Effect of porcine stress syndrome on the solubility and degradation of myofibrillar/cytoskeletal proteins.

This study examined the effect of stress classification (stress-positive, stress-carrier, stress-negative) of pigs on selected properties of postmortem muscle, including protein solubility and degradation of proteins such as titin. Longissimus muscle samples were removed 45 min postslaughter, divided into samples, and stored at 0 to 2 degrees C for analysis at 0, 1, 3, 5, and 7 d postmortem. Whole-muscle samples (homogenates) and purified myofibrils were prepared from each sample for analysis by SDS-PAGE. A portion of each muscle sample also was extracted 1) with a low-ionic-strength solution to obtain a sarcoplasmic protein fraction and 2) with two different high-ionic-strength solutions to obtain a myofibrillar/cytoskeletal protein fraction for measurement of protein solubility and for analysis of extracts by SDS-PAGE. No significant differences were observed between muscle from stress-negative and stress-carrier animals in this study. Sarcoplasmic (P less than .05) and myofibrillar/cytoskeletal (P less than .01) protein solubility was lower in muscle samples from stress-positive animals than in muscle samples from stress-carrier and stress-negative animals at all postmortem times studied. The high molecular weight protein titin was degraded more slowly postmortem in muscle from stress-positive than in muscle from stress-negative animals, as observed by SDS-PAGE analysis of whole-muscle samples (homogenates) an myofibrils. The combination of lowered protein solubility and reduced rate of postmortem degradation of structural proteins such as titin may explain, at least in part, the reduced quality and protein functionality of muscle from stress-positive pigs.     

Myofibrillar proteolysis in chick muscle cell cultures during heat stress

The effect of heat stress on protein oxidation and myofibrillar proteolysis in chick myotubes was investigated. Myotubes were incubated at 37 or 41°C for 6 and 24 h. Protein carbonyl content, as an index of protein oxidation, increased more at 41°C than at 37°C for 6 and 24 h incubations. N^τ‐methylhistidine release as an index of myofibrillar proteolysis also increased more at 41°C than at 37°C for 6 and 24 h incubations. Proteasome activity also increased more under those same conditions. Calpain and cathepsin D but not B + L activities showed a greater increase at 41°C than at 37°C for 24 but not the 6 h incubation. These results indicate that heat stress increases protein oxidation and proteasome activity, resulting in an increase in myofibrillar proteolysis for short‐term incubation and, for long‐term incubation, it increases calpain, proteasome and cathepsin D activities, finally accelerating myofibrillar proteolysis in chick myotubes.     

Spoilage of light (PSE-like) and dark turkey meat under aerobic or modified atmosphere package: microbial indicators and their relationship with total volatile basic nitrogen

1. The aim of this work was to evaluate the shelf life of turkey meat from different colour categories (Pale, Soft and Exudative (PSE)-like), intermediate and dark), packaged under aerobic or modified atmosphere (MAP) conditions; also to establish a relationship between microbial quality and total volatile basic nitrogen (TVB-N), evaluating its capacity for shelf life determination. 2. Breasts were selected according to luminance (L*) and pH(24): L >/= 51 and pH < 5.8 for light colour, 43 < L < 51 for intermediate colour, L 5.8 for dark colour. Sliced meat was packaged under aerobic or MAP conditions with 50% N(2) and 50% CO(2), then stored in the dark at 0 +/- 1 degrees C for periods of 12 or 25 d. Meat under aerobic conditions was evaluated for microbiological characteristics and TVB-N on d 0, 5 and 12. This evaluation was extended to include d 19 and 25 when samples were under MAP conditions. 3. The dark meat group after 12 d of storage in aerobiosis presented significantly higher plate counts of aerobic mesophilic, psychrotrophic micro-organisms and higher TVB-N than other meat colour categories. The shelf life of turkey meat under MAP was one week longer for intermediate and light colour meat (20 d) than for dark meat. TVB-N values of 20 to 30 mg NH(3)/100 g turkey meat correspond to advanced spoilage stages. We proposed 14 mg NH(3)/100 g as the limit of freshness acceptability for turkey meat. 4. TVB-N was an indicator of turkey meat microbial spoilage but was not a suitable early predictor for microbial spoilage and in particular for turkey meat stored under MAP conditions because counts of micro-organisms were moderately correlated (Pseudomonas spp. and Enterobacteriaceae) with this index, as they were inhibited by MAP gas mixture and storage temperature used in the present study.     

