J. Anim Sci. 2008. 86:1904-1916. doi:10.2527/jas.2007-0478
© 2008 American Society of Animal Science
Chemical properties of cow and beef muscles: Benchmarking the differences and similarities1,2
L. E. Patten*,
J. M. Hodgen*,
A. M. Stelzleni
,
C. R. Calkins*,3,
D. D. Johnson and
B. L. Gwartney
* Department of Animal Science, University of Nebraska, Lincoln 68583-0908;
and
Department of Animal Sciences, University of Florida, Gainesville 32611; and
National Cattlemen’s Beef Association, Englewood, CO 80155
 |
Abstract
|
|---|
The objective of this study was to identify muscles from cow populations that are equivalent or may possibly be made equivalent to muscles from A-maturity, Select-grade cattle in terms of chemical, compositional, and color characteristics. Objective color, expressible moisture, proximate composition, pH, heme iron concentration, and total collagen content were determined for 9 muscles (M. gluteus medius, M. infraspinatus, M. longissimus dorsi, M. psoas major, M. rectus femoris, M. tensor fascia latae, M. teres major, M. triceps brachii lateral-head, and M. triceps brachii long-head) from 15 cattle from each of 5 commercially identified populations [fed beef cows (B-F), non-fed beef cows (B-NF), fed dairy cows (D-F), non-fed dairy cows (D-NF), and A-maturity, Select-grade cattle (SEL)]. Muscles from B-F and B-NF populations were more similar to the SEL than were the D-F and D-NF. There were 2 muscles, the M. infraspinatus and M. teres major, from the population of B-F that were similar, physically and chemically, to SEL in most traits. The majority of the 9 muscles from the cows did not differ (P < 0.05) from SEL for percentage expressible moisture, proximate composition, and total collagen content. However, notable differences in pH, objective color L*, total pigment content, and heme iron content existed between cow populations and SEL. The muscles from SEL had significantly (P < 0.05) lower total pigment and heme iron concentrations. These differences likely relate to the visual appearance of muscles from the different populations of cattle. Two of the 9 muscles studied were similar among cow populations and A-maturity, Select-grade beef.
Key Words: cow muscle • beef • color • composition • dairy • muscle property
|
INTRODUCTION
|
|---|
According to the 1999 National Market Cow and Bull Beef Quality Audit (Roeber et al., 2001
), 25 to 30% of a producer’s revenue comes from market cows and bulls. Typically, cows fall in the C, D, and E maturity carcasses, and much of the carcass is processed into ground beef. By marketing cows and bulls differently, an increase in the value of those animals might be increased. Hodgson et al. (1992) and Johnson and Rogers (1997) developed prediction equations to better classify cows so that value could be enhanced by utilizing more of the subprimals or altering manufacturing procedures.
One way to improve the value of the cow carcass is to feed cull cows an energy-dense diet before slaughter to improve the fat color and palatability and increase the fat content and lean yields (Schnell et al., 1997). Additionally, Apple (1999) found that cull cows with BCS of 6 had the most economic value to producers and packers. In a further study, it was shown that cows with a body score of 6 or above had at least 73.3% of the carcasses grading US Utility or higher (Apple et al., 1999).
The longissimus muscle from cull cows fed 0, 28, 56, and 84 d on a high-energy, high protein diet or a high-energy, low protein diet with electrical stimulation were found to have some improvement in palatability and quality traits, but it was speculated these longissimus steaks were not comparable with steaks from young fed beef (Boleman et al., 1996).
Following the muscle profiling that was done on A-maturity cattle (Von Seggern et al., 2005), a similar study was done with cow carcasses to characterize 21 muscles based on chemical and physical properties (Buford, 2003). Based on cattle type (beef vs. dairy), chemical and physical properties of the cow carcasses were found to be similar on all measured traits except percent moisture. There may be potential to market cow muscles that are comparable in chemical and physical traits to A-maturity animals.
The objective of this study was to identify muscles from different cow populations that are equivalent or may possibly be made equivalent to muscles from A-maturity, Select grade cattle in chemical, compositional, and color characteristics.
|
MATERIALS AND METHODS
|
|---|
Experimental Design
No approval was obtained from the Institutional Animal Care and Use Committee because the samples were obtained from a federally inspected slaughter facility.
