Dynamical Changes of Beef Intramuscular Connective Tissue and Muscle Fiber during Heating and their Effects on Beef Shear Force

Changes of meat shear force and its characteristics during cooking have been extensively studied, but great variability existed due to the cooking method among different studies. This study was designed to focus on the dynamic changes of beef intramuscular connective tissue (IMCT) and muscle fiber during water-bath heating and their effects on beef shear force. At 4 d postmortem, beef semitendinosus muscles were divided into 11 steaks and then cooked respectively to an internal temperature of 40, 50, 55, 60, 65, 70, 75, 80, 85, and 90°C (the remainder was not cooked as control). Collagen content and its solubility, transition temperature of perimysia and endomysia, fiber diameter, and Warner–Bratzler shear force values (WBSF) were determined. The results showed that fiber diameter decreased gradually during cooking, concomitant with the increases in filtering residue and WBSF. The maximum transition temperature (T _max) of endomysial components was lower than that of perimysial components (50.2 vs. 65.2°C). Muscle fiber and IMCT (especially perimysia) shrank during cooking, resulting in the increase of WBSF when the internal temperature was lower than 75°C, but further cooking led to the disintegration of perimysial structure, lowing up the increase of WBSF between 75 and 90°C. For beef semitendinosus muscle, the internal temperature of 65°C is a critical cooking point where meat gets tougher.     

Effects of cooked temperature on pork tenderness and relationships among muscle physiology and pork quality traits in loins from Landrace and Berkshire swine

The effect of, and associations between, loin muscle morphology and pork quality indicator traits were assessed at three cooked temperatures in loin chops from 38 purebred Berkshire and 52 purebred Landrace swine. Three loin chops from each pig were randomly assigned to cooked temperature treatments of 62, 71, or 79 °C and loin tenderness was assessed as Warner–Bratzler shear force (WBSF). Cooked temperature (P < 0.001), breed (P < 0.001) and breed × cooked temperature (P < 0.001) effects influenced loin chop WBSF, whereby WBSF increased as cooked temperature increased. Chops from Landrace pigs had greater WBSF at each cooked temperature compared with chops from Berkshire pigs. Chops from Landrace pigs became less tender with increasing cooked temperature, whereas chops from Berkshire pigs became less tender only when cooked to 79 °C. In loins from Landrace pigs, Minolta a1 at 62 °C (R² = 0.07), and average muscle fiber diameter at 71 °C and 79 °C (R² = 0.07 and 0.24, respectively), contributed to WBSF variation. In contrast, for loins from Berkshire pigs, loin ultimate pH and intramuscular fat percentage accounted for 27% and 30% of the variation in WBSF at 62 °C and 71 °C, respectively, and loin ultimate pH accounted for 7% of variation in WBSF at 79 °C. Results suggest that loins from Berkshire pigs have properties that resist toughening at greater cooked temperatures and that associations between quality measures and loin tenderness differ between Landrace and Berkshire pigs.     

TENSILE PROPERTIES OF BEEF SEMITENDINOSUS MUSCLE AS AFFECTED BY HEATING RATE AND END POINT TEMPERATURE

The effects of heating rate and end point temperature on tensile properties of beef semi-tendinosus muscle were studied. Samples of meat heated in glass tubes in a water bath to simulate oven roasting at 93 °C had lower (P < 0.01) shear values than those heated to simulate oven roasting at 149 °C. Samples heated to 60 and 70°C had lower (P < 0.001) shear values than samples heated to 50°C. Instron breaking strength values varied (P < 0.001) with end point temperature, but were not significantly affected by the rate of heating. Significant (P < 0.001) interactions between the end point temperature and heating rate, as well as between the end point temperature and fiber direction suggested that Instron breaking strength measurements may be more sensitive to changes in tenderness than Warner Bratzler shear measurements.     