Influence of packaging method and storage time on shear value and mechanical strength of intramuscular connective tissue of chevon

The objectives of this study were to determine the effects of storage time (ST) and packaging method (PM) on tenderness and changes in intramuscular connective tissue (IMCT) strength of chevon. Spanish does (8 mo of age, average BW 25 kg) were harvested (n = 12), chilled at 4 degrees C for 24 h, and then fabricated into 2.5-cm-thick leg, shoulder/arm, and loin/rib cuts. The cuts from six carcasses were vacuum-packed and aged at 2 degrees C for 0, 4, 8, or 12 d. To assess the influence of a packaging method that favors oxidation on postmortem tenderization, the cuts from the remaining six carcasses were placed on styrofoam trays, overwrapped with polyvinyl-chloride film, and stored at 2 degrees C for similar periods. At each ST, longissimus (LM), semimembranosus (SM), and triceps brachii (TB) muscles were assessed for Warner-Bratzler shear (WBS) values. The WBS of uncooked meat, myofibrillar fragmentation index (MFI), and collagen solubility were assessed on LM. The IMCT samples were prepared to assess changes in mechanical strengths and for scanning electron microscopy (SEM). Intact honeycomb structures of endomysium, with no muscle fiber elements, were observable under SEM. The PM or ST did not influence the mechanical strength of IMCT preparations, as measured by a texture analyzer. Collagen solubility of LM muscles also did not change during aging. For both PM, cooked meat WBS values were higher (P < 0.01) in SM and TB than in LM. In the SM samples, the average WBS values were higher (P < 0.01) at d 0 than at other ST. Although MFI of LM increased with increasing aging time (P < 0.05), changes in WBS over ST were minimal in TB and LM samples. The WBS of uncooked LM decreased sharply up to 8 d postmortem in both PM (P < 0.05). However, there was no PM x ST interaction to indicate any adverse influence of packaging on tenderization of chevon. The results suggest that aging chevon cuts for more than 4 d may not result in significant additional improvement in tenderness.     

Physicochemical properties of water-soluble myofibrillar proteins prepared from chicken breast muscle

The solubility of skeletal muscle myofibrillar proteins in water was examined. The solubility of the proteins was found to be sensitive to ionic strength and pH of the solution. At the ionic strength of less than 12 mM and neutral pH, more than 80% of myofibrillar proteins were solubilized. Heating at a temperature of more than 70°C was required for the proteins to retain their solubility. The solubility of freeze‐dried protein powder prepared from water‐soluble myofibrillar proteins was also examined, and it was found that addition of trehalose and heating were essential for re‐solubilization in water. Amino acid composition of water‐soluble myofibrillar proteins was found to be almost the same as that of myofibrillar proteins.     

Resistance of Berne virus to physical and chemical treatment

Thermal inactivation of Berne virus proceeded at a linear rate between 31 degrees and 43 degrees C. Storage at temperatures lower than -20 degrees C preserved the infectivity, while at 4 degrees C appreciable loss occurred between 92 and 185 days. Freeze-drying or desiccation at 22 degrees C caused only insignificant loss of infectivity. Virus preparations were not affected by pH values between 2.5 and 10.3. Inactivation by UV occurred more rapidly than with herpes, toga and rhabdoviruses. Berne virus infectivity was sensitive to pronase and B. subtilis proteinase. It was not inactivated by trypsin and chymotrypsin treatment, which resulted in enhancement of infectivity; low concentrations of pronase (less than 10 micrograms ml-1) had a similar effect on Berne virus. Neither phospholipase C or RNase, alone or in combination, nor sodium deoxycholate (0.1%) inactivated the virus; in contrast, Triton X-100 (0.1%; 1.0%) caused rapid inactivation with a constant level of residual infectivity.     

