Results 331 to 340 of about 7,838,731 (404)
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Physicochemical changes in Pacific whiting muscle proteins during iced storage
, 1997No changes in actomyosin Ca 2+ -, Mg 2+ -, or Mg 2+ -Ca 2+ -ATPase activities were observed during iced storage of Pacific whiting fillets, but Mg 2+ -EGTA-ATPase increased with a loss of Ca 2+ -sensitivity. Surface hydrophobicity of actomyosin increased
S. Benjakul +3 more
semanticscholar +1 more source
Micro-calpain is essential for postmortem proteolysis of muscle proteins.
Journal of Animal Science, 2006The objective of this investigation was to test the hypothesis that -calpain is largely responsible for postmortem proteolysis of muscle proteins. To accomplish this objective, we compared proteolysis of known muscle proteins in muscles of wild type and ...
G. Geesink +3 more
semanticscholar +1 more source
Journal of Agricultural and Food Chemistry, 2000
Protein hydrolysates (5, 10, and 15% degrees of hydrolysis) were made from minced salmon muscle treated with one of four alkaline proteases (Alcalase 2.4L, Flavourzyme 1000L, Corolase PN-L, and Corolase 7089) or endogenous digestive proteases.
H. Kristinsson, B. Rasco
semanticscholar +1 more source
Protein hydrolysates (5, 10, and 15% degrees of hydrolysis) were made from minced salmon muscle treated with one of four alkaline proteases (Alcalase 2.4L, Flavourzyme 1000L, Corolase PN-L, and Corolase 7089) or endogenous digestive proteases.
H. Kristinsson, B. Rasco
semanticscholar +1 more source
Muscle proteins — their actions and interactions
Current Opinion in Structural Biology, 1996Muscle contracts by the myosin cross-bridges "rowing' the actin filaments past the myosin filaments. In the past year many structural details of this mechanism have become clear. Structural studies indicate distinct states for myosin S1 in the rigor, ATP or "down' conformation and in the products complex (ADP.Pi) or "up' to state.
openaire +4 more sources
Effects of alkali and acid solubilization on gelation characteristics of rockfish muscle proteins
, 2006: Solubility of rockfish whole muscle and actomyosin was minimum at pH 5 and gradually increased as the pH was shifted to acidic or alkaline pH. Acidic and alkaline solubilization was followed by isoelectric precipitation induced degradation of myosin ...
J. Yongsawatdigul, J. W. Park
semanticscholar +1 more source
, 2006
: Extraction and recovery of fish muscle proteins with the pH-shift process was investigated for Atlantic croaker and compared to a laboratory scale surimi process. The acid-aided process led to higher recoveries (P < 0.05) than the alkali-aided process,
H. Kristinsson, Yong Liang
semanticscholar +1 more source
: Extraction and recovery of fish muscle proteins with the pH-shift process was investigated for Atlantic croaker and compared to a laboratory scale surimi process. The acid-aided process led to higher recoveries (P < 0.05) than the alkali-aided process,
H. Kristinsson, Yong Liang
semanticscholar +1 more source
Heat‐induced Gelation Properties of Salt‐Soluble Muscle Proteins as Affected by Non‐Meat Proteins
, 2006Addition of whey protein concentrate (WPC), whey protein isolate (WPI) or soy protein isolate (SPI) to salt-soluble muscle proteins (SSP) decreased the gel strength. WPI:SSP gels had higher water-holding capacity than SSP, SSP:WPC or SSP:SPI gels. Myosin
A. McCord, A. Smyth, E. O’Neill
semanticscholar +1 more source
Solitary excitations in muscle proteins.
Physical review. A, General physics, 1985In order to elucidate the molecular mechanism of muscle contraction, we propose a theory of nonlinear lattice solitons in muscle proteins. In a superstructure of myosin molecules, there are two ..cap alpha..-helical polypeptides.
Yomosa
semanticscholar +1 more source
2004
Proteins within the muscle matrix play an essential role in the quality attributes of cooked meat, such as tenderness, juiciness, and mouthfeel. In processed meats, salt- and phosphate-extracted myofibrillar proteins, which are superior gelling, fat-emulsifying, and water-binding agents, are largely responsible for the product textural properties.
openaire +3 more sources
Proteins within the muscle matrix play an essential role in the quality attributes of cooked meat, such as tenderness, juiciness, and mouthfeel. In processed meats, salt- and phosphate-extracted myofibrillar proteins, which are superior gelling, fat-emulsifying, and water-binding agents, are largely responsible for the product textural properties.
openaire +3 more sources
Reexamination of the conformation of muscle proteins by optical activity.
Biochemistry, 1976The circular dichroism and optical rotatory dispersion of muscle proteins are reexamined. By the method of Chen et al. (Chen, Y.H., Yang, J.T., and Chau, K.H.
C. S. Wu, J. T. Yang
semanticscholar +1 more source