Pork Skin Connective Tissue Gel Utilization in Reduced-Fat Bologna

This study determined temperature (50°, 60°, 70° and 80°C) and time (0.5, 1.0, 1.5 and 2.0h) factors that enhanced the water binding of pork skin connective tissue (PCT); the functionality of added water (AW, 100–600%, w/w) PCT gels; and attributes of bologna containing 10-30% addition of 100–600% AW PCT gels. Heating (70°C) PCT increased water binding. Gels (100–600% AW) were formed by heating PCT (70°C) for 30 min. Higher AW levels increased (p < 0.05) gel moisture content, while decreasing fat, melting points, collagen content, and hardness. Addition of PCT gels in bologna decreased (p < 0.05) hardness and increased juiciness, indicating the potential of PCT gels as water binders and texture-modifying agents.     

Heat-Induced Tendering of Turban Shell (Batillus cornutus) Muscle

The foot, opercular and visceral muscles were excised from the turban shell Batillus cornutus, and their heat-induced changes in toughness and ultrastructure were compared. When heated up to 30°C, the toughness of foot muscle decreased in the upper and middle regions, but increased in the lower region. The toughness of these three regions decreased at temperatures between 50-70°C, where collagen might be denatured. Some changes in toughness were also observed in the opercular muscle by heating up to 30°C, whereas the toughness of visceral muscle remained unchanged over a wide range of temperature. Transmission electron microscopy showed that the intrinsic structure of collagen fibrils in each muscle was lost at 60°C, with partial swelling.     

Changes in the texture,microstructures, colour and volatile compounds of pork meat loins during superheated steam cooking

We evaluated changes in the texture, colour, microstructure and volatile compounds of pork loins after superheated steam (SHS) cooking at 120, 140, 160 or 180 °C for 5, 10, 15 and 20 min. Results showed that the texture changed significantly with heating temperature and time. Hardness increased significantly with increasing temperature above 140 °C. Scanning electron microscopy micrographs showed that cooked pork with SHS had more complete muscle fibre bundle structure than that of pork in HA. The L* value indicating colour was significantly increased during the early period and then decreased, whereas the a* and b* values showed a continuous increase. Ninety-five volatile compounds were identified in cooked pork from SHS by gas chromatography/mass spectrometry with solid-phase microextraction. The amount of volatile compounds increased during cooking and decreased as cooking time increased and was well retained at 140 °C. Considering those variations, samples cooked at 140 °C showed better quality attributes.     

猪肉剪切力的测定方法

为建立可靠、规范的猪肉剪切力测定方法,研究不同加热中心温度(65～80℃)、水浴温度(70～80℃)、保温时间(0～20min)及冷却温度(0～25℃)对猪背最长肌剪切力值和蒸煮损失的影响。结果表明：猪肉的剪切力和蒸煮损失随着中心温度和水浴温度的升高、保温时间的延长而增加,冷却至0～4℃的肉样其剪切力值的变异系数最小,不同的预处理方法对猪肉剪切力的影响差异显著。综合而言,猪肉剪切力测定的预处理条件应为：水浴温度72℃,加热至中心温度70℃,不保温,煮后肉样放至0～4℃冷库中过夜。     

Heating Conditions and Bread-Making Potential of Substandard Flour

ABSTRACT Heating weak bread flours (commercial cookie flour; commercial stone‐milled bread flour; Fundulea, a weak bread cultivar) at 80°C for 15 min had a positive effect on bread volume (P < 0.05). This positive effect was best seen when ascorbic acid was removed from bread formulation. Crumb springiness and fineness of grain, but not crumb hardness, were significantly improved after flour heating; cohesiveness improved with heated cookie flour (P < 0.05). After heating, flour a‐amylase content was lower; dough‐mixing stability of cookie flour doubled to 7.1 min but dropped from 18.0 to 4.8 min with standard bread flour. Heating offers possibility to upgrade substandard flour for bread‐making applications, especially in oxidant‐free dough system.     

Effect of Heat Treatments on In Vitro Digestibility of Delactosed Whey Protein as Determined by the Digestion Cell Technique

Diafiltered whey protein concentrates (WPC) were heated, in liquid form, under various conditions of time and temperature. Protein and amino acid digestibilities were determined by in vitro pepsin and pan-creatin digestion with continuous dialysis. Whey nitrogen digestibility decreased (P < 0.05) after heating at 121°C for 5000 sec. Heating WPC for 5000 set at temperatures below 121°C increased the digestibility of all amino acids except alanine and lysine at 75°C, and methionine and lysine at 100°C. In general, the longer was the heating period at 100°C or 121°C the lower was the amino acid digestibility. These results emphasized the importance of structural modifications brought about by heat treatments on protein digestibility.     