Effect of stresses before slaughter on changes to the physiological, biochemical and physical characteristics of duck muscle.

1. This experiment was designed to study the effects of fasting and enforced exercise on the physiological, biochemical and physical characteristics of duck muscle. 2. Sixty 75-d-old male ducks weighing 3.0 +/- 0.2 kg were assigned to three treatments: a control, and an 8 and 24 h fast plus enforced exercise for 10 min. The ducks were then sacrificed and the carcass stored at 4 degrees C for 24 h. 3. Although the pH and serum lactate contents gradually increased with fasting time the responses were not significant. The ultimate pH was elevated and the lactate of breast and thigh muscles was lower in stressed birds. 4. The activity of lactic dehydrogenase was significantly increased by the stress, and the activities of creatine phosphokinase and alkaline phosphatase were also increased slightly. However, no effect was found on the ATPase activity of the myofibrillar protein of either breast or thigh muscle as a result of the stress. The ATPase activity of myofibrillar protein of breast muscle significantly increased with storage time. 5. The extractability of myofibrillar protein increased with storage time for all treatments. The SDS-PAGE patterns of myofibrillar proteins were also studied. 6. Consequently DFD-like muscle was observed in the breast and thigh muscles of ducks which had been stressed.     

Effect of pre-incubation storage conditions on hatchability,chick weight at hatch and hatching time in broiler breeders

1. Eggs were stored for two different times at varying temperatures. The effects on hatchability, chick weight at hatch and hatching time were examined in two broiler breeder lines from 33 to 58 weeks of age. 2. Short storage (1 to 3 d). Storage at 20 degrees C compared with 16.5 degrees C reduced hatchability of all eggs set. No effect was observed on hatchability of fertile eggs, hatching time or chick weight. 3. Long storage (9 to 11 d). Storage at 16.5 degrees C compared with 10 degrees C decreased both hatchability of fertile eggs and chick weight at hatch. Incidence of early embryonic death increased and incubation time decreased at 16.5 degrees C compared with 10 degrees C. 4. Chicks from morning eggs were heavier than those from afternoon eggs irrespective of storage conditions. 5. Hatchability (all eggs set and fertile eggs) and chick weight varied with hen age irrespective of storage conditions. During long storage, hatching time varied with hen age independently of breeder line, storage temperature or egg laying time. 6. Hatchability (all eggs set and fertile eggs) was higher in line A than in line B. Line B eggs hatched later and produced heavier chicks than line A eggs irrespective of storage time.     

