Cooked color of precooked ground beef patties manufactured with mature bull trimmings.

Lean (80%) ground beef was formulated with 0, 25, 50, 75, or 100% mature bull trimmings, formed into patties, cooked to 71 °C in an air-impingement oven, and stored at -20 °C until reheating to 71 °C either in a microwave oven or on a gas-fired chargrill. Instrumental color of raw patties was not (P ≥ .080) affected by levels of bull trim. After initial cooking, internal cooked redness values were not affected (P ≥ .202) by the proportion of bull trim; however, the internal reheated patty redness increased (greater a* values and lesser HA; P ≤ .001) with increasing proportions of bull trimmings. Formulating ground beef with high levels (>50%) of mature, bull trimmings had minimal effects on raw ground beef color, but patties formulated with the highest proportions of bull trimmings appeared undercooked even after cooking twice to 71 °C.

Application of tension to prerigor goat carcasses to improve cooked meat tenderness.

In two separate experiments, carcasses of intact Kiko × Boer male kids were assigned randomly to tension treatments applied 30 min postmortem: 1) suspended by the Achilles tendon (AT); 2) suspended from the pelvic bone with front and hind legs tied together (TS); or 3) suspended by the Achilles tendon, and the fore- and hindsaddle were separated at the 12th/13th thoracic intervertebral disk, external fat, accessory muscles and epimysium surrounding the longissimus muscle (LM) were cut (TC), and a 2.3-kg weight attached to the neck (TC + W). Warner-Bratzler shear force values for the LM were reduced (P < 0.05) 24.4 to 35.9 N in TS carcasses compared to AT carcasses, and WBSF values of SM from TS carcasses were 25.0 and 20.3 N less (P < 0.05) than those for AT and TC + W carcasses, respectively. Results indicated that cooked goat meat tenderness, particularly the LM and SM, may be improved greatly by suspending goat carcasses by the pelvic bone.

Color stability and tenderness variations within the gluteus medius from beef top sirloin butts.

Beef top sirloin butts (n=48) from USDA quality grade (QG; upper 2/3 US Choice vs. US Select) and yield grade categories (YG; 1 and 2 vs. 4 and 5) were aged 14 days, GM steaks were cut, with 2 steaks removed from the anterior (ANT), middle (MID) and posterior (POST) sections of the GM. One steak from each section was cut into lateral (LAT), central (CENT) and medial (MED) portions, packaged aerobically, and displayed for 7 days, whereas the second steaks were cooked to 71°C for WBSF. Top Choice-steaks were redder and more yellow (P<0.05) than Select steaks during display. Cooking losses were greatest (P<0.05) in the MED, and least (P<0.05) in the CENT, portions of GM steaks. Neither QG nor YG category affected WBSF, but differences within the GM were found for (P<0.05) WBSF. Results of this experiment indicate tenderness and color stability gradients exist within the GM.

Compositional and instrumental firmness variations within fresh pork bellies.

Fresh pork bellies (n=24) were cut into 15 sections to measure the intra-belly variation in compositional and mechanical firmness characteristics. Length and width of each belly was measured before the belly was divided into 3 rows (D = dorsal; C = central; and V = ventral) and 5 columns (labeled 1, 2, 3, 4, and 5 from cranial to caudal), resulting in 15 belly sections of equal dimensions. The belly section with the greatest compression value was D-1, whereas the lowest compression value was found in the V-4 section (column×row, P<0.001). Conversely, the greatest and least puncture values were observed in the C-2 and V-5 locations, respectively (column×row, P=0.016). The D-3 section had the lowest proportion of lean and the greatest proportion of fat, but the greatest lean and lowest fat percentages were found in the V-1 and C-4 sections, respectively (column×row, P<0.001). The greatest proportions of saturated fatty acids (SFA) were found in the V-4 and V-5, and the lowest proportions of SFA were in D-1 (column×row, P<0.001). Moreover, C-4 and V-1 had the greatest percentages of monounsaturated fatty acids (MUFA), whereas the lowest MUFA content was observed in D-1, D-2, and D-3 (column×row, P<0.001). The D row (columns 1, 2, 3, and 5) also had the greatest proportion of polyunsaturated fatty acids (PUFA), but the lowest proportions of PUFA were located in C-4, V-4, and V-5 (column×row, P<0.001). Consequently, the iodine value was greatest in D-1 and lowest in V-4, V-5, and C-5 (column×row, P<0.001). It is apparent from these results that there is an obvious fatty acid composition gradient within bellies, which results in considerable intra-belly variation in composition and firmness.

Plk1 activation by Ste20-like kinase (Slk) phosphorylation and polo-box phosphopeptide binding assayed with the substrate translationally controlled tumor protein (TCTP).

The mitotic protein kinase Plk1 catalyzes events associated with centrosome maturation, kinetocore function, spindle formation, and cytokinesis and is a target for anticancer drug design. It is composed of a N-terminal kinase domain and a C-terminal polo-box domain (PBD). The PBD domain serves to localize the kinase on cognate phosphorylated substrates, and this binding relieves the inhibition of the kinase by the PBD. Similar to many protein kinases, Plk1 is activated by phosphorylation on a threonine residue, Thr210, in the activation segment. In this work, we describe expression in Escherichia coli cells and purification of full-length Plk1 in quantities suitable for structural studies and use this material for quantitative characterization of the activation events with the substrate translationally controlled tumour protein (TCTP). The presence of the PBD-binding phosphopeptide enhances phosphorylation by the activating Ste20-like kinase (Slk). Native Plk1 exhibits a basal catalytic efficiency k cat/ K(M) of 9.9 x 10 (-5) s (-1) microM (-1). Association with a polo-box-binding phosphopeptide increased the catalytic efficiency by 11x largely through an increase in k(cat) with no change in K(M). Phosphorylation by Slk increases catalytic efficiency by 202x with a 2.3-fold reduction in K(M) and 88-fold increase in k(cat). Phosphorylation and the presence of the PBD-binding phosphopeptide result in an increase in catalytic efficiency of 1515x with a 2.3-fold decrease in K(M) and a 705-fold increase in k(cat) over the unmodified Plk1. Knowledge of kinase regulatory mechanisms and the structures of the Plk1 individual domains has allowed for a model to be proposed for these activatory events.