Five commercially identified populations of cattle were the main effects: fed dairy cows (D-F), non-fed dairy cows (D-NF), fed beef cows (B-F), non-fed beef cows (B-NF), and A-maturity, USDA Select grade steers (SEL). Sample collection occurred on separate occasions with multiple lots at Packerland Packing Co., Green Bay, WI, because all 5 treatment groups were slaughtered at the facility. The lot numbers and identities of the cattle were used to identify the groups of cattle that could be used for this study. The live cattle were classified by experienced plant personnel. Cows commercially identified as fed were those that were perceived by buyers and plant personnel to have received supplemental energy before slaughter. The carcasses from each group came together across the grading chain, which made selection of the final samples possible. At the grading chain, personnel from the University of Nebraska-Lincoln and the University of Florida-Gainesville selected the carcasses that met the specified criteria. All carcasses had to have at least 2.54 mm of backfat and have medium or greater muscling (1 = light– and 8 = heavy°; EUROP conformation system; Anonymous, 1981). Carcasses with missing muscles due to trimming were not selected. Hot carcass weight, LM, lean and bone maturity, KPH percentage, marbling score, fat color (1 = white, 2 = creamy white, 3 = slightly yellow, 4 = moderately yellow, 5 = yellow), and lean color (1 = extremely dark red, 2 = dark red, 3 = moderately dark red, 4 = slightly dark cherry-red, 5 = slightly bright cherry-red, 6 = moderately bright cherry-red, 7 = bright cherry-red, 8 = extremely bright cherry-red) were recorded.
Fifteen carcasses from each population of cattle were selected. The total number of carcasses was 75. Nine muscles were removed from each side of the carcasses for a total of 1,350 muscles. The muscles studied were the M. gluteus medius (GLM), M. infraspinatus (INF), M. longissimus dorsi (LOD), M. psoas major (PSO), M. rectus femoris (REF), M. tensor fascia latae (TFL), M. teres major (TER), M. triceps brachii lateral-head (MTB), and M. triceps brachii long-head (LTB; Table 1). When each carcass was fabricated, the muscles from each side were grouped and labeled. Muscles from one side of each carcass were shipped to the University of Florida, Gainesville, for sensory and shear force measurements (Stelzleni et al., 2007) and muscles from the other side of each carcass were shipped to the University of Nebraska, Lincoln.
The carcasses were split between the 12th and 13th rib, separating the forequarter from the hindquarter. Shoulder clods, from the primal chuck, were removed from the selected carcasses. No muscles were collected from the rib and plate primals. The primal loin was separated from the hindquarter, leaving the sirloin and knuckle intact with the loin. No muscles were collected from the primal round. The 9 muscles were then fabricated from the primal chuck and loin. Individual muscles were excised from the primal and labeled with an identification tag. Commodity (untrimmed) weight was taken. The muscles were then denuded of all external fat and epimysium using a mechanical membrane skinner, and a denuded weight was taken. The length, width, and depth of the muscles were measured. The dimensions and weights were taken by personnel from the University of Florida, Gainesville (Stelzleni et al., 2007). Muscles were vacuum-packaged (without heat shrink), boxed, palletized according to destination (University of Nebraska, Lincoln, or University of Florida, Gainesville), and stored under refrigerated conditions (2 to 4°C) until transportation under refrigeration to the respective universities. Muscles arrived at the University of Nebraska, Lincoln, Loeffel Meat Laboratory within 2 to 5 d. Upon arrival, the muscles were held in a cooler (2 to 4°C) until further sample preparation. All muscles were aged for a total of 7 to 10 d in dark storage.
Objective Color
Objective color was measured at the University of Nebraska, Lincoln, Loeffel Meat Laboratory. After the aging period, the vacuum bags were carefully opened to minimize the loss of purge, as it would be added back to the sample during grinding. Muscles were allowed to bloom for one h before color measurement. A Mini Scan XE Plus (Model 45/0-L, HunterLab, Reston, VA), hand-held colorimeter was used to determine objective color. Care was taken to avoid taking color measurements of areas of the muscles with large amounts of connective tissue or fat streaking. The colorimeter was fitted with a 2.54-cm port and was standardized using a black tile and white tile (X = 78.5, Y = 83.2, and Z = 88.7). The colorimeter was programmed to take a series of 3 color readings, measuring L*, a*, and b* using illuminant A and 10° standard observer. Illuminant A represents incandescent lamplight with an approximate color temperature of 2,854°K. The average of the 3 readings was used for statistical analysis. Chroma values were calculated as the square root of (a*)2 + (b*)2.