单宁酸对生长猪胃-小肠仿生消化中消化酶活性及饲粮粗蛋白消化率的影响

本试验旨在探讨单宁酸对生长猪胃、小肠仿生消化中消化酶活性及玉米-豆粕型饲粮干物质和粗蛋白消化率的影响，为评价单宁酸的生物学效应提供参考。试验一采用单因素完全随机设计，考察在无饲粮下2种单宁酸对猪模拟胃液、模拟小肠液消化酶活性的影响。设5个处理，单宁酸添加量分别为0 mg （胃液体积为20 mL，小肠液体积为22 mL）；单宁酸1，10 mg；单宁酸1，20 mg；单宁酸2，10 mg；单宁酸2，20 mg。测定各处理的胃蛋白酶、淀粉酶、胰蛋白酶和糜蛋白酶的活性。试验二考察玉米-豆粕型饲粮添加单宁酸对猪仿生消化中胃、小肠阶段消化酶活性及养分消化率的影响。采用单因素完全随机设计，设5个处理，单宁酸在饲粮中的含量分别为0 mg·（2 g）^-1；单宁酸1，10 mg·（2 g）^-1；单宁酸1，20 mg·（2 g）^-1；单宁酸2，10 mg·（2 g）^-1；单宁酸2，20 mg·（2 g）^-1。测定仿生消化中胃阶段0.5和4 h时胃蛋白酶活性，小肠阶段0.5、4和8 h时淀粉酶、胰蛋白酶和糜蛋白酶活性及生长猪胃-小肠仿生消化测定饲粮的干物质和粗蛋白消化率。结果表明：1）无饲粮的情况下，和空白对照组相比，2种单宁酸对模拟胃液中胃蛋白酶活性无显著影响（P>0.05），单宁酸1比单宁酸2更高地降低了模拟小肠液中淀粉酶、胰蛋白酶和糜蛋白酶的活性（P<0.05）。2）在饲粮进行仿生消化的胃消化0.5～4 h内，除4 h时10 mg·（2 g）^-1添加量外，添加单宁酸1时胃蛋白酶的活性均显著高于添加单宁酸2时的相应值（P<0.05），除单宁酸2在消化0.5 h外，2种单宁酸在添加10 mg·（2 g）^-1时胃蛋白酶活性均显著高于20 mg·（2 g）^-1添加量的相应值（P<0.05）。在小肠仿生消化0.5 h时，饲粮中添加单宁酸1、2的2个水平对消化液中淀粉酶活性无显著影响（P>0.05），但均显著降低了糜蛋白酶的活性（P<0.05）；单宁酸1的消化液中胰蛋白酶活性高于单宁酸2的相应值（P<0.05）。在小肠仿生消化4 h时，除添加水平为20 mg·（2 g）^-1时的糜蛋白酶活性外，饲粮中添加单宁酸1消化液中淀粉酶、糜蛋白酶活性高于添加单宁酸2的相应值，而胰蛋白酶活性低于添加单宁酸2的相应值（P<0.05）。单宁酸1、2的两个添加量均降低了胰蛋白酶和糜蛋白酶的活性（P<0.05）。在小肠仿生消化8 h时，饲粮中单宁酸的添加量影响了淀粉酶的活性，但单宁酸1和单宁酸2各两个添加量在淀粉酶的平均活性上无显著差异（P>0.05）。单宁酸1、2的两个添加量均降低了胰蛋白酶、糜蛋白酶的活性（P<0.05）。3）与对照组相比，两种单宁酸在两种添加水平下均显著降低了饲料粗蛋白消化率（P<0.05），且单宁酸2比单宁酸1更多地降低了饲粮粗蛋白的消化率（P<0.05）。综上所述，在有、无饲粮条件下，单宁酸对消化酶活性呈现不一致影响。单宁酸影响饲粮粗蛋白的消化率可能主要与消化液中糜蛋白酶活性降低以及单宁酸与饲粮中的化学成分形成螯合物降低了小肠消化酶的水解效率有关。     

In ovo temperature manipulation influences post-hatch muscle growth in the turkey

1. The effect of manipulating egg incubation temperature for short periods on turkey muscle development was determined using the M. semitendinosus, a thigh muscle, as the model. 2. Experiment 1. Eggs were incubated at a control temperature of 37.5 degrees C. For a 4-d period of 0 to 4, 5 to 8, 9 to 12, 13 to 16, 17 to 20 or 21 to 24 embryonic days (ED) eggs were transferred to either 38.5 or 35.5 degrees C. A regime of 38.5 degrees C at 5 to 8 and 9 to 12 ED caused an increased myonuclei number and muscle fibre number, respectively. 3. Experiment 2. Eggs were incubated at a control temperature of 37.5 degrees C. At 5 to 8 ED eggs were transferred to 38.5 or 35.5 degrees C. Temperature-manipulated embryos showed a delay in differentiation (myogenin expression) of the semitendinosus muscle compared to controls. 4. Manipulating the incubation temperature for 4 d in early incubation alters muscle development in the turkey with no observation of deformities or reduction in hatchability. We speculate that this increase in temperature may result in an improved muscle growth in the post-hatch bird.     

