Journal of Food Science

JOHNSON, R. C.; CHEN, C. M.; MULLER, T. S.; COSTELLO, W. J.; ROMANS, J. R.; JONES, K. W.

doi: 10.1111/j.1365-2621.1988.tb09249.xpmid: N/A

ABSTRACT Thirty‐four muscles/muscle groups, each 0.1 kg or greater, were dissected from each of 16 forequarters to establish a data base of individual muscle traits. Individual muscle yields, tenderness profiles, and chemical analyses indicated the muscles within the forequarter are extremely variable. The Serratus ventralis (SRV), Infraspinatus (INF) and Triceps brachii complex (lateral, long and medial heads, TBT, TBL and TBM, respectively), which are several of the larger muscles/muscle groups within the forequarter, possess tenderness profiles comparable to the Longissimus dorsi (LGD). This study suggests that maximum utilization of the beef forequarter may best be achieved when individual muscles are fabricated and marketed according to their size, tenderness potential and composition.

WHITE, F. D.; RESURRECCION, A. V. A.; LILLARD, D. A.

doi: 10.1111/j.1365-2621.1988.tb09250.xpmid: N/A

ABSTRACT Retail samples of semimembranosus were roasted, sliced, wrapped in aluminum foil and stored at 1.0°C for 0, 1, 4, and 7 days. A panel of 100 consumers evaluated samples for the variables: preference, purchase intention, flavor, off‐flavor, and intended purchase frequency at three price levels. Panelists did not rate the 0, 1, and 4‐day samples differently on all sensory variables, but the 7‐day sample was rated as significantly different (P < 0.05) from all samples on each sensory variable. Results indicate that consumers were unable to detect off‐flavor in reheated semimembranosus samples at TBA numbers of 6.3 or lower.

KOOHMARAIE, M.; BABIKER, A.S.; MERKEL, R.A.; DUTSON, T.R.

doi: 10.1111/j.1365-2621.1988.tb09251.xpmid: N/A

ABSTRACT Bovine longissimus muscles excised at slaughter were compared to cross‐sectional slices of contralateral longissimus muscles obtained 12 hr postmortem for calcium‐dependent protease (CDP), cathepsins B, H and L activity, and myofibrillar fragmentation index (MFI). Slices were suspended in either Tris‐acetate buffer, buffer + ethylene diaminotetraacetic acid (EDTA), buffer + ethylene glycol‐bis (β, aminoethyl ether) N, N, N', N'‐tetraacetic acid (EGTA) or buffer + CaCl2 for either 1, 3, or 7 days while the postmortem associated changes were followed. EDTA, EGTA and Ca++ had no effect on cathepsin B, H or L activities. EDTA and EGTA treated slices had 149% whereas Ca++ 48% of control CDP activity. Postmortem changes were completed after 24 hr of Ca++ treatment but did not occur in EDTA‐ and EGTA‐treated slices. Thus, the changes observed during postmortem storage appeared to be associated with CDP activity rather than catheptic enzymes.

PATERSON, B. C.; PARRISH, F. C.; STROMER, M. H.

doi: 10.1111/j.1365-2621.1988.tb09252.xpmid: N/A

ABSTRACT The effects of sodium chloride (NaCl) and pyrophosphate (PP) were examined by treating beef sternomandibularis muscle tissue and isolated beef myofibrils with various concentrations of NaCl, with and without 10 mM PP. Gel electrophoresis showed that higher NaCl concentrations (1.0M > 0.7M > 0.4M) increased the extraction of titin, myosin, and other myofibrillar proteins from beef tissue and that the inclusion of 10 mM PP to NaCl solutions enhanced the extraction of those proteins. Beef tissue water‐holding capacity (WHC) was increased by higher NaCl concentrations and the presence of 10 mM PP. Increased myofibrillar/cytoskeletal protein extraction, especially titin, was associated with increased beef myofibril swelling and increased beef muscle WHC.

CLARKE, A. D.; SOFOS, J. N.; SCHMIDT, G. R.

doi: 10.1111/j.1365-2621.1988.tb09253.xpmid: N/A

ABSTRACT Structured beef was prepared with eight combinations of the ingredients (sodium alginate, calcium carbonate, lactic acid/calcium lactate) used to bind meat with the algin/calcium gelation mechanism at nine pH values (4.1–6.4) in order to evaluate their influence on its physical and sensory characteristics. Products with alginate alone were similar to samples from the treatment without binders. The combination of alginate/calcium/lactate gave products of higher values (P>0.05) for parameters such as hardness in the raw state, bind and penetration than all other treatments. Decreasing pH values increased raw and cooked product hardness and penetration force. Products of pH values 5.7–5.8 were superior to other treatments in bind scores evaluated by a sensory panel.

