ALBERT

All Library Books, journals and Electronic Records Telegrafenberg

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
Filter
  • Articles  (3)
  • Blackwell Publishing Ltd  (3)
  • International Union of Crystallography
  • MDPI Publishing
  • Molecular Diversity Preservation International (MDPI)
  • Public Library of Science
  • Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition  (3)
  • 1
    Electronic Resource
    Electronic Resource
    Quantitative Estimation of Dark Muscle Content in the Mackerel Meat Paste and its Products Using Antisera Against Myosin Light Chains (2001)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 66 (2001), 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: : Based on the high level of extractability of myosin subunits (light chains), even after prolonged heat treatment of muscle, a new method to evaluate the dark muscle content in the fish meat and products of mackerel is proposed. Tissue-specific rabbit antisera with myosin light chains (A1 from ordinary muscle and D1 from dark muscle) from mackerel Scomber japonicus were obtained. Mackerel meat paste (surimi) was dissolved in 8 M urea containing 1% SDS, and diffused on agar plates containing antiserum against A1 or D1 by single radial immunodiffusion (SRID). The results obtained showed that the area of halos formed in the plates was quite proportional to the content of dark muscle.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.2001.tb15205.x
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 2
    Electronic Resource
    Electronic Resource
    Autoxidation of Bluefin Tuna Myoglobin Associated with Freezing and Thawing (1987)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 52 (1987), 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: Bluefin tuna oxymyoglobin (oxyMb) solutions were frozen either quickly at −80°C or slowly at −2O°C, thawed, and the metmyoglobin (metMb) to total myoglobin (Mb) ratio (metMb%) determined. When quick freezing was applied, autoxidation was clearly pH-dependent, with a minimum (metMb%, 15–40) at around pH 5.9–6.3. When slowly frozen and thawed, on the other hand, tuna Mb generally showed an extremely high metMb%. Freezing and thawing partially insolubilized tuna Mb, depending upon pH. The Mb showed the minimum ratio of insolubilization at pH 6–6.3 again. Insolubilization of tuna Mb was markedly accelerated by NaCl.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1987.tb06681.x
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 3
    Electronic Resource
    Electronic Resource
    Heat-Induced Tendering of Turban Shell (Batillus cornutus) Muscle (1985)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 50 (1985), 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: 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.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1985.tb12994.x
    Location Call Number Expected 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...