Quality Evaluation of an Ohmically Cooked Ham Product

Selected parameters (cooking loss, instrumental colour and texture and sensory quality) of a brine-injected pork muscle cooked by a novel and rapid ohmic cooking protocol were examined and compared with those obtained in conventionally cooked samples. Ohmic samples were cooked using either a low-temperature long-time (LTLT) protocol (2 min equilibration, 5 min ohmic heating to 70 °C, 8 min holding) or a high-temperature short-time (HTST) procedure (2 min equilibration, 6 min ohmic heating to 95 °C) performed within a hot air cabinet set at 80 °C (LTLT) and 100 °C (HTST). Conventional cooking (steam oven at 80 °C for 120 min) was conducted to a core temperature of 70 °C. The LTLT treatment gave a much lower cooking loss value (4–5% lower, p < 0.05) than the other treatments, though the full magnitude of this difference was not completely reflected in the proximate composition of the cooked products. Ohmically cooked ham showed a significantly (p < 0.05) lighter surface colour with Hunter L values of 65.3 (LTLT) and 63.5 (HTST) relative to the control (61.4). Texture profile analysis (TPA) indicated a significant difference (p < 0.05) in hardness (N) especially between the HTST surface (82.1 N) and the conventional centre (58.8 N). Although the ohmic cooking protocols yielded products with quite acceptable eating qualities, sensory evaluation found the overall quality of the conventionally cooked ham to be significantly (p < 0.05) superior, indicating that further optimisation of the ohmic cooking protocols would be required prior to any commercial adoption.     

Heat-Induced Textural and Histological Changes of Ordinary and Dark Muscles of Yellowfin Tuna

When a fresh specimen of yellowfin tuna Neothunnus albacora was analyzed, the cross-sectional area of ordinary (white) muscle fiber was 3.5 times larger than that of dark muscle. As heating temperature was raised, the shear force of dark muscle became progressively larger than that of ordinary muscle. Simultaneously, the A band in the ultrastructure of both muscles was stained more densely. While the Z line in I band of dark muscle still remained, that of ordinary muscle disappeared completely by heat treatment at 60°C for 30 min. Therefore, the differences in toughness change during heat treatment correlated well with that fiber sizes and ultrastructures of the two types of muscle.     

Oxidative stress-induced textural and biochemical changes of scallop Patinopecten yessoensis adductor muscle under heat treatment

In this study, the effects of heat treatment (45°C and 65°C, respectively) on the quality of Patinopecten yessoensis adductor muscle (PYAM) were investigated. Water mobility in PYAM samples was analyzed using low-field nuclear magnetic resonance. The texture of treated PYAM was analyzed using texture profile analysis. Protein degradation was characterized using SDS-PAGE. Activities of cathepsin L (CL), superoxide dismutase (T-SOD), glutathione peroxidase (GSH-Px), and catalase (CAT) were determined using chemical analysis methods. The production of free radicals was measured using electron spin resonance. It was revealed that water mobility in PYAM samples increased with the extension of heated time. Cohesiveness of PYAM was higher in samples heated at 65°C than at 45°C, while hardness showed an opposite trend, higher in the samples heated at 45°C than at 65°C. The degradation of structural proteins was more severe in the samples heated at 65°C than at 45°C, with the greater CL activity being observed. It was also found that heating caused elevation in T-SOD, GSH-Px, and CAT enzyme activities. Considering the chemical changes in the PYAM samples, contents of carbonyl and malonaldehyde increased, but sulfhydryl content decreased with heating. Level of free radicals increased significantly from 6 h on after heat treatment, with higher level at 65°C than at 45°C. These results suggested that oxidative stress is directly involved in quality changes during heat treatment of PYAM.     

