Results 201 to 210 of about 18,427 (259)

Effects of different protein cross-linking degrees on physicochemical and subsequent thermal gelling properties of silver carp myofibrillar proteins sol subjected to freeze-thaw cycles. [PDF]

Food Chem X
Ding Y, Feng R, Zhu Z, Xu J, Xu Y.
europepmc   +1 more source

Contribution of Sarcoplasmic Proteins to Myofibrillar Proteins Gelation

Journal of Food Science, 2012
Abstract:  Surimi, a refined protein extract, is produced by solubilizing myofibrillar proteins during the comminuting and salting stages of manufacturing. The resulting paste gels on heating to produce kamaboko or a range of analog shellfish such as crab claw, filament sticks, fish mushroom, and so on.
Ali, Jafarpour, Elisabeth M, Gorczyca
openaire   +3 more sources

Some of the next articles are maybe not open access.

Related searches:

Oxidation affects pH buffering capacity of myofibrillar proteins via modification of histidine residue and structure of myofibrillar proteins

International Journal of Biological Macromolecules
The pH buffering capacity is an important functionality of muscle proteins, and muscle foods are susceptible to being oxidized during storage and processing. In order to study the effect of oxidation on the pH buffering capacity of myofibrillar proteins, myofibrils extracted from snakehead fish (Channa argus) were oxidized with H2O2.
Hui Hong, Yueyue Liu, Abdul Razak Monto   +2 more
exaly   +3 more sources

Phosphorylation of the Myofibrillar Proteins

Annual Review of Physiology, 1980
In muscle, protein phosphorylation takes place in both the sarcoplasm and the myofibrils. This review deals only with those myofibrillar proteins that can be phosphorylated-i.e. myosin light chain and in a few cases the heavy chain, the inhibitory and tropomyosin-binding subunits of troponin, and tropomyosin.
M, Bárány, K, Bárány
openaire   +2 more sources

Note on differentiation of myofibrillar proteins

Journal of the Science of Food and Agriculture, 1970
AbstractThe detection of qualitative differences between the myofibrillar proteins of muscles, which superficial examination would classify as similar on the basis of their ‘redness’ or ‘whiteness’, emphasises the need for more subtle criteria for understanding meat quality.
A, Champion, A L, Parsons, R A, Lawrie
openaire   +2 more sources

On cryodenaturation of chicken myofibrillar proteins

Cryobiology, 1968
Summary Myofibrillar protein preparations isolated from chicken pectoralis major containing 81 to 95% protein and 3 to 4% lipids, on dry weight basis, were used as a model system to study the nature of protein and lipid changes occurring as a result of frozen storage.
A W, Khan, E, Davidkova, L, Van den Berg
openaire   +2 more sources

Ionic Strength and Myofibrillar Protein Solubilization

Journal of Animal Science, 1987
Myofibrils from bovine longissimus muscle were obtained at 2 h postmortem and incubated in .10 to .35 M ionic strength buffers under various conditions in vitro. Increasing ionic strength or increasing the incubation time from 1 to 72 h decreased the turbidity of suspensions of myofibrils and increased myofibrillar solubilization (P less than .01 for ...
F Y, Wu, S B, Smith
openaire   +2 more sources

Interaction of Fish Myoglobin and Myofibrillar Proteins

Journal of Food Science, 2008
ABSTRACT:  Interactions between fish myoglobin (Mb) and myofibrillar proteins were investigated in a Mb‐natural actomyosin (NAM) model at 4 °C. Increases in metmyoglobin (MetMb) formation and the relative content of bound Mb were observed, as were decreases in whiteness and Ca 2+
M, Chaijan, S, Benjakul, W, Visessanguan, S, Lee, C, Faustman   +4 more
openaire   +2 more sources

Myofibrillar Proteins of Skeletal Muscle

1971
Publisher Summary Muscle is a highly integrated chemical machine. One of the most impressive aspects of this integration is the ability to increase the rate of energy utilization by approximately 2500-fold within milliseconds. This efficient transduction of chemical into mechanical energy occurs through the subtleties of the interactions of myosin ...
E J, Briskey, T, Fukazawa
openaire   +2 more sources