Results 151 to 160 of about 16,198 (215)

Advances in Research on the Improvement of Low-Salt Meat Product Through Ultrasound Technology: Quality, Myofibrillar Proteins, and Gelation Properties. [PDF]

Molecules
Guo X, Xu S, Fu C, Peng Z.
europepmc   +1 more source

Effects of high-intensity ultrasound on physicochemical and gel properties of myofibrillar proteins from the bay scallop (Argopecten irradians). [PDF]

Ultrason Sonochem
Liu B, Wu Y, Liang QY, Zheng H.
europepmc   +1 more source

Retrograded Resistant Starch Improves Emulsion Stability and Emulsion Gel Properties Stabilized by Myofibrillar Proteins Without Degrading In Vitro Protein Digestibility. [PDF]

Foods
Chen J, Hu F, Guo J, Zhang W, Wu Z.
europepmc   +1 more source

Insight into the effects of ultrasound-assisted intermittent tumbling on the gelation properties of myofibrillar proteins: Conformational modifications, intermolecular interactions, rheological properties and microstructure. [PDF]

Ultrason Sonochem
Zhang R, Zhou L, Zhang W.
europepmc   +1 more source

Insighting the effect of ultrasound-assisted polyphenol non-covalent binding on the functional properties of myofibrillar proteins from golden threadfin (Nemipterus virgatus). [PDF]

Ultrason Sonochem
Wei X, Zhou C, Luo D, Jiang G, Zhao Z, Wang W, Hong P, Dou Z.   +7 more
europepmc   +1 more source

Uncovering the rheological properties basis for freeze drying treatment-induced improvement in the solubility of myofibrillar proteins. [PDF]

Curr Res Food Sci
Yang H, Chen Z, Wang H, Jin D, Wang X, Wang F, Cen X, Liu J, Shen Q.   +8 more
europepmc   +1 more source

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

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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.
Ruichang Gao, Yulong Bao, Hui Hong
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