Expressible Moisture
Samples (no less than 3 g) for expressible moisture determination were removed from individual muscles following objective color measurements and before grinding. Water holding capacity was measured using a centrifugation procedure that measures expressible moisture. Expressible moisture was measured in duplicate on the meat samples according to the method of Jauregui et al. (1981). Two pieces of Whatman #3 (Whatman International Ltd., Maidstone, UK) filter paper were folded around one piece of VWR grade 410 (Whatman International Ltd.) filter paper to form a thimble. The meat sample was added to the filter paper thimble, and the thimble was placed into a 50-mL centrifuge tube to be centrifuged (Sorvall RC 5B, DuPont Co., Wilmington, DE) at 32,500 x g for 15 min at 4°C. Expressible moisture was calculated as the percentage of weight lost from the original sample.
Further Sample Preparation
After objective color measurements were made and samples for water holding capacity had been removed, individual muscles were ground through a 1.27-cm plate using a Hobart Grinder, model number 4732 with a #32 head (The Hobart Manufacturing Co., Troy, OH) or a Toledo Chopper, model number 5120-0-009 (Toledo Scale Co., Toledo, OH). The larger muscles were ground through the Hobart Grinder, and the smaller muscles were ground through the Toledo Chopper. Muscle purge was added back to the meat during grinding. One hundred grams of ground sample was collected, formed into a patty, placed in a plastic bag with an identification tag, and frozen at –29°C. The grinder plate and blades were removed and cleaned after the grinding of each muscle to prevent mixing of muscle samples. The samples were later pulverized using liquid nitrogen and a Waring blender (Waring Products Division, New Hartford, CT) and used for proximate analysis, pH, and heme iron, and total collagen analyses. Pulverized muscle was stored at –29°C no longer than 6 mo to complete the chemical analysis.
Proximate Composition
Pulverized samples were used to determine moisture, ash, and fat composition. Moisture and ash were measured using a LECO Thermogravimetric Analyzer-601 (Model 604–100–400, Leco Corp., St. Joseph, MI). This machine calculates the percent moisture and ash with the assistance of the TGA-601 Windows option (version 1.2, Leco Corp.) software. Fat content of the homogenized samples was determined by Soxhlet ether extraction using AOAC (1990) procedures. The distillation process was allowed to continue for 48 h. Moisture, ash, and fat content were determined in duplicate. Protein content was calculated by difference.
Measurement of pH
A 10 g sample of powdered muscle was weighed into a beaker, and 90 mL of distilled, deionized water was added to the sample. The meat and water solution was homogenized at 10,800 rpm for 30 s using a Polytron (Brinkman Instruments, New York, NY) blender. A stir bar was placed in the homogenized solution, and pH was measured while stirring. A bulb tip combination electrode (Orion model 9256BN, Orion Research Inc., Boston, MA) with an Orion SA 720 pH meter (Orion Research Inc.) was used.
Total Heme Iron Concentration
Total pigment and heme iron concentrations were analyzed using the method of Hornsey (1956) as modified by Lee et al. (1998). Total pigment of the precipitate was determined using a Cary 100 Varian UV/Visible Spectrophotometer (Varian Instruments, Sugar Land, TX) by taking the absorbance at 640 nm multiplied by 680. Total pigment was then used to calculate total heme iron [(total pigment x 8.82)/100]. Total heme iron values are reported as ppm (parts per million, or mg/kg).
Total Collagen Content
Due to the expense of the assay and time limitations, only one-third of the muscles were analyzed for total collagen content, so 5 carcasses from each group of cattle were analyzed. To determine which carcasses were sampled for total collagen content, the means for HCW and 12th-rib fat thickness were taken. The 5 carcasses that had HCW and 12th-rib fat thicknesses most closely matching the means were chosen for analysis. Total collagen was determined in duplicate using pulverized samples. Samples (3 ± 0.03 g) of pulverized muscle were weighed and then hydrolyzed for 18 h with 25 mL of 6 N HCl to liberate hydroxyproline (Hill, 1966). Hydroxyproline was quantified using the spectrophotometric assay outlined by Bergman and Loxley (1963) and modified by using a stronger buffer in the oxidant solution, which negated the need to raise the pH of the filtrate (Kolar, 1990). A factor of 7.25 was used to convert hydroxyproline values into total collagen values (Goll et al., 1963). Collagen values were reported as milligrams of collagen per gram of sample.
