, M. (1996). Biochemical factors regulating the toughening and tenderization processes of meat. Meat Science, 43, 193-201.
  • Koohmaraie, M., Seideman, S. C., Schollmeyer, J. E., Dutson, T. R., & Babiker, A. S. (1988). Factors associated with the tenderness of three bovine muscles. Journal of Food Science, 53(2), 407-410.
  • Lawrie, R. A. (1977). Meat: Current developments and future status. Meat Science, 1(1), 1-13.
  • Lee, M. S., Apple, J. K., Yancey, J. W. S., Sawyer, J. T., & Johnson, Z. B. (2008). Influence of vacuum-aging period on bloom development of the beef gluteus medius from top sirloin butts. Meat Science, 80(3), 592-598.
  • Leisner, J. J., Greer, G. G., Dilts, B. D., & Stiles, M. E. (1995). Effect of growth of selected lactic acid bacteria on storage life of beef stored under vacuum and in air. International Journal of Food Microbiology26(2), 231-243.
  • Luchiari Filho, A. (2000). Pecuária da carne bovina (1 ed.). São Paulo, SP: LinBife.
  • Macedo, L. M., Prado, I. M., Prado, J. M., Rotta, P. P., Prado, R. M., Souza, N. E., & Prado, I. N. (2008). Chemical composition and fatty acids profile of five carcass cuts of crossbred heifers finished in feedlot. Semina: Ciências Agrárias29(3), 597-608.
  • Maggioni, D., Prado, I. N., Zawadzki, F., Valero, M. V., Marques, J. A., Bridi, A. M., ... Abrahão, J. J. S. (2012). Grupos genéticos e graus de acabamento sobre qualidade da carne de bovinos. Semina: Ciências Agrárias, 33(1), 391-402.
  • Mancini, R. A., & Hunt, M. C. (2005). Current research in meat color. Meat Science, 71(1), 100-121.
  • McCormick, R. J. (1994). The flexibility of the collagen compartment of muscle. Meat Science, 36(1), 79-91.
  • Melton, C. C., Dikeman, M., Tuma, H. J., & Schalles, R. R. (1974). Histological relationships of muscle biopsies to bovine meat quality and carcass composition. Journal of Animal Science, 38(1), 24-31.
  • Melton, C. C., Dikeman, M. E., Tuma, H. J., & Kropf, D. H. (1975). Histochemical relationships of muscle biopsies with bovine muscle quality and composition. Journal of Animal Science, 40(3), 451-456.
  • Miller, M. F., Carr, M. A., Ramsey, C. B., Crockett, K. L., & Hoover, L. C. (2001). Consumer thresholds for establishing the value of beef tenderness. Journal of Animal Science, 79(12), 3062-3068.
  • Monin, G. (1991). Facteurs biologiques des qualités de la viande bovine. Production Animales4(2), 151-160.
  • Monin, G. (1998). Recent methods for predicting quality of whole meat. Meat Science, 49(1), S231-S243.
  • Morales, D. C., Chardulo, L. A. L., Silveira, A. C., Oliveira, H. N., Arrigoni, M. B., Martins, C. L., & Cervieri, R. C. (2003). Avaliação da qualidade da carne de bovinos de diferentes grupos genéticos. Acta Scientiarum. Animal Sciences, 25(1), 171-175.
  • Moreira, F. B., Souza, N. E., Matsushita, M., Prado, I. N., & Nascimento, W. G. (2003). Evaluation of carcass characteristics and meat chemical composition of Bos indicus and Bos indicus x Bos taurus crossbred steers finished in pasture systems. Brazilian Archives of Biology and Technology46(4), 609-616.
  • Oliveira, E. A., Sampaio, A. A. M., Henrique, W., Pivaro, T. M., Rosa, B. L., Fernandes, A. R. M., & Andrade, A. T. (2012). Quality traits and lipid composition of meat from Nellore young bulls fed with different oils either protected or unprotected from rumen degradation. Meat Science, 90(1), 28-35.
  • Page, J. K., Wulf, D. M., & Schwotzer, T. R. (2001). A survey of beef muscle color and pH. Journal of Animal Science, 79(3), 678-687.
  • Pereira, A. S. C., Sobral, P. J. A., Leme, P. R., & Silva, S. L. (2008). Physical and chemical characteristics of frozen ground beef and aged beef meat from Bos indicus steers supplemented with α-tocopherol acetate. Italian Journal of Food Science ,20(3), 419-425.
  • Prado, I. N., Abrahão, J. J. S., Zawadzki, F., Valero, M. V., Marques, J. A., Ito, R. H., & Perotto, D. (2011). Composição química e perfil de ácidos graxos do músculo Longissimus de bovinos de diferentes grupos genéticos alimentados com silagem de sorgo ou cana-de-açúcar e terminados com 3, 4 ou 4, 8 mm de espessura de gordura de cobertura. Semina: Ciências Agrárias, 32(4), 1461-1476.