Effect of tumbling time and cooking temperature on quality attributes of cooked ham

This study evaluates effect of tumbling time and cooking temperature on cooking rate, cooking loss (CL), colour, water activity and water‐holding capacity of cooked restructured ham rolls. In experiment were investigated three tumbling times (2, 4 and 6 h) at constant temperature (+4 °C) and three cooking temperatures (76, 86 and 96 °C). It was observed that CL decreased (P < 0.01) from 5.41% to 3.22% with tumbling time (2 h vs. 6 h) but increased (P < 0.01) from 2.35% to 7.25% along with cooking temperature (76 °C vs. 96 °C). In contrast, pH value increased (P < 0.01) from 6.18 to 6.24 with tumbling time (2 h vs. 6 h) but decreased (P < 0.01) from 6.22 to 6.17 along with cooking temperature (76 °C vs. 96 °C). In addition, high temperature had higher efficiency for thermal lethality than low temperature (F₀ values were 19 and 92 min at 96 and 76 °C, respectively). Intermediate tumbling (4 h) and cooking (86 °C) could be preferential.     

Protein degradation of olive flounder (Paralichthys olivaceus) muscle after postmortem superchilled and refrigerated storage

The aim of this study was to investigate the effect of superchilling at ?2°C in comparison with refrigerated storage at 4°C on the protein degradation of olive flounder (Paralichthys olivaceus) muscle. Flounder muscle softened and shear force value decreased markedly (P < 0.05) with prolonged storage time, while values of electrical conductivity, TCA-soluble peptide, free amino acids, and proteolysis index increased (P < 0.05). The changes were slowed down significantly in samples superchilled at ?2°C (P < 0.05). The fracture of muscle fibre and formation of cracks were accelerated in the samples refrigerated at 4°C, and intercellular spaces were observed after 9 days of storage. Moreover, protein bands of myosin heavy chain (MHC), actin, tropomyosin, 97 kDa, 50 ~ 60 kDa and 35 ~ 36 kDa occurred in varying degrees of degradation with storage time. The results demonstrated that significant postmortem degradation of muscle proteins occurred with extending storage time, while the changes were retarded obviously in samples during superchilled storage.     

End-point Temperature (EPT) Affects N-Acetyl-β-D-Glucosaminidase Activity in Beef, Pork and Turkey

End-point tempcraturc (EPT) affected N-acetyl-β-D-glucosaminidase (NAGasc) activity in nonfrozcn and previously frozen cores and ground sampics of beef, pork, turkey breast and ground turkey leg muscle tissue. There was little loss of NAGase activity when heating the products to 40°C; however, as EPT increased from 40–70°C, them was (Pc0.05) loss of activity. At 70°C 90% of activity was lost in beef, 98% in pork, and 93 to 98% in turkey. Inactivation temperature values, IT50, (50% inactivation) were: beef, 59.8°C; pork, 53.4°C; turkey breast, 55.6°C; and turkey leg, 56.6°C.     

Injection of marinade with actinidin increases tenderness of porcine M. biceps femoris and affects myofibrils and connective tissue

BACKGROUND: Marination of beef muscles with brine solutions containing proteolytic enzymes from fruit extracts has been shown to tenderize meat. However, the effect of marination with actinidin on tenderness of pork muscles has not been investigated. Tenderness and eating quality of porcine M. biceps femoris was investigated by Warner–Bratzler (WB) shear test and sensory evaluation after injection of brine containing up to 11 g L^?1 actinidin‐containing kiwi fruit powder and 2, 5 or 9 days of storage. RESULTS: Actinidin decreased WB shear force, increased tenderness and did not affect flavour and juiciness. Injection of 2.8 g L^?1 actinidin powder and storage for 2 days resulted in WB shear force values similar to control samples stored for 5 or 9 days. In samples injected with 10 g L^?1 actinidin powder, degradation of desmin and percentage of heat‐soluble collagen (P < 0.05) increased compared to control samples. Myofibrillar particle size tended to decrease (P < 0.1) with increasing actinidin concentration. No major changes were observed by proteome analysis. Atomic force microscopy showed actinidin‐induced damage of endomysium surrounding isolated single muscle fibres. CONCLUSION: Our results indicate that actinidin tenderizes pork M. biceps femoris by affecting both the myofibrils and connective tissue. Copyright © 2009 Society of Chemical Industry     