Statistical Analysis
Individual muscle samples were analyzed using the GLIMMIX procedure (SAS Inst. Inc., Cary, NC) to test main effects and interactions. A randomized complete block design with 5 treatments was used. There were 15 carcasses per treatment. For collagen analysis, a subsample of 5 carcasses per treatment was used. In all models, the Kenward-Roger denominator degree of freedom approximation was used. When indicated significant by ANOVA (P 
0.05) main effects were separated using the LSMEANS, DIFF, and LINES functions, whereas simple effects of interactions were generated using the LSMEANS, SLICE, and SLICEDIFF functions.
|
RESULTS AND DISCUSSION
|
|---|
Carcass Characteristics
Carcass characteristics (Table 2) differed between SEL and B-F, B-NF, D-F, and D-NF. Hot carcass weights from the population of SEL were lighter (P < 0.05) than carcass weights of D-F and heavier than carcass weights of B-NF, but similar to B-F and D-NF. The HCW from the SEL population were slightly heavier than HCW from A-maturity native or dairy cattle (356.67 and 364.60 kg, respectively) in the 2000 National Beef Quality Audit (McKenna et al., 2001). As expected, the overall maturity of SEL was younger than the other populations. A-maturity, USDA Select-grade cattle had whiter fat color and brighter lean color scores than the other populations. These cattle may have been fed a high concentrate diet for a longer period of time resulting in whiter fat color (Strachan et al., 1993; French et al., 2000), and younger animals display lighter and brighter lean color. With the exception of the B-F population, SEL had the most external fat measured at the 12th rib, and SEL had less KPH than D-NF and D-F. The SEL population mean 12thrib fat thickness fell between fat thickness values for A-maturity native and dairy cattle, whereas KPH was higher than the native cattle, but only slightly lower than the dairy cattle in the 2000 NBQA (McKenna et al., 2001). Carcasses from B-F, D-NF, and D-F had more marbling than SEL. However, SEL carcasses were heavier muscled and had larger LM than the other populations. Muscling scores can be influenced by the nutritional status of the animal. If cattle are on a low plane of nutrition they may be forced to metabolize muscle tissue to maintain energy, thereby reducing yields (Murphy and Loerch, 1994; Gomez-Pasten et al., 1999). Yield grades were higher (P < 0.05) for B-F, D-NF, and D-F than SEL.
Although a feeding trial was not conducted as part of this experiment, it is obvious that different populations of cows exist. Carcass data indicate that beef cows are more like A-maturity, USDA Select-grade cattle than dairy cows for many carcass characteristics. In many cases, there are apparent differences between the populations of cows that likely received additional feeding and those not selected for additional feeding. For example, B-NF cattle were older, leaner, and lighter in weight than B-F cattle. Perhaps those cows not selected for additional feeding are not going to benefit enough from feeding to make it worth the cost.
Objective Color
There was a group x muscle interaction (P < 0.001) for L* value (Table 3). Seven of 9 muscles from SEL cattle were significantly (P < 0.05) lighter (higher L*) than the same muscles from each of the other populations of cattle (Table 3). The INF and TER from B-F did not differ from SEL. In general, as animals advance in age the muscle tissue becomes darker. When results from Buford (2003) whose work was conducted on cow muscles were compared with results from Von Seggern et al. (2005) who studied A-maturity muscles, muscles from cows were darker than muscles from A-maturity carcasses. Boleman et al. (1996) found cows fed 0 d had higher metmyoglobin levels and lower L* values than cows fed 28 or 56 d, but in this study only the REF, TER, and TFL in beef cows showed a difference L* values in fed versus non-fed cows.
The majority of muscles from the SEL population did not differ from muscles from the other populations of cattle for a* values (Table 4) with a higher a* value indicating the muscle is more red than green. There were 7 of 36 comparisons with SEL cattle that were different (P < 0.05) and a group x muscle interaction of P < 0.001. The GLM and MTB from B-F had greater a* values than the same muscles from SEL, and the MTB was unique and different from the other cow groups. For D-NF, the LOD had a greater a* value and the LTB had a lower a* value than the SEL LOD and LTB, respectively. Interestingly, the TER a* value was lower in all the groups (P = 0.040 B-NF, 0.005 D-NF, and 0.015 D-F) except B-F (P = 0.066) when compared with the TER from SEL.
Table 5 shows the group x muscle interaction (P = 0.015) for b* color values. The higher the b* value, the more yellow the muscle appears. The B-F muscles were not different from the SEL muscles for b* values. In contrast, the D-F, D-NF, and B-NF had 5, 3, and 2 muscles different from the SEL with the TER being less yellow than the SEL for all 3 groups. The LTB and MTB from D-NF and D-F cows had lower b* values (LTB P = 0.030 and 0.005; MTB P = 0.005 and 0.011, respectively) than the LTB and MTB from SEL. The REF from B-NF and D-F were also slightly less yellow (P = 0.046 and 0.044, respectively) than the same muscles from SEL.