  • Prado, I. N., Aricetti, J. A., Rotta, P. P., Prado, R. M., Perotto, D., Visentainer, J. V., & Matsushita, M. (2008). Carcass characteristics, chemical composition and fatty acid profile of the Longissimus muscle of bulls (Bos taurus indicus vs. Bos taurus taurus) finished in pasture systems. Asian-Australasian Journal of Animal Sciences21(10), 1449-1457.
  • Puga, D. M. U., Contreras, C. J. C., & Turnbull, M. R. (1999). An evaluation of tenderization of forequarter bovine meat (Triceps brachii) through methods of ageing and injection with acetic and lactic acids. Food Science and Technology19(1), 88-96.
  • Renerre, M. (2004). La couleur de la viande et sa mesure. INRA1, 63-68.
  • Rotta, P. P., Prado, I. N., Prado, R. M., Moletta, J. L., Silva, R. R., & Perotto, D. (2009a). Carcass characteristics and chemical composition of the Longissimus muscle of Nellore, Caracu and Holstein-friesian bulls finished in a feedlot. Asian-Australasian Journal of Animal Sciences22(4), 598-604.
  • Rotta, P. P., Prado, R. M., Prado, I. N., Valero, M. V., Visentainer, J. V., & Silva, R. R. (2009b). The effects of genetic groups, nutrition, finishing systems and gender of Brazilian cattle on carcass characteristics and beef composition and appearance: a review. Asian-Australasian Journal of Animal Sciences22(12), 1718-1734.
  • Rowe, L. J., Maddock, K. R., Lonergan, S. M., & Huff-Lonergan, E. (2004). Oxidative environments decrease tenderization of beef steaks through inactivation of μ-calpain. Journal of Animal Science, 82(11), 3254-3266.
  • SAS. (2004). SAS/STAT User guide, Version 9.1.2. Cary, NC, USA: SAS Institute Inc.
  • Savell, J. W., Mueller, S. L., & Baird, B. E. (2005). The chilling of carcasses. Meat Science 70(3), 449-459.
  • Shackelford, S. D., Morgan, J. B., Cross, H. R., & Savell, J. W. (1991). Idedntification of threshold levels for Warner-Bratzler shear force in beef top poils steakes. Journal of Muscle Foods, 2(4), 289-296.
  • Stolowski, G. D., Baird, B. E., Miller, R. K., Savell, J. W., Sams, A. R., Taylor, J. F., ... Smith, S. B. (2006). Factors influencing the variation in tenderness of seven major beef muscles from three Angus and Brahman breed crosses. Meat Science, 73(3), 475-483.
  • Tschirhart-Hoelscher, T. E., Baird, B. E., King, D. A., McKenna, D. R. & Savell, J. W. (2006). Physical, chemical, and histological characteristics of 18 lamb muscles. Meat Science, 73(1), 48-54.
  • Valadares Filho, S. C. (2006). Tabelas brasileiras de composição de alimentos para bovinos (Vol. 1). Viçosa, MG: UFV.
  • Valero, M. V., Torrecilhas, J. A., Zawadzki, F., Bonafé, E. G., Madrona, G. S., Prado, R. M., ... Prado, I. N. (2014). Propolis or cashew and castor oils effects on composition of Longissimus muscle of crossbred bulls finished in feedlot. Chilean Journal of Agricultural and Research74(4), 445-451. doi:10.4067/S0718-58392014000400011
  • Voges, K., Mason, C., Brooks, J., Delmore, R., Griffin, D., Hale, D., ... Maddock, R. (2007). National beef tenderness survey-2006: Assessment of Warner-Bratzler shear and sensory panel ratings for beef from US retail and foodservice establishments. Meat Science, 77(3), 357-364.
  • Wheeler, T. L., Cundiff, L. V., & Koch, R. M. (1994). Effect of marbling degree on beef palatability in Bos taurus and Bos indicus cattle. Journal of Animal Science, 72(12), 3145-3151.
  • Zawadzki, F., Prado, I. N., Marques, J. A., Zeoula, L. M., Prado, R. M., Fugita, C. A., ... & Maggioni , D.(2011). Sodium monensin or propolis extract in the diet of Nellore bulls finished in feedlot: chemical composition and fatty acid profile of Longissimus muscle. Semina: Ciências Agrárias, 32(4), 1627-1636.

Publication Dates

  • Publication in this collection
    Dec 2015

History

  • Received
    11 Feb 2015
  • Accepted
    25 June 2015
Editora da Universidade Estadual de Maringá - EDUEM Av. Colombo, 5790, bloco 40, CEP 87020-900 , Tel. (55 44) 3011-4253, Fax (55 44) 3011-1392 - Maringá - PR - Brazil
E-mail: actaanim@uem.br