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
Filter
  • Lipid oxidation  (2)
  • Hypervalent myoglobin  (1)
  • Key words Flavonoids  (1)
  • 1
    ISSN: 1438-2385
    Keywords: Key words High pressure ; Lipid oxidation ; Chicken meat ; Metmyoglobin ; Non-heme iron
    Source: Springer Online Journal Archives 1860-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract  The oxidative stability of chicken breast muscle subjected to high-pressure treatment at 300, 400, 500, 600, 700 or 800 MPa for 5 min or 10 min, or to heat treatment (80  °C for 10 min) and subsequent storage at 5  °C was evaluated over a 2-week period. Lipid oxidation in pressure-treated chicken breast muscle monitored as formation of thiobarbituric acid reactive substances depended to a high degree on the working pressure and less on the pressurizing time. The pressure treatment at 800 MPa for 10 min was found to enhance lipid oxidation to the same extent as the heat treatment. Pressure treatment at 600 MPa and 700 MPa resulted in less oxidation. Chicken breast muscle exposed to pressure at or below 500 MPa showed no indication of rancidity, similar to what was found for untreated meat during chill storage; accordingly 500 MPa is a critical pressure for pressure treatment of chicken breast muscle. Analysis of non-heme iron in pressure-treated chicken breast muscle revealed that the notable increase in lipid oxidation caused by high pressure above 500 MPa did not result from the release of iron ions during high-pressure treatment. Furthermore, no influence of high-pressure treatment on the catalytic activity of metmyoglobin on lipid oxidation was observed in a model system, and it is concluded that increased lipid oxidation is probably related to membrane damage.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
  • 2
    ISSN: 1438-2385
    Keywords: Key words Flavonoids ; Radicals ; Electron spin resonance ; Oxygen consumption ; Antioxidants
    Source: Springer Online Journal Archives 1860-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract The rate of scavenging of peroxyl radicals and of diphenylpicrylhydrazyl radicals by flavanones, flavones, flavanols and flavonols commonly occurring in foods was found, when determined by ESR spin trapping and by stopped-flow spectroscopy, respectively, to be the highest for the most reducing of the flavonoids. Among 12 flavonoids investigated a threshold potential of approximately +0.4 V seems to exist, above which the flavonoids become ineffective radical scavengers, as determined by ESR spectroscopy using 5,5-dimethyl-1-pyrroline-N-oxide as spin trap. Scavenging of diphenylpicrylhydrazyl radicals showed (pseudo) first order kinetics for excess of flavonoids, and the reaction half-life could also be determined for the less effective flavonoids. For kaempferol and eriodictyol, flavonoids with very similar reduction potentials for their phenoxyl radicals, rate constants for the bimolecular scavenging could be determined in methanol and had the value (7.0 ±0.7)×102 s−1 M−1 and 33±1 s−1 M−1 at 25°C, respectively, showing that other factors than the driving force, such as hydrophilic/lipophilic balance are important, as was further confirmed in an oxygen consumption assay based on a linoleic acid emulsion, where decreasing antioxidant efficiency followed the order: (+)-catechin〉(±)-taxifolin≥luteolin〉kaempferol〉quercetin〉〉naringenin.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
  • 3
    Electronic Resource
    Electronic Resource
    Springer
    Zeitschrift für Lebensmittel-Untersuchung und -Forschung 205 (1997), S. 11-13 
    ISSN: 1431-4630
    Keywords: Key words High-pressure treatment ; Lipid oxidation ; Chill storage ; Turkey thigh muscle
    Source: Springer Online Journal Archives 1860-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract  Formation of secondary lipid oxidation products during chill storage of vacuum-packed (99% vacuum), pressure-treated turkey thigh muscle was found to depend on working pressure (pressure range up to 500 MPa at 10°C) and to a lesser degree on pressurization time (10 and 30 min). Pressure treatment at 400 MPa and lower pressures for 30 min (and for 10 min) resulted in less formation of thiobarbituric-acid-reactive substances (TBARS) during 6 days of storage at 5°C compared to heat treatment at 100°C for 10 min, while pressure treatment at 500 MPa for 30 min gave similar development of TBARS as did the heat treatment. The formation of TBARS during storage at 5°C was found to depend exponentially on the pressure used for treatment at both 10 min and 30 min, and apparent volumes of activation are proposed as a parameter for quantification of the effects of pressure on lipid oxidation in meat during subsequent storage.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
  • 4
    Electronic Resource
    Electronic Resource
    Springer
    Zeitschrift für Lebensmittel-Untersuchung und -Forschung 206 (1998), S. 199-202 
    ISSN: 1431-4630
    Keywords: Key words Proteolytic enzymes ; Oxidative damage ; Hypervalent myoglobin
    Source: Springer Online Journal Archives 1860-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract  Ferrylmyoglobin [MbFe(IV)=O], formed by activation of metmyoglobin by hydrogen peroxide, inactivates the cysteine proteinases papain (EC 3.4.22.2) and ficin (EC 3.4.22.3) more efficiently than hydrogen peroxide, but less efficiently than hydroxyl radicals as generated by peroxynitrite or the Fenton reaction. Metmyoglobin and oxymyoglobin could not inactivate papain and ficin. Oxidation of papain and ficin by ferrylmyoglobin occurs in enzyme/haem-protein complexes with binding constants of approximately 105 l · mol–1; inactivation of proteolysis by papain plateaus at neutral pH to about 1/3 whereas the inactivation under acidic conditions was larger.
    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...