Survival of dietary antigens in the digestive tract of calves intolerant to soybean products

Preruminant calves were given a series of feeds containing heated soybean flour. Digesta collected from the small intestine were analysed by haemagglutination inhibition assay for soluble soybean antigens. The presence of undenatured glycinin and beta-conglycinin in ileal contents was associated with digestive disturbances. In vitro experiments showed that, under optimal conditions of pH for protease activity, beta-conglycinin but not glycinin, was unaffected by pepsin and both antigens were resistant to rennin and trypsin. The solubility of glycinin and beta-conglycinin in saline extracts remained high over pH ranges of 2 to 3 and 6 to 10 but under conditions of intermediate pH, about 4.5, solubility was minimal. It was concluded that preruminant calves suffer from gastrointestinal hypersensitive responses to certain soybean products because major proteases of the digestive tract fail to denature soluble antigenic constituents of the soybean protein.     

Pancreatic exocrine secretion in steers infused postruminally with casein and cornstarch

Our objective was to evaluate the effect of postruminal protein infusion on pancreatic exocrine secretions. One Holstein, two crossbred, and five Angus steers (305 +/- 5 kg) with pancreatic pouch-duodenal reentrant cannulas and abomasal infusion catheters were used in a replicated 4 x 4 Latin square. All steers were abomasally infused with 1,050 g/d of raw cornstarch with treatments of 0, 60, 120, or 180 g/d of sodium casein suspended in water to yield 6,000 g/d of infusate daily. Steers were limit-fed (1.5 x NEm; 12 equal portions daily) a 90% corn silage, 10% supplement diet formulated to contain 12.5% CP. Periods consisted of 3 d of adaptation to infusion, 7 d of full infusion, 1 d of collection, and 7 d of rest. Pancreatic juice was collected in 30-min fractions continuously for 6 h. Total juice secreted and the pH of individual fractions were recorded, a 10% subsample was retained to form a composite sample, and remaining fluid was returned to the duodenum. Juice composite samples were stored (-30 degrees C) until analyzed for total protein and activities of alpha-amylase, trypsin, and chymotrypsin. Casein infusion linearly increased alpha-amylase concentration (182 to 271 units/mL; P < 0.02; 17.5 to 24.6 units/mg of protein; P < 0.03) and secretion rate (26,847 to 41,894 units/h; P < 0.01). Total juice secretion (155 g/h), pH of pancreatic juice (8.13), secretion rate of protein (1,536 mg/h), and concentration of protein (10.2 mg/mL) in pancreatic secretions were not affected (P > 0.05) by casein infusion. Similarly, casein infusion did not change 0.05) trypsin and chymotrypsin concentrations (1,379 and 349 units/L or 0.134 and 0.033 units/mg of protein, respectively) or secretion rates (206 and 52 units/h, respectively). Abomasal infusion of protein with starch stimulated a greater pancreatic secretion of alpha-amylase activity into the intestine than infusion of starch alone.     

Stability of glutathione peroxidase in swine plasma samples under various storage conditions.

The stability of plasma glutathione peroxidase under different temperatures (4 degrees C vs. -15 degrees C), various durations of storage (0, 1, 2, 3, 7, 14, 28 and 56 d), and storage under inert gas (nitrogen (N2)) vs air is described. The glutathione peroxidase activity of swine plasma decreased consistently with storage at either 4 degrees C or -15 degrees C 1-56 d after collection, and differed (P less than or equal to 0.01) from the initial values. Storage under N2 at -15 degrees C slowed the rate of enzyme activity decrease but did not maintain the initial activity. For absolute measurements, it is suggested that swine plasma glutathione peroxidase activity be measured immediately after separation from the blood cells or be assayed within 24 h in plasma samples stored at -15 degrees C with air space displaced by N2. If relative treatment differences in enzyme activity are satisfactory, then assays can be conducted after controlled periods of storage.     

