Library

X
feed icon rss

Your email was sent successfully. Check your inbox.

An error occurred while sending the email. Please try again.

Proceed reservation?

Export
  • 1
    Electronic Resource
    Electronic Resource
    EFFECT OF POSTMORTEM CONDITIONS ON CERTAIN CHEMICAL, MORPHOLOGICAL AND ORGANOLEPTIC PROPERTIES OF BOVINE MUSCLE (1973)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 38 (1973), S. 0 
    Details
    ISSN: 1750-3841
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Paired sides from U.S. Choice grade beef were aged immediately after slaughter at 2 and 16°C. Samples were removed from longissimus and semitendinosus at slaughter and at 1, 3 and 7 days postmortem for ATPase assay, phase microscopy, shear and organoleptic evaluation. Rib steaks from sides aged at 16°C for 1-day postmortem were as tender as steaks from sides aged at 2°C for 7 days postmortem. Flavor development of rib steaks also was more rapid at 16°C than at 2°C. Tenderness of semitendinosus steaks was improved by aging sides at 16°C; the difference in improvement of tenderness of semitendinosus, however, was not as great between 2°nd 16° as it was for rib steaks. Ca++, Mg++ and EGTA-modified ATPase activity of myofibrils from both muscles increased with postmortem time, with myofibrils from muscles held at 16°C having slightly higher ATPase activity than myofibrils from muscles held at 2° Increased EGTA-modified ATPase activity was indicative of loss of calcium sensitivity of the myofibril. Sarcomeres of myofibrils from longissimus were longer at 1-day postmortem than those from at-death longissimus and they remained essentially unchanged during the remainder of postmortem aging; however, tenderness improved at 16°C for 1 day and at 2°C for 3 days. Also greater fragmentation of myofibrils from longissimus postmortem aged at 16°C for 1 day and at 2°C for 3 days was observed, suggesting that the rate of myofibril fragmentation is an important factor in tenderization.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1973.tb02846.x
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 2
    Electronic Resource
    Electronic Resource
    PALATABILITY AND VISUAL ACCEPTANCE OF DARK, NORMAL AND PALE COLORED PORCINE M. LONGISSIMUS (1976)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 41 (1976), S. 0 
    Details
    ISSN: 1750-3841
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Pork loins from carcasses weighing 68–75 kg were compared for quality characteristics. A total of 120 loins, with equal numbers of pale and watery, normal and dark colored loins, were evaluated. Pale chops had a significantly higher cooking loss than normal or dark colored chops. The consumer panel scored the pale chops significantly lower in organoleptic acceptability than normal or dark chops. The trained panel gave a similar rating for the organoleptic evaluation. When the consumer panel selected pork chops from a retail display case, the normal colored chops received the highest rating and the pale, watery chops the lowest. The pale chops were the most unstable and developed a greenish-gray cast after 2–3 days' storage. The normal colored chops had significantly more intramuscular fat and less protein than either pale or dark chops.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1976.tb00685.x
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 3
    Electronic Resource
    Electronic Resource
    MICROBIOLOGY OF PALE, DARK AND NORMAL PORK (1976)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 41 (1976), S. 0 
    Details
    ISSN: 1750-3841
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Pale, soft, exudative (PSE), dark cutting, and normal colored pork were compared to determine differences in susceptibility to microbial growth. Chops were packaged and stored under simulated retail conditions. Color, marbling, pH, numbers of total aerobic mesophiles, psychrotrophs, proteolytic and lipolytic bacteria and fluorescent Pseudomonas and incidence of Salmonella and coagulase positive Staphylococcus were recorded for pork chops as storage time progressed. Data were statistically analyzed. Differences in pH between PSE and normal chops, after aging, were significant, and dark chops had significantly higher pH values than normal chops. Development of microorganisms during storage was influenced by pH. Most rapid growth of organisms occurred on dark meat and slowest bacterial growth on PSE pork, although exudative conditions of the latter provided the highest expressible juice. pH of the meat also seemed to have a selective action on the microflora. Marbling of the meat did not influence growth of lipslytic bacteria. Relevance of various stages of processing as sources of contamination for the meat is discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1976.tb01114.x
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 4
    Electronic Resource
    Electronic Resource