Chroma is a measure of color intensity, and a higher chroma value means the muscle color is more vivid. Twenty-nine of 36 observations from cow muscles did not have significantly (P < 0.05) different chroma values than SEL (Table 6), but there was a group x muscle interaction (P = 0.002). Except for the B-F, the TER from the other 3 cow groups were significantly less vivid (P < 0.05) from the SEL. The LTB from the 2 dairy groups and the MTB from the D-NF were also less vivid than the respective muscle from the SEL, whereas the GLM from B-F was more vivid than the GLM from SEL and the other cow groups. The MTB from the B-F was also more vivid in color than the other cow groups. Romans et al. (1965a) indicated that chroma values decreased significantly (P < 0.01), indicating that muscles became darker with increasing maturity. This study indicated that only a few muscles were different in chroma values compared with SEL, but when there is a significant difference the chroma value from the cow muscles are typically less than the SEL muscles.
Expressible Moisture
Expressible moisture is the amount of liquid removed from a sample when force is applied (Fennama, 1990), and it is a measure of the water-holding capacity of a muscle. For 8 of 9 muscles, the cow populations did not differ from SEL (Table 7) although the group x muscle interaction was P = 0.004. Only the TFL from D-NF and D-F had significantly (P = 0.003 and 0.002, respectively) lower percentages of expressible moisture compared with the SEL, meaning that they had greater water-holding capacity. The pH values for the TFL from the 2 populations of cows were higher (P = 0.030 D-NF and 0.005 D-F), which would increase water-holding capacity. The reason pH has such a profound effect on water-holding capacity is because of the relationship between muscle swelling and pH.
Proximate Composition
There was a significant interaction (P < 0.001) between group and muscle for moisture content (Table 8). When differences existed, muscles from B-F and D-F had lower percentages of moisture, whereas muscles from B-NF had higher percentages of moisture. The D-NF and the SEL muscles were not different for moisture content. Buford (2003) reported that the percent-age moisture and fat were most commonly influenced by 12th-rib fat thickness where the moisture content decreased and fat content increased as fat thickness increased. This relationship between moisture and fat content was also observed in this study. For those muscles from populations of cattle that had lower moisture values, higher fat values were observed and vice versa. Twelfth-rib fat thickness may also have influenced findings in this study. Muscles that differed in fat composition (Table 9) from D-F and B-F had higher percentages of fat than SEL, whereas B-NF had lower percentages of fat than SEL. The amount of intramuscular fat is a major contributor to the variation in percentage of moisture and fat. Romans et al. (1965b) reported increases in marbling increase fat content and decrease water content.
Percentage protein (Table 10) from cow muscles was the same as muscles from SEL for most of the muscles studied in each group, but an interaction of P < 0.001 was observed for the 9 muscles from the 5 groups. Only the PSO from D-F (P < 0.001) and D-NF (P = 0.005), REF from B-F (P = 0.045) and D-F (P = 0.009), LTB from D-NF (P = 0.034), and GLM from D-F (P = 0.006) had lower percentages of protein than SEL. Similar results were observed in a study of the beef longissimus from cattle that were 6, 18, 42, or 90 mo of age because Tuma et al. (1963) found no difference in protein content.
Unlike the other compositional components of the different cattle population, there was no group x muscle interaction for ash content (P = 0.084). Only the muscles from the B-F had more ash than the other populations (Table 11). There were also significant differences observed between muscles (P < 0.001) with the GLM having the most ash and the INF and TFL having the least.
Variation in age of the animal, muscle function, nutritional status, and the quality grade of the carcass may all impact the proximate composition of individual muscles.
Muscle pH
Muscle pH differed (P = 0.05) between the 5 cattle populations and 9 muscles (Table 12). The most noticeable differences from the SEL muscles were muscles from the populations of D-NF and D-F. For 12 of 18 observations the pH of muscles from the dairy populations was higher than the SEL. Only the LOD and GLM had a pH similar to SEL for all the cattle populations. The INF, REF, and TFL from B-NF also had higher (P = 0.013, 0.001, and 0.035, respectively) pH values than SEL. Muscle pH is dependent on the amount of glycogen present in the muscles at the time of slaughter. Muscle glycogen content may be influenced by the animal’s diet and stress before slaughter. If glycogen stores are depleted before slaughter, pH decline is slowed and a higher than normal ultimate pH will occur (Lawrie, 1958). The role of pH is very broad because it has an effect on many characteristics of meat. Muscles that maintain a high pH will be very dry in appearance on the exposed surface because water is tightly bound to the proteins and very dark in color.