Immunoblot analysis of calpastatin degradation: evidence for cleavage by calpain in postmortem muscle.

A negative correlation exists between calpastatin activity and meat tenderness. Therefore, it is important to determine the mechanism of calpastatin inactivation in postmortem skeletal muscle. Western immunoblot analysis was performed to determine the protease(s) responsible for degradation of muscle calpastatin during postmortem storage. To accomplish this, purified calpastatin was digested with different proteases in vitro, and their pattern of calpastatin degradation was compared with that of calpastatin degradation in postmortem muscle. Polyclonal antibodies raised in mice against recombinant bovine skeletal muscle calpastatin were used to monitor calpastatin degradation. Lamb longissimus was stored at 4 degrees C and sampled at 0, 6, 12, 24, 72, 168, and 336 h postmortem. Postmortem storage produced a discrete pattern of calpastatin degradation products that included immunoreactive bands at approximately 100, 80, 65, 54, 32, and 29 kDa. Undegraded calpastatin (130 kDa) was barely detectable after 72 h of postmortem storage at 4 degrees C, and no immunoreactive calpastatin was observed by 336 h postmortem. For in vitro proteolysis, lamb longissimus calpastatin (0 h postmortem) was purified using Affi-Gel Blue chromatography. Calpastatin was digested with m-calpain, mu-calpain, cathepsin B, proteasome, trypsin, or chymotrypsin. Each of these enzymes degraded calpastatin. Immunoreactive fragments resulting from digestion of calpastatin with m- and mu-calpain were similar to each other and closely resembled those observed during postmortem aging of lamb longissimus at 4 degrees C. Digestion of calpastatin with mu-calpain reduced calpastatin activity. Degradation of calpastatin by other proteases resulted in unique patterns of immunoreactive fragments, distinct from that observed in longissimus. Thus, m- and(or) mu-calpain seem to be responsible for calpastatin degradation during postmortem storage of meat.     

Digestive enzyme concentrations and activities in healthy pancreatic tissue of horses

OBJECTIVE: To measure concentrations and activities of major digestive enzymes in healthy equine pancreatic tissue. ANIMALS: 7 adult horses with normal pancreatic tissues. PROCEDURES: Small pieces of pancreatic tissue were collected immediately after euthanasia, immersed in liquid nitrogen, and maintained at -80 degrees C until analyzed. Concentrations and activities of amylase, lipase, chymotrypsin, trypsin, and elastase were determined by use of a microtiter technique. Relative pancreatic protein concentrations were determined by use of bovine serum albumin as the standard. Pancreatic DNA was extracted and con-centrations determined by use of the diphenylamine method with calf thymus DNA as the standard. RESULTS: The pancreatic cellular concentration of each enzyme, expressed as units per milligram of DNA, was consistent among horses. Cellular concentration of lipase (1,090.8 +/- 285.3 U/mg of DNA) was highest, followed by amylase (59.5 +/- 9.8 U/mg of DNA). Elastase, trypsin, and chymotrypsin were detected in small concentrations (1.9 +/- 0.6, 3.5 +/- 1.5, and 9.6 +/- 2.9 U/mg of DNA, respectively). Similar results were obtained for specific activities of the enzymes. CONCLUSIONS AND CLINICAL RELEVANCE: Results were unexpected because, under natural conditions, the predominant energy source for horses is carbohydrate. These results may indicate, in part, the reason horses seem to tolerate large amounts of fat added to their diet.     