PRABHU, G. A.; MOLINS, R. A.; KRAFT, A. A.; SEBRANEK, J. G.; WALKER, H. W.

doi: 10.1111/j.1365-2621.1988.tb09254.xpmid: N/A

ABSTRACT The shelf‐life of refrigerated (2–4°C) pork chops inoculated with Clostridium sporogenes PA3679 and Staphylococcus aureus Z88 was examined in products sliced from loins cooked to 66°C (150°F), dipped in 5% polyphosphate blend, 2.5% potassium sorbate or 2% acetic acid solutions, vacuum‐packaged and stored at 2–4°C. The effect of a second in‐the‐bag cooking step to 66°C (150°F) after vacuum packaging was also studied. Pork chops not reheated after packaging showed incipient spoilage after 15 days at 2–4°C, depending on surface treatment. The second cooking increased the shelf‐life of refrigerated product to more than 60 days and reduced counts of inoculated cultures to undetectable levels. However, on exposure of the chops to simulated mishandling (24–25°C), clostridial growth was detected in all samples except those dipped in polyphosphate or acetic acid solutions.

CHEN, C.M.; JONES, K.W.

doi: 10.1111/j.1365-2621.1988.tb09255.xpmid: N/A

ABSTRACT Cured hams prepared with various blends of pork and turkey were investigated. No difference in cooking yield was found. Product containing 50% or more turkey meat was lower (P < 0.05) in fat than blends containing predominantly pork. The presence of turkey thigh meat resulted in higher (P < 0.01) pH and TBA values compared to blends containing all pork. Total pigment and nitroso pigment values increased (P < 0.05) as the amount of turkey meat increased in the formulation. Consumer sensory panelists found no significant preferential difference between blends. Storage effects revealed only minor changes in pH, TBA values, and microbiological profiles over the 9 wk storage period.

DUDZIAK, JUDITH A.; FOEGEDING, E. ALLEN; KNOPP, JAMES A.

doi: 10.1111/j.1365-2621.1988.tb09256.xpmid: N/A

ABSTRACT A myosin/actomyosin mixture (MAM), actomyosin and myosin were isolated from post‐rigor turkey. Rheological properties of MAM gels were determined by uniaxial compression. Breast MAM formed gels which were stable at lower protein concentrations (10 and 15 mg/mL) than thigh MAM (20 and 25 mg/mL). Differential scanning calorimetry (DSC) and a fluorescent hydrophobic probe, 8‐anilino‐l‐napthalene sulfonate (ANS), were used to study thermal transitions. One DSC peak was observed in breast and thigh MAM. ANS thermograms showed that thigh actomyosin had a greater transition temperature (Tr) (51.8°C) than breast actomyosin (49.7°C). The ANS Tr was 48°C for both myosins. The difference in gelation appeared to be associated with protein‐protein interactions.

HUBER, DONNA GERWIG; REGENSTEIN, JOE M.

doi: 10.1111/j.1365-2621.1988.tb09257.xpmid: N/A

ABSTRACT An exhaustively washed chicken breast muscle fraction formed a stable emulsion despite the absence of any soluble material. Measurements of the oil droplet size suggested that about 1 mg of myosin was available per square meter of oil droplet surface. This was less than the amount required to fully cover the surface of the oil droplets and suggested that the classical emulsification theory did not hold for meat “emulsion” products. The formation of a matrix (gel) in the aqueous phase might be a significant contributor towards stabilizing meat sausage‐type products.

DUDZIAK, JUDITH A.; FOEGEDING, E. ALLEN

doi: 10.1111/j.1365-2621.1988.tb09258.xpmid: N/A

ABSTRACT Myosin/actomyosin (MAM) was extracted from post‐rigor turkey breast and thigh muscles using Hasselbach‐Schneider solution. Electrophoretic evaluation of the breast muscle protein extract showed it to be 86.4% myosin and 7% actin. Thigh muscle MAM contained 79.4% myosin and 4.7% actin. Slight variations in minor protein bands were observed between the breast and thigh MAM electrophoretic profiles. Gel filtration of MAM on a 2% agarose column separated actomyosin from myosin. Myosin purity was 97.9% and 99.2% for breast and thigh, respectively. Gel filtration data indicated that myosin, unassociated with actin, was the predominate protein extracted from the post‐rigor tissue. Myosin was approximately 67‐72% of the original MAM.