    EFFECT OF POSTMORTEM STORAGE AND CALCIUM ACTIVATED FACTOR ON THE MYOFIBRILLAR PROTEINS OF BOVINE SKELETAL MUSCLE (1977)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 42 (1977), S. 0 
    Details
    ISSN: 1750-3841
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Myofibrils isolated from bovine longissimus (L), semitendinosus (ST) and psoas major (PM) muscles at-death and at 1, 2, 3, 6 and 10 days postmortem storage (2 and 25°C) were analyzed with sodium dodecyl sulfate (SDS) polyacrylamide gel electrophoresis. One of the subunits of troponin, troponin T, disappeared from L and ST muscle during postmortem storage at 25°C, and concurrently a 30,000 dalton component appeared. Storage of muscles at 25°C accelerated these changes in myofibrils from L and ST muscles, but SDS polyacrylamide gels of PM muscle changed little during storage at either 2 or 25°C. Crude preparations of a Ca2+-activated factor (CAF) were isolated from bovine L, ST and PM muscles. Total CAF activity was high and similar in L and ST muscles, but PM muscle contained less than half the total CAF activity of L and ST muscles. Incubation of purified CAF with myofibrils isolated from at-death muscle caused Z-disk degradation and disappearance of troponin T and the simulataneous appearance of a 30,000 dalton component. That incubation of purified CAF with purified troponin caused degradation of troponin-T to a 30,000-dalton component indicates that the 30,000-dalton component in whole myotibrils originates from troponin-T. The effects of CAF on Z-disk and troponin-T degradation and the relative total activity of CAF in L, ST and PM muscles are similar to the effects of postmortem storage in myofibril fragmentation, myotibrillar protein degradation and WB shear force values. These parallel effects indicate that the limited and. specific proteolysis of myofibrillar proteins is caused by a Ca2+-activated factor endogenous to the muscle cell.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1977.tb01233.x
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 5
    Electronic Resource
    Electronic Resource
    SCANNING ELECTRON MICROSCOPY OF BOVINE MUSCLE: EFFECT OF HEATING ON ULTRASTRUCTURE (1976)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 41 (1976), S. 0 
    Details
    ISSN: 1750-3841
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Notes: SEM was used to determine the effect of postmortem aging (unheated) and cooking (heated to internal temperatures of 60, 70 and 80°C by broiling) on the ultrastructural characteristics of bovine longissimus and psoas major muscles. Micrographs from postmortem aged (unheated) muscle clearly showed the fibrillar and connective tissue structures of muscle. Progressive changes with increased temperature were observed in endomisial sheath swelling, collagen fiber disintegration and myo-fibril fragmentation, coagulation and shrinkage. Specifically, after heating to 70°C, banding patterns and myofibril fragmentation at Z-disks were clearly evident. Degradation of collagen fibers in the perimysium was initiated at 70°C and intense disintegration was observed at 80°C. Changes observed in psoas major were different from those in the longissimus in that intact myofibrils and tubules were observed in both the heated and unheated samples. This may be due to the “loose” packing of myofibrils unique to psoas major muscle. Furthermore, less shrinkage and coagulation of myofilaments in the A band region and wider I band regions were noted. These observations of looser packing of myoflbrils, thinner myotibril threads and wider I band regions offer additional evidence as to why steaks from psoas major muscle are more tender than those from longissimus muscle.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1976.tb01193.x
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 6
    Electronic Resource
    Electronic Resource
    RELATIONSHIP OF TENDERNESS MEASUREMENTS MADE BY THE ARMOUR TENDEROMETER TO CERTAIN OBJECTIVE, SUBJECTIVE AND ORGANOLEPTIC PROPERTIES OF BOVINE MUSCLE (1973)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 38 (1973), S. 0 
    Details
    ISSN: 1750-3841
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1973.tb07241.x
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 7
    Electronic Resource
    Electronic Resource
    RELATIONSHIP OF USDA MARBLING GROUPS TO PALATABILITY OF COOKED BEEF (1985)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food quality 7 (1985), S. 0 
    Details
    ISSN: 1745-4557
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: As marbling increased from“practically devoid” to“moderately abundant”, loin steaks were more palatable (P〈0.05) about 2/3 of the time, round steaks were more palatable (P〈0.05) about 1/8 of the time, and loin steaks were more likely to be assigned high (≥6.00) panel ratings and to have low (≤3.63 kg) shear values. However, increases in marbling from“slight” to“moderately abundant” (A maturity) and from“small” to“moderately abundant” (A+B maturity) had little or no efect on percentage incidence of loin or round steaks with panel ratings ≤2.99 or ≥4.00, or with shear values ≥6.35 kg or ≤4.99 kg. Differences in marbling explained about 33% (loin) and 7% (top round) of the variation in overall palatability ratings in A, B, C, and A+B maturity carcasses.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1745-4557.1985.tb01061.x
