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Digitale Medien

Effect of frozen storage on protein denaturation in bovine muscle. (1986)

WAGNER, J. R. ; AÑÓN, M. C.

Oxford, UK : Blackwell Publishing Ltd

International journal of food science & technology 21 (1986), S. 0

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ISSN: 1365-2621

Quelle: Blackwell Publishing Journal Backfiles 1879-2005

Thema: Werkstoffwissenschaften, Fertigungsverfahren, Fertigung

Notizen: The effect of frozen storage on the solubility, viscosity, rheological and electrophoretic behaviour of myofibrils was studied. The solubility, viscosity, swelling and thixotropic behaviour of myofibrils showed a period in which it was constant or changed slowly, and then began to decrease. The results obtained by polyacrylamide gel electrophoresis indicated that during storage the formation of aggregates occurred in addition to alteration in the actin-myosin interaction. These results were correlated with those obtained from measurements of viscosity, rheological behaviour and swelling of myofibrils in solution.

Materialart: Digitale Medien

URL: http://dx.doi.org/10.1111/j.1365-2621.1986.tb00393.x

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Digitale Medien

Effect of freezing rate on the denaturation of myofibrillar proteins (1985)

WAGNER, J. R. ; AÑON, M. C.

Oxford, UK : Blackwell Publishing Ltd

International journal of food science & technology 20 (1985), S. 0

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ISSN: 1365-2621

Quelle: Blackwell Publishing Journal Backfiles 1879-2005

Thema: Werkstoffwissenschaften, Fertigungsverfahren, Fertigung

Notizen: Freezing of bovine muscle has a denaturating effect on myofibrillar proteins, Differ-ential Scanning Calorimetry (DSC) studies of fresh and frozen muscle at different freezing rates show a decrease on denaturation enthalpies; the lower the freezing rate the greater the loss. When measuring the specific areas (ratio between each partial area in cm', and the dry weight of the sample, in mg) of the DSC thermograms, it can be observed that the area ascribed to myosin decreases with freezing, while the area corresponding to actin is not affected. These results are in agreement with the ATPase activity decreases as a consequence of freezing observing higher losses at lower freezing rates. The denaturation observed could be a result of a partial unfolding of the myosin head being more pronounced at low freezing rate.

Materialart: Digitale Medien

URL: http://dx.doi.org/10.1111/j.1365-2621.1985.tb01971.x

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Digitale Medien

Effect of frozen storage on protein denaturation in bovine muscle 1. Myofibrillar ATPase activity and differential scanning calorimetric studies (1986)

WAGNER, J. R. ; AÑON, M. C.

Oxford, UK : Blackwell Publishing Ltd

International journal of food science & technology 21 (1986), S. 0

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ISSN: 1365-2621

Quelle: Blackwell Publishing Journal Backfiles 1879-2005

Thema: Werkstoffwissenschaften, Fertigungsverfahren, Fertigung

Notizen: The effect of frozen storage on myofibrillar ATPase activity and thermal transitions in bovine muscle was investigated. Myofibrillar ATPase activity and total enthalpy of denaturation (ΔH) decreased with time of storage. The rate of decrease was lower at −20°C than at −5°C or −10°C. Differences in behaviour during storage of muscle after fast or slow freezing could be attributed to differences in ice recrystallization. The observed decreases in area of the first peak seen in the thermograms and Ca2+-myo-fibrillar ATPase activity show that the myosin head denaturated progressively during storage. The myosin tail also denaturated during storage but the thin filament remained unaltered. Kinetic analysis suggested that the denaturation of the myofibrillar proteins took place through two consecutive first order reactions; an initial rapid reaction followed by a slower one.

Materialart: Digitale Medien

URL: http://dx.doi.org/10.1111/j.1365-2621.1986.tb01925.x

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Digitale Medien

Denaturation Kinetics of Myofibrillar Proteins in Bovine Muscle (1985)

WAGNER, J. R. ; AÑON, M. C.

Oxford, UK : Blackwell Publishing Ltd

Journal of food science 50 (1985), S. 0

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ISSN: 1750-3841

Quelle: Blackwell Publishing Journal Backfiles 1879-2005

Thema: Land- und Forstwirtschaft, Gartenbau, Fischereiwirtschaft, Hauswirtschaft , Werkstoffwissenschaften, Fertigungsverfahren, Fertigung

Notizen: Differential scanning calorimetry was used to monitor the thermal denaturation kinetics of myofibrillar proteins in bovine muscle at pH 5.6. The activation energy, pre-exponential factor, rate constant and mean life time for each transition were calculated by means of a dynamic method. The kinetic values and the proposed reaction order (n= 1) were confirmed applying an isothermal method as a test. The position of the endothermal peaks proved to be pH dependent. Evidences suggest that peak III is a result of actin denaturation and possibly other thin filament proteins. Peaks I and II would represent the thermal transition of thick filaments. The number of bonds involved in each transition were estimated.

Materialart: Digitale Medien

URL: http://dx.doi.org/10.1111/j.1365-2621.1985.tb10530.x

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