Influence of early postmortem protein oxidation on beef quality

The objective of this study was to examine the effect of early postmortem protein oxidation on the color and tenderness of beef steaks. To obtain a range of oxidation levels, the longissimus lumborum muscles (LM) from both strip loins of 20 steers fed either a finishing diet with vitamin E (1,000 IU per steer daily, minimum of 126 d [VITE]; n = 10 steers) or fed the same finishing diet without vitamin E (CON; n = 10 steers) were used. Within 24 h after slaughter, the LM muscle from each carcass was cut into 2.54-cm-thick steaks and individually vacuum packaged. Steaks from each steer were assigned to a nonirradiated group or an irradiated group. Steaks were irradiated within 26 h postmortem, and were aged at 4 degrees C for 0, 1, 3, 7, and 14 d after irradiation. Steaks from each diet/irradiation/aging time treatment were used to determine color, shear force, and degree of protein oxidation (carbonyl content). Steaks from steers fed the VITE diet had higher (P < 0.01) alpha-tocopherol contents than steaks from steers fed the CON diet. Immediately following irradiation, steaks that had been irradiated had lower (P < 0.05) L* values regardless of diet. Irradiated steaks, regardless of diet, had lower a* (P < 0.05) and b* (P < 0.01) values than nonirradiated steaks at all aging times. Carbonyl concentration was higher (P < 0.05) in proteins from irradiated steaks compared to nonirradiated steaks at 0, 1, 3, and 7 d postirradiation. Immunoblot analysis showed that vitamin E supplementation decreased the number and extent of oxidized sarcoplasmic proteins. Protein carbonyl content was positively correlated with Warner-Bratzler shear force values. These results indicate that increased oxidation of muscle proteins early postmortem could have negative effects on fresh meat color and tenderness.     

Nutritional quality of extruded kidney bean (Phaseolus vulgaris L. var. Pinto) and its effects on growth and skeletal muscle nitrogen fractions in rats

The influence of extrusion cooking on the protein content, amino acid profile, and concentration of antinutritive compounds (phytic acid, condensed tannins, polyphenols, trypsin, chymotrypsin, alpha-amylase inhibitors, and hemagglutinating activity) in kidney bean seeds (Phaseolus vulgaris L. var. Pinto) was investigated. Growing male rats were fed diets based on casein containing raw or extruded kidney beans with or without methionine supplementation for 8 or 15 d. Rates of growth, food intake, and protein efficiency ratio were measured and the weight of the gastrocnemius muscle and the composition of its nitrogenous fraction was determined. Extrusion cooking reduced (P < 0.01) phytic acid, condensed tannins, and trypsin, chymotrypsin, and (alpha-amylase inhibitory activities. Furthermore, hemagglutinating activity was abolished by extrusion treatment. Protein content was not affected by this thermal treatment. Rats fed raw kidney bean lost BW rapidly and the majority died by 9 d. Pretreatment of the beans by extrusion cooking improved food intake and utilization by the rats and they gained BW. Supplementation of extruded kidney bean with methionine further enhanced (P < 0.01) food conversion efficiency and growth. However, BW gains and muscle composition still differed (P < 0.01) from those of rats fed a high-quality protein.     

Rigor temperature and meat quality characteristics of lamb longissimus muscle

The present experiment was conducted to determine the effect of muscle temperature during the prerigor and early postrigor period on meat tenderness, postmortem proteolysis, calpain system activity, water-holding capacity, and color. Lamb longissimus muscle (n = 14) from the right and left carcass sides was excised immediately after dressing, divided into an anterior and posterior sample, vacuum-packaged, and stored overnight at 5 to 35 degrees C. Further storage, up to 14 d postmortem, was at 2 degrees C. Tenderness at 1 d postmortem, tenderization during further storage, and postmortem proteolysis were negatively affected by overnight incubation above 25 degrees C. This effect could be explained by an effect of temperature on muscle contraction and activity of the calpain system. Muscle contraction was at a minimum after incubation at 15 degrees C. Water-holding capacity was negatively affected by incubation above 25 degrees C. Color scores improved with increasing incubation temperature at 1 d postmortem. However, after 14 d of postmortem storage, no differences in color scores were observed. Based on the present results and results of other groups, a temperature around 15 degrees C at the onset of rigor seems optimal to maximize tenderness without having detrimental effects on water-holding capacity or color.     