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 8
    Electronic Resource
    Electronic Resource
    CONTINUATION OF SYMPOSIUM: FUNDAMENTAL PROPERTIES OF MUSCLE PROTEINS IMPORTANT IN MEAT SCIENCE: ROLE OF NEW CYTOSKELETAL ELEMENTS IN MAINTENANCE OF MUSCLE INTEGRITY (1984)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food biochemistry 8 (1984), S. 0 
    Details
    ISSN: 1745-4514
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: Evidence suggests that desmin, titin and nebulin, three recently discovered proteins, have cytoskeletal roles in muscle cells. The three proteins have been purified from mature skeletal muscle and partially characterized. Properties of the three proteins are described, with special regard to their probable roles and importance in maintaining muscle cell integrity. Results will be shown that demonstrate ability of purified desmin to self-assemble into synthetic 10-nm (intermediate) diameter filaments. Taken together with immunoelectron microscope results (Richardson et al. 1981), it is evident that desmin is the major component of 10-nm filaments of mature skeletal muscle cells and that the desmin filaments link adjacent myofibrils at their Z-line levels and seemingly tie the myofibrils into the cell cyto-skeleton. Desmin is degraded at about the same rate as is the highly susceptible troponin-T in bovine semitendinosus muscle postmortem. Alterations in desmin and other recently discovered cytoskeletal proteins would be expected to disrupt muscle cell integrity and to have marked effects on properties of muscle important to its use as food.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1745-4514.1984.tb00310.x
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 9
    Electronic Resource
    Electronic Resource
    Physicochemical Properties and Partial Purification of Porcine Muscle Cathepsin (1966)
    s.l. : American Chemical Society
    Journal of agricultural and food chemistry 14 (1966), S. 232-237 
    Details
    ISSN: 1520-5118
    Source: ACS Legacy Archives
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/jf60145a010
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 10
    Electronic Resource
    Electronic Resource
    EFFECTS OF POSTMORTEM STORAGE CONDITIONS ON MYOFIBRILLAR ATPase ACTIVITY OF PORCINE RED AND WHITE SEMITENDINOSUS MUSCLE (1978)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 43 (1978), S. 0 
    Details
    ISSN: 1750-3841
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Notes: This study was carried out to determine the effects of postmortem storage time, temperature and pH on myofibrillar proteins of red and white muscle. Myofibrils were isolated from (1) the red and white portion of semitendinosus muscle postmortem stored at 2°C and (2) at-death red and white portions and suspended and stored in unbuffered 0.15M KC1 at 2°C and in buffered 0.15M KC1 (pH 5.5 and 7.0) at 2° and 25°C. To determine the effect of storage conditions on myofibrillar proteins, ATPase activity was assayed at different ionic strengths and with different modifiers. Assays of myofibril ATPase activity from postmortem muscle showed that (1) myofibrils from the white portion had greater ATPase activity than those from the red portion, (2) Ca2+-modified activity from both portions increased and (3) Mg2+ -EGTA-modified activity increased from the white portion, but remained unchanged from the red portion, during postmortem storage. These changes could be due to modifications of the regulatory protein components of muscle by calcium-activated factor activity. For those myofibrils isolated from at-death muscle and incubated under simulated storage conditions, a precipitous decrease occurred in Ca2+ -and Mg2+-(low ionic strength) and Ca2+- and EDTA-(high ionic strength) modified ATPase activity of myofibrils stored in 0.15M KC1, pH 5.5, at 25°C. Otherwise, little change occurred in these activities under other simulated conditions of storage (i.e., 2°, pH 5.5 and 7.0; and 25°, pH 7.0) with the exception that EGTA modified activity (indicates loss of Ca2+ sensitivity) increased from the white portion at 25° and 2°C, pH 7.0, and from the red portion at 25°C, pH 7.0. Hence, a high storage temperature of 25°C has more detrimental effect on the integrity of myofibrillar proteins, as measured by changes in ATPase activity, than does a low pH of 5.5, or fiber type.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1978.tb09726.x
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...