Total Pigment and Heme Iron Concentration
The SEL population had significantly (P < 0.001) lower total pigment and heme iron concentrations than the other cattle populations (Tables 13 and 14, respectively). These findings relate to research by Buford (2003) and Von Seggern et al. (2005) indicating the heme iron content of muscles from A-maturity cattle is lower than the same muscles from market cows. Romans et al. (1965a) reported an increase in myoglobin content as animals increased in maturity, and Field et al. (1980) observed the pigment content of steers and cows were double and triple the concentrations of pigment found in veal calves, respectively. The TER and the TFL had the lowest pigment content, whereas the GLM, INF, and LTB were among the highest (Tables 13 and 14).
Total Collagen Content
Total collagen content (Table 15) did not differ between SEL and the other cow populations, nor among cow populations, for 7 of 9 muscles. The GLM from D-NF had more total collagen (P = 0.032) than SEL, whereas the INF from the B-NF, B-F, and D-F had significantly less collagen than the SEL and D-F. Several researchers have established the amount of heat-labile collagen in bovine skeletal muscle decreases as the animal matures, but cattle fed high-energy diets see increases in protein synthesis and therefore should see an increase in heat-labile collagen (Aberle et al., 1981; Miller et al., 1987). The decrease in heat-labile collagen is responsible for the age-associated toughness of beef (Goll et al., 1964; Hill, 1966; Herring et al., 1967; Shimokomaki et al., 1972). Prost et al. (1975) indicated no change in content of connective tissue with the age of the animal. Conversely, Wilson et al. (1954) reported significantly higher amounts of collagen in veal samples compared with cow or steer samples. However, Wilson et al. (1954) found no differences in collagen content between steer and cow samples. Total collagen content for SEL was 8.45 mg/g in the LOD. Much research has been done using the longissimus. According to Herring et al. (1967), total collagen content in the longissimus from A-maturity cattle was 4.52 mg/g. However, Miller et al. (1983) reported a much higher value of 11.00 mg/g of total collagen for the longissimus from A-maturity cattle.
The majority of muscles from cows did not differ from SEL for percent expressible moisture, proximate composition, and total collagen content although the SEL muscles were almost always lighter (higher L* value) than the older cattle populations. In general, muscles from both populations of beef cows had similar objective color measurements for a* and b* and pH as muscles from SEL. However, this was not always the case for muscles from the populations of dairy cows. In speculation, breed type may influence these findings. Most likely, the SEL were beef breed type and therefore genetically more like beef cows than dairy cows. Furthermore, SEL may have been managed more like beef cows than dairy cows.
In general, the B-F and SEL muscles were very similar for most traits especially in respect to the INF and TER. The INF had less total collagen in the B-F and B-NF than the SEL, and not surprisingly, the B-F and B-NF had a higher total pigment and heme iron content than SEL.
Overall, the most notable difference between muscles from dairy cow populations and SEL was found in objective color (L*), pH, total pigment content, and heme iron content. Muscle pH from cows, particularly in the populations of dairy cows, was higher than SEL. Although this does not appear to affect water holding capacity, except in the case of the TFL from D-NF and D-F, it may influence muscle color. Muscles with higher pH values may appear darker. Furthermore, muscles from cows have greater total pigment and heme iron content than muscles from SEL.
Different populations of cows exist, and there are muscles from those populations that have similar chemical, compositional, and color properties when compared with muscles from A-maturity, USDA Select-grade cattle. Perhaps those muscles could be utilized in a manner similar to muscles from younger cattle, which would increase the value of those muscles from cows when these data are combined with the sensory and WBSF data (Stelzleni et al., 2007). However, most muscles from cows were darker in color, had higher pH values, and had greater heme iron content than muscle from younger cattle, which may be undesirable to consumers. The chemical, compositional, and color data in combination with the physical, WBSF, and sensory data (Stelzleni, 2006) will reveal important information comparing meat from young fed cattle to fed and non-fed beef and dairy cattle. Supplemental technology may be needed to upgrade muscles from cow carcasses.
|
Footnotes
|
|---|
1 Funded by the Beef Checkoff. The authors would also like to thank J. Hyde, N. Brown, and T. Jones for technical assistance and S. Pitchie for secretarial assistance. 
2 A contribution of the University of Nebraska Agricultural Research Division, Lincoln, NE 68583. Journal Series No. 15121.
3 Corresponding author: ccalkins1{at}unl.edu
Received for publication July 30, 2007.
Accepted for publication March 18, 2008.
|
LITERATURE CITED
|
|---|
Aberle, E. D., E. S. Reeves, M. D. Judge, R. E. Hunsley, and T. W. Perry. 1981. Palatability and muscle characteristics of cattle with controlled weight gain: Time on high energy diet. J. Anim. Sci. 52:757–763.[Abstract/Free Full Text]
Anonymous. 1981. Council Regulation (EEC) No. 1208/81 determining the Community scale for the classification of carcasses of adult bovine animals. Off. J. L 123:7.5.1981, 3–6.
