rdf-syntax-grammar
mods:
  schema location: http://www.loc.gov/mods/v3 http://www.loc.gov/standards/mods/v3/mods-3-2.xsd
  title info:
    title: Lactate dehydrogenase detection immunoassay in roast beef
  name:
    name part: Morris, Craig Allen.
    role:
      role term: creator
  type of resource: text
  genre: bibliography
  origin info:
    place:
      place term: xx
    date issued: 1995
    issuance: monographic
  language:
    language term: eng
  physical description:
    form: print
    extent: xi, 134 leaves : illustrations ; 28 cm.
  abstract: Recent outbreaks of foodborne illness linked to undercooked meats have raised concerns about the safety of meat products. Currently, USDAFSIS requires minimum cooking of beef roasts to an instantaneous internal temperature of 62.8'C. Development of rapid and accurate techniques to assess if the USDA required heating endpoint temperature had been achieved would enable regulators and quality control personnel to verify the safety of products while ensuring consumer confidence. The objective of this experiment was to determine if a test capable of determining if minimum safe endpoint cooking temperatures had been achieved in beef roasts. Previous research showed lactate dehydrogenase isoenzyme 5 (LDH5) to lose enzymatic activity near 63'C while SDS-PAGE results of beef Semitendinosus muscles (n = 3) cooked to 55, 60, 65, 70, 75, 80, and 85'C showed loss of LDH5 banding between 60 and 65'C. LDH5 polyclonal antibodies were raised in rabbits and immunoblot analysis performed on incrementally heated model roasts. Integrated intensities of immunoblot results revealed a loss of antigenicity between 55 and 65'C (P < .05). The effects of salt and phosphate ingredients in beef roast models were investigated. Model beef Semitendinosus roasts (n = 120) were injected with a 10% brine of either 0% Na5P3010 (P) and 0% NaCl (S), O%P 1%S, O%P 2%S, O%P 3%S, .5%P O%S, .5%P 1%S, .5%P 2%S, or .5%P 3%S. Roasts then were left raw or cooked to 60, 62, 64, or 66'C. Crude protein, pH, extractable protein, SDS-PAGE banding intensities, and immunoblot banding intensities were determined. There were no (P > .05) interactions between cooking and brine ingredient on crude protein content. Cooking and addition of sodium tripolyphosphate increased (P < .05) pH of roasts. Protein concentration in extracts from roasts decreased with heating and addition of S, but increased with addition of P (P < .05). Integrated intensities of SDS-PAGE and immunoblot results indicated that at the lower level of P and …
  note: by Craig Allen Morris.
  note: "Major Subject: Animal Science."
  note: Library's copy imperfect : page 135, vita lacking.
  note: Issued also on microfiche from University Microfilms Inc.
  note: Includes bibliographical references.
  note: Ph. D. Texas A&M University 1995.
  subject:
    topic: Major animal science
  identifier: 96-15850 UMI
  identifier: http://proxy.library.tamu.edu/login
  related item:
    location:
      url: http://proxy.library.tamu.edu/login
  record info:
    record content source: TXA
    record creation date: 961011
    record change date: 20190325093225.0
    record identifier: in00001322251