Effects of Heat-Stable Alakaline Protease Activity of Atlantic Menhaden (Brevootii tyrannus) on Surimi Gels

Heat stable protease isolated from the sarcoplasmic fraction of menhaden (Brevoorti tyrannus) muscle tissue was characterized as to optimum temperature and pH against casein substrate and its degradative action on actomyosin and surimi during heating. The optimum conditions for activity were 60°C at a pH of 7.5 to 8.0. Activity dropped off remarkably at temperatures below 45°C or above 70°C and when pH was below 7.0 or above 8.0. The enzyme(s) was capable of degrading actomyosin as observed by sodium dodecyl sulfate electrophoresis. This implicated a causative role for this protease system in the texture degradation observed during thermal processing of menhaden surimi at temperatures of 50-70°C.     

Properties of Dark and Light Tissue from Horse Mackerel (Trachurus murphyi)

Mechanical and physical properties of light and dark tissues from horse mackerel (Trachurus murphyi) were determined for tissue separation. Raw dark tissue was 1.8 times harder than raw white (1.4 and 0.79 kg-f/g, respectively). Hardness after heating to 20°C decreased slightly but it increased sharply to a value of about 2.4 kg-f/ g at 40°C. Tensile strength of the skin was highest at 30°C and a large reduction in the shearing force of the interfibrillar matrix (connective tissue) was also attained at that temperature. Pieces of light muscle were denser (d =1.082) than those of dark tissue (d = 1.059) and relative separation was attained based on terminal velocities. Heating at 30°C appeared adequate to implement future mechanical disruption processes.     

Ultramicroscopical Structures and Liquid Loss in Heated Cod ( Gadus morhuaL) and Salmon ( Salmo salar) Muscle

This study was performed in order to assess the effect of heating in pre- and post-rigor muscle of fed cod, wild cod and farmed salmon harvested at different times of the year. The structural changes in muscle samples pre-heated from 5 to 60°C were qualitatively evaluated using both light and transmission electron microscopy techniques. The microstructural changes are discussed in relation to the liquid loss measured by a low-speed centrifugation test. The heat-induced structural changes varied between the fish tested, reflecting different degrees of post mortem degradation prior to heating, the muscle-pH and species-specific structural properties. The fed fish, both cod and salmon, underwent the most severe structural degradation. This reflected both the low muscle pH and the more severe post mortem degradation observed in these fish prior to heating, compared with the wild cod. Heating caused extensive shrinkage of the myofibrils and hence, widened intermyofibrillar and extracellular spaces in both the fed cod and the salmon muscle. In the sample of wild cod muscle, the extracellular spaces were narrow and the myofibrils were closely packed. The difference in heat-induced liquid loss of the fed compared with the wild cod muscle coincides with their different structural features, as observed both by LM and TEM. The better liquid-holding properties of the salmon muscle than the cod muscle are attributed to the species-specific ultrastructural features as observed with TEM. In addition to the denser appearance of the salmon myofibres, it is suggested that both fat droplets and aggregated sarcoplasmic proteins filling the intermyofibrillar and extracellular spaces are important in preventing release of liquid upon heating.     

Oxidative Effects of Meat Grinder Wear on Lipids and Myoglobin in Commercial Fresh Pork Sausage

Pork ground before and after the replacement of worn meat grinder plates and knives was formulated as commercial fresh pork sausage containing antioxidants and processed into 454-g chubs. The sausage was frozen at ^?15°C for 4, 8, 12, and 16 wk and monitored for oxidation after 1 day, 2 wk and 3 wk of postfrozen refrigeration at 1°C. Estimated average grinder metal in sausage was 136 ppb. Meat temperature rise during grinding was higher (P<0.05) with the worn hardware (2.3°C vs 1.6°C). Hunter “a” values were greater (P<0.05) with the sharp than with the worn equipment. 2-Thiobarbituric acid (TBA) numbers did not differ with equipment state of wear. Significant correlations (P<0.05) indicated in inverse relationship between the oxidation of lipids and myoglobin.