AOAC. 1990. Official Methods of Analysis, 14th Edition. Assoc. Off. Anal. Chem., Washington, DC.
Apple, J. K. 1999. Influence of body condition score on live and carcass value of cull beef cows. J. Anim. Sci. 77:2610–2620.[Abstract/Free Full Text]
Apple, J. K., J. C. Davis, J. Stephenson, J. E. Hankins, J. R. Davis, and S. L. Beaty. 1999. Influence of body condition score on carcass characteristics and subprimal yield from cull beef cows. J. Anim. Sci. 77:2660–2669.[Abstract/Free Full Text]
Bergman, I., and R. Loxley. 1963. Two improved and simplified methods for the spectrophotometric determination of hydroxyproline. Anal. Chem. 35:1961–1965.
Boleman, S. J., R. K. Miller, M. J. Buyck, H. R. Cross, and J. W. Savell. 1996. Influence of realimentation of mature cows on maturity, color, collagen solubility, and sensory characteristics. J. Anim. Sci. 74:2187–2194.[Abstract]
Buford, M. L. 2003. Cow muscle profiling: Chemical and physical properties of 21 muscles from beef and dairy cows. MS Thesis. Univ. Nebraska, Lincoln, NE.
Fennama, O. R. 1990. Comparative water holding properties of various muscle foods (a critical review relating to definitions, methods of measurement, governing factors, comparative data and mechanistic matters). J. Muscle Foods 1:363–381.[CrossRef]
Field, R. A., L. R. Sanchez, J. E. Kunsman, and W. G. Kruggel. 1980. Heme pigment content of bovine hemopoietic marrow and muscle. J. Food Sci. 45:1109–1112.[CrossRef]
French, P., E. G. O’Riordan, F. J. Monahan, P. J. Caffery, M. Vidal, M. T. Mooney, D. J. Troy, and A. P. Moloney. 2000. Meat quality of steers finished on autumn grass, grass silage or concentratebased diets. Meat Sci. 56:173–180.[CrossRef]
Goll, D. E., R. W. Bray, and W. G. Hoekstra. 1963. Age associated changes in muscle composition. The isolation and properties of collagenous residue from bovine muscle. J. Food Sci. 28:503–509.[CrossRef]
Goll, D. E., W. G. Hoekstra, and R. W. Bray. 1964. Age-associated changes in bovine muscle connective tissue. II. Exposure to increasing temperature. J. Food Sci. 29:615–621.[CrossRef]
Gomez-Pasten, M., O. Mora, J. Pedraza-Chaverri, and A. Shimada. 1999. The effect of long term feed restriction on metabolism and tissue composition of goats. J. Agric. Sci. 132:227–232.[CrossRef]
Herring, H. K., R. G. Cassens, and E. J. Briskey. 1967. Factors affecting collagen solubility in bovine muscles. J. Food Sci. 32:534–538.[CrossRef]
Hill, F. 1966. The solubility of intramuscular collagen in meat animals of various ages. J. Food Sci. 31:161–166.[CrossRef]
Hodgson, R. R., K. E. Belk, J. W. Savell, H. R. Cross, and F. L. Williams. 1992. Development of a quantitative quality grading system for mature cow carcasses. J. Anim. Sci. 70:1840–1847.[Abstract]
Hornsey, H. C. 1956. The color of cooked cured pork. I. Estimation of nitric oxidehaem pigments. J. Sci. Food Agric. 7:534–540.[CrossRef]
Jauregui, C. A., J. M. Regenstein, and R. C. Baker. 1981. A simple centrifugal method for measuring expressible moisture, a waterbinding property of muscle foods. J. Food Sci. 46:1271–1273.[CrossRef]
Johnson, D. D., and A. L. Rogers. 1997. Predicting the yield and composition of mature cow carcasses. J. Anim. Sci. 75:1831–1836.[Abstract/Free Full Text]
Kolar, K. 1990. Colorimetric determination of Hydroxyproline as a measure of collagen content in meat and meat products: NMKL collaborative study. J. Assoc. Off. Anal. Chem. 73:54–57.[Medline]
Lawrie, R. A. 1958. Physiological stress in relation to dark-cutting beef. J. Sci. Food Agric. 9:721–727.[Medline]
Lee, B. J., D. G. Hendricks, and D. P. Cornforth. 1998. Antioxidant effects of carosine and phytic acid in a model beef system. J. Food Sci. 63:394–398.[CrossRef]
McKenna, D. R., P. K. Bates, D. L. Roeber, T. B. Schmidt, J. B. Morgan, J. W. Savell, T. H. Montgomery, and G. C. Smith. 2001. National beef quality audit-2000: Results of carcass assessments. Final Report. National Cattleman’s Beef Association, Engelwood, CO.