Effects of age and diet on the development of the pancreas and the synthesis and secretion of pancreatic enzymes in the young pig

Effects of age and diet composition on amylase, trypsin and chymotrypsin activities in the pancreas and intestinal contents, pancreas weights and body weights were determined from birth to 56 d. A total of 120 pigs, five to seven pigs/litter from 18 litters, were slaughtered at birth, 14, 27, 29, 31, 42 and 56 d. Litters were allotted to dietary treatments (corn-soy, A; corn-soy + 20% dried whey, B; corn-soy + 5% lard, C) and offered these diets as creep feed at 14 d. All pigs were weaned at 28 d, placed in elevated nursery pens and fed their respective diets. Total activities of amylase, trypsin and chymotrypsin in the pancreas and small intestine increased (P less than .05) with age. Both trypsin and amylase activities, measured per kilogram body weight or gram pancreas weight, were low at 29 d in the intestine and increased to 56 d. Pigs on diet B had the highest level of trypsin and chymotrypsin in the intestinal contents (P less than .05). Trypsin activity in the pancreas (units/kg body weight) was lowest (P less than .05) for pigs on diet B and highest (P less than .05) for those on diet C (units/g pancreas and units/kg body weight). Amylase activity (units/kg body weight) was lower (P less than .05) in the pancreas for pigs on diet B than for those on diets A and C. Pigs on diet A had lower (P less than .01) intestinal amylase activities than those on diets B and C. Enzyme activities in the intestinal contents and pancreas were low following weaning. In the pancreas, activities decreased at 31 d.(ABSTRACT TRUNCATED AT 250 WORDS)     

舍饲、放牧对滩羊股二头肌纤维特性及宰后成熟过程中蛋白降解的影响

试验旨在研究舍饲（concentrate feeding,CF）、放牧（pasture feeding,PF）对滩羊股二头肌肉品质、肌纤维特性、宰后成熟过程中超微结构及蛋白降解变化的影响。选取体重接近的4~5月龄滩羊公羔28只,随机分为2组,每组14个重复,每个重复1只羊,分别以舍饲、放牧方式饲养,试验期60 d。试验结束后采集股二头肌作为试验样品,并对其肉质性状、肌纤维特性及宰后成熟过程中超微结构与蛋白降解各项指标进行测定分析。结果显示,放牧组羊肉剪切力、硬度和内聚性均显著高于舍饲组（P<0.05）,弹性则显著低于舍饲组（P<0.05）;放牧组羊肉肌纤维密度和Ⅱ型肌纤维的数量比例均显著低于舍饲组（P<0.05）,Ⅰ型肌纤维的直径、横截面积和数量比例均显著高于舍饲组（P<0.05）。在宰后成熟过程中,舍饲组羊肉肌浆蛋白溶解度显著高于放牧组（P<0.05）;两组肌原纤维蛋白溶解度在宰后24 h至最低后逐渐回升,但各时间点差异均不显著（P>0.05）;肌原纤维小片化指数显著上升后趋于平稳,舍饲组增加率（50.97%）高于放牧组（41.94%）;超微结构显示,宰后肌肉肌原纤维结构松弛、裂解,Z线发生降解,肌原纤维小片化出现,舍饲组肌原纤维结构破坏程度比放牧组更严重。舍饲组肌浆蛋白变性程度小,宰后降解速率较慢,而肌原纤维蛋白降解较明显,降解产生的小分子蛋白量高于放牧组。综上所述,饲养方式改变了滩羊股二头肌纤维特性,并对宰后成熟过程中肌肉超微结构及蛋白降解产生影响,舍饲饲养使得股二头肌纤维密度增加,肌纤维直径与横截面积减小,并降低了肌肉剪切力;此外,由于Ⅱ型肌纤维比例的增加,舍饲饲养提高了肌肉宰后肌原纤维小片化指数增长率、肌浆蛋白溶解度和蛋白降解速率,使宰后成熟过程加快,改善了股二头肌肉嫩度。