Library

feed icon rss

Your email was sent successfully. Check your inbox.

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

Proceed reservation?

Export
  • 11
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 43 (1978), S. 0 
    ISSN: 1750-3841
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Three commercially available brands of beef and pork frankfurters were compared by light and scanning electron microscopy for protein matrix structure and fat distribution within the sausages. One brand had a coarse protein matrix structure, large fat droplets and some large pieces of intact muscle, while a second brand had a more uniform fat and protein distribution with some visible muscle fragments present. A third brand of frank had uniformly small fat droplets evenly distributed in a protein matrix. Scanning electron micrographs show this frank to be a true meat emulsion. These observations show the wide variation between the microstructure of acceptable commercial frankfurters.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
  • 12
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 43 (1978), S. 0 
    ISSN: 1750-3841
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Notes: The purpose of the study was to determine the effects of ultrasonic treatment on muscle microstructure, breaking strength, cook yield, and protein extractability of ground cured ham rolls. A miniaturized system was designed which subjected ground ham to slow mixing and ultrasonic treatment. The samples were mixed for various times up to 2 hr, then stuffed into stoppered glass tubes for cooking in 80°C water bath. Controls were treated similarly, but without ultrasonic treatment. Results showed that ultrasound caused changes in muscle microstructure, increased breaking strength as measured in g/cm2 on an Instron Universal Testing Machine, decreased cooking loss and increased the extractability of salt-soluble protein. Ultrasound had no effect on the extractability of water-soluble protein.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
  • 13
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 43 (1978), S. 0 
    ISSN: 1750-3841
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Samples of rectus femoris were collected from cured ham muscles which had been massaged for 0, 1, 2, 4, 8 or 24 hr with 0, 1, 2, or 3% of added salt in the presence or absence of 0.5% phosphate for examination with a scanning election microscope (SEM). After several hours of massaging, fiber disruption became evident. Further massaging resulted in longitudinal disruption of the fibers. Myofibrils were observed to separate and shred from the surface of the fibers. After 24 hr of massage, all treatments showed massive fiber disruption and loss of normal structural integrity. The effects of massaging were more pronounced in the presence of salts and phosphates at all time intervals.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
  • 14
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 42 (1977), S. 0 
    ISSN: 1750-3841
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Suspensions of myosin, actomyosin and sarcoplasmic protein, isolated from beef semitendinosus muscle, were prepared at several protein concentrations and with various amounts of added sodium chloride up to 1.4M. An aliquot from each suspension was pressed between two pieces of muscle of fixed cross-sectional area and cooked. Binding strength was estimated from the force required to separate the meat pieces. At salt concentrations up to 1M the binding strength of myosin was superior to that of actomyosin (P = 0.05 – 0.001), and that of sarcoplasmic protein was too low to be measured by the techniques that were used. However in the absence of added sodium chloride, a mixture of sarcoplasmic protein and myosin had greatest (P = 0.05) binding strength.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
  • 15
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 40 (1975), S. 0 
    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
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
  • 16
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 44 (1979), S. 0 
    ISSN: 1750-3841
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Combination hams were prepared by injecting excised porcine muscles with a brine containing solubilized isolated soy protein. The microstructure of the muscle in the combination ham was compared to that of a water added ham to determine the location of the isolated soy protein. The effect of massaging on the location of the isolated soy protein was also studied. The results showed that the isolated soy protein occupied primarily perimysial spaces and the massaging acts to incorporate these proteins into the endomysial spaces and mix them with extracted myofibrillar proteins. The isolated soy protein appeared to enhance myofibrillar protein extraction by binding water, thus increasing the effective concentration of salt and phosphate. Scanning electron microscopy showed that the gel formed by the isolated soy protein possessed a denser structure than the gel formed by a crude myosin preparation. The gel formed by a mixture of myosin and isolated soy protein possessed a structure more comparable to the structure of the crude myosin gel.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
  • 17
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 44 (1979), S. 0 
    ISSN: 1750-3841
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Investigations on the binding abilities of some nonmeat proteins showed that those studied were inferior to the binding ability previously reported for myosin. Their binding abilities in the presence of 8% salt and 2% sodium tripolyphosphate were ranked from highest to lowest as wheat gluten, egg white, corn gluten, calcium reduced dried skim milk, bovine blood plasma, isolated soy protein and sodium caseinate. Structures of gels formed by these proteins and mixtures of them with crude myosin showed that a three dimensional network of protein fibers is not indicative of good binding ability. The types of molecular interactions stabilizing their gel structures are thought to be more important.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
  • 18
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 44 (1979), S. 0 
    ISSN: 1750-3841
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Combination hams were prepared by injecting deboned ham muscles with brines containing solubilized isolated soy protein. The muscles were injected to levels of 30%, 45% or 60%, and then subjected to either 0 hr or 18 hr of intermittent massaging. The effects of massaging, isolated soy protein, and the level of injection on binding strengths, cooking yields and taste-panel scores were examined. Massaging and isolated soy protein improved both binding strength and cooking yield. increasing levels of injection decreased binding strength and cooking yield. Massaging improved uniformity, textural appeal, and overall acceptability, but decreased tenderness and did not affect juiciness and flavor.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
  • 19
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 44 (1979), S. 0 
    ISSN: 1750-3841
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Notes: A model system designed for the Instron Universal Testing Machine to record the peak force required to separate pieces of meat at a binding junction was used to measure the ability of various muscle protein fractions to bond meat pieces. The binding abilities of crude myosin preparations were found to be significantly greater than the binding ability of either a muscle homogenate free of fat and sarcoplasmic proteins, a total muscle homogenate or a nonprotein control consisting of salt, phosphate and water. Crude myosin fractions extracted from pre- and post-rigor bovine muscle over short and long extraction times with three extracting solutions, Guba-Straub, Hasselbach-Schneider and Weber-Edsall, were measured for binding ability, yield and mole ratio of myosin to actin by scanning SDS-PAGE gels. Results showed that the Hasselbach-Schneider myosin was superior to the Guba-Straub and Weber-Edsall myosins in both binding ability and yield. Comparisons of mole ratios with binding abilities showed that when the same extracting conditions were present the higher proportion of myosin resulted in a higher binding ability. However, when different extracting conditions were present, the higher proportion of myosin did not always give a higher binding ability. These results imply that ionic interactions are inculpated in the binding phenomenon.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
  • 20
    ISSN: 1750-3841
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Samples of the tacky exudate formed on meat surfaces as a result of salt, phosphate and massaging were removed at intervals during 24 hr of massaging, and analyzed by SDS polyacrylamide gel electrophoresis to determine the relative percentage of various myofibrillar proteins present. The results showed that phosphate exerts the greatest effect on the relative percentages of actin, myosin and tropomyosin, and its action occurs primarily on meat surfaces before the massaging process is initiated. The massaging process involves great degrees of tissue destruction at the cellular level which aids in the extraction, solubilization, concentration and distribution of the major myofibrillar proteins on surfaces and in interiors of muscle chunks, which is beneficial in the improvement of binding.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...