Miller, R. K., H. R. Cross, J. D. Crouse, and T. G. Jenkins. 1987. Effect of feed energy intake on collagen characteristics and muscle quality of mature cows. Meat Sci. 21:287–294.[CrossRef]
Miller, R. K., J. D. Tatum, H. R. Cross, R. A. Bowling, and R. P. Clayton. 1983. Effects of carcass maturity on collagen solubility and palatability of beef from grain-finished steers. J. Food Sci. 48:484–486.[CrossRef]
Murphy, T. A., and S. C. Loerch. 1994. Effects of restricted of growing steers on performance, carcass characteristics, and composition. J. Anim. Sci. 72:2497–2507.[Abstract]
Prost, E., E. Pelczynska, and A. W. Kotula. 1975. Quality characteristics of bovine meat. I. Content of connective tissue in relation to individual muscles, age and sex of animals and carcass quality grade. J. Anim. Sci. 41:534–540.[Abstract/Free Full Text]
Roeber, D. L., P. D. Mies, C. D. Smith, K. E. Belk, T. G. Field, J. D. Tatum, J. A. Scanga, and G. C. Smith. 2001. National market cow and bull beef quality audit-1999: A survey of producer-related defects in market cows and bulls. J. Anim. Sci. 79:658–665.[Abstract/Free Full Text]
Romans, J. R., H. J. Tuma, and W. L. Tucker. 1965a. Influence of carcass maturity and marbling on the physical and chemical characteristics of beef. I. Palatability, fiber diameter and proximate analysis. J. Anim. Sci. 24:681–685.[Abstract/Free Full Text]
Romans, J. R., H. J. Tuma, and W. L. Tucker. 1965b. Influence of carcass maturity and marbling on the physical and chemical characteristics of beef. II. Muscle pigments and color. J. Anim. Sci. 24:686–690.[Abstract/Free Full Text]
Schnell, T. D., K. E. Belk, J. D. Tatum, R. K. Miller, and G. C. Smith. 1997. Performance, carcass, and palatability traits for cull cows fed high-energy concentrate diets for 0, 14, 28, 42 or 56 days. J. Anim. Sci. 75:1195–1202.[Abstract/Free Full Text]
Shimokomaki, M., D. F. Elsden, and A. J. Bailey. 1972. Meat tenderness: Age related changes in bovine intramuscular collagen. J. Food Sci. 37:892–896.[CrossRef]
Stelzleni, A. S. 2006. Feeding and aging effects on carcass composition, fatty acid profiles and sensory attributes of muscles from cull cow carcasses. PhD Diss. Univ. Florida, Gainesville.
Stelzleni, A. M., L. E. Patten, D. D. Johnson, C. R. Calkins, and B. L. Gwartney. 2007. Benchmarking carcass characteristics and muscles from commercially identified beef and dairy cull cow carcasses for Warner-Bratzler shear force and sensory attributes. J. Anim. Sci. 85:2631–2638.[Abstract/Free Full Text]
Strachan, D. B., A. Yang, and R. D. Dillon. 1993. Effect of grain feeding on fat colour and other carcass characteristics in previously grass-fed Bos indicus steers. Aust. J. Exp. Agric. 33:269–273.[CrossRef]
Tuma, H. J., R. L. Henrickson, G. V. Odell, and D. F. Stephens. 1963. Variation in the physical and chemical characteristics of the longissimus dorsi muscle from animals differing in age. J. Anim. Sci. 22:354–357.[Abstract/Free Full Text]
Von Seggern, D. D., C. R. Calkins, D. D. Johnson, J. E. Brickler, and B. L. Gwartney. 2005. Muscle profiling: Characterizing the muscles of the beef chuck and round. Meat Sci. 71:39–51.[CrossRef]
Wilson, G. D., R. W. Bray, and P. H. Phillips. 1954. The effect of age and grade on the collagen and elastin content of beef and veal. J. Anim. Sci. 13:826–831.[Abstract/Free Full Text]
This article has been cited by other articles:
|
|
|
|
 
E. Pavan and S. K. Duckett
Corn oil or corn grain supplementation to steers grazing endophyte-free tall fescue. I. Effects on in vivo digestibility, performance, and carcass quality
J Anim Sci,
November 1, 2008;
86(11):
3215 - 3223.
[Abstract]
[Full Text]
[PDF]
|
|
|
Top
Abstract
INTRODUCTION
