Effect of sarcoplasmic proteins oxidation on the gel properties of myofibrillar proteins from pork muscles

2021 ◽  
Author(s):  
Xiaolong Feng ◽  
Di Wu ◽  
Kun Yang ◽  
Limei Wang ◽  
Xian Wang ◽  
...  
Keyword(s):  
Myofibrillar Proteins ◽  
Gel Properties ◽  
Sarcoplasmic Proteins

Characterization of Muscle Sarcoplasmic and Myofibrillar Protein Hydrolysis Caused by Lactobacillus plantarum

1999 ◽  
Vol 65 (8) ◽  
pp. 3540-3546 ◽  
Author(s):  
Silvina Fadda ◽  
Yolanda Sanz ◽  
Graciela Vignolo ◽  
M.-Concepción Aristoy ◽  
Guillermo Oliver ◽  
...  
Keyword(s):  
Lactobacillus Plantarum ◽  
Myofibrillar Protein ◽  
Myofibrillar Proteins ◽  
Muscle Proteins ◽  
Whole Cells ◽  
Sarcoplasmic Proteins ◽  
Cell Extracts ◽  
Hydrophobic Nature ◽  
Hydrolysis Of

ABSTRACT Strains of Lactobacillus plantarum originally isolated from sausages were screened for proteinase and aminopeptidase activities toward synthetic substrates; on the basis of that screening,L. plantarum CRL 681 was selected for further assays on muscle proteins. The activities of whole cells, cell extracts (CE), and a combination of both on sarcoplasmic and myofibrillar protein extracts were determined by protein, peptide, and free-amino-acid analyses. Proteinase from whole cells initiated the hydrolysis of sarcoplasmic proteins. The addition of CE intensified the proteolysis. Whole cells generated hydrophilic peptides from both sarcoplasmic and myofibrillar proteins. Other peptides of a hydrophobic nature resulted from the combination of whole cells and CE. The action of both enzymatic sources on myofibrillar proteins caused maximal increases in lysine, arginine, and leucine, while the action of those on sarcoplasmic proteins mainly released alanine. In general, pronounced hydrolysis of muscle proteins required enzyme activities from whole cells in addition to those supplied by CE.

scholarly journals Protein turnover in skeletal muscle of piglets

1974 ◽  
Vol 31 (1) ◽  
pp. 35-45 ◽  
Author(s):  
H. N. Perry
Keyword(s):  
Protein Turnover ◽  
Plasma Proteins ◽  
Hind Limb ◽  
Acid Metabolism ◽  
Specific Activity ◽  
Whole Body ◽  
Myofibrillar Proteins ◽  
Sarcoplasmic Proteins ◽  
Sarcoplasmic Protein ◽  
Suckling Piglets

1. Rates of protein synthesis and catabolism were measured in longissimus dorsi and hind-limb muscles of suckling piglets.2. Half-lives for synthesis and catabolism for mixed sarcoplasmic proteins were 4.8 and 9.4 d respectively. The corresponding values for mixed myofibrillar proteins were 5.7 and 16.4 d.3. The half-lives for synthesis of sarcoplasmic proteins were significantly different from those of myofibrillar proteins and were not confounded by contamination of the sarcoplasmic protein fraction with plasma proteins of higher specific activity.4. Individual myofibrillar proteins were synthesized and catabolized at rates which were not statistically significantly different. Intramuscular connective tissue also appeared to turnover rapidly, the half-life for synthesis being 8 d and that for catabolism 20 d.5. Values obtained for the specific radioactivities of aspartate + glutamate in mixed plasma proteins support the view that, in so far as the young of animals larger in mature body size than rats or mice are concerned, muscle assumes a more important role relative to liver in regulating whole body amino acid metabolism.

Regulation of myofibrillar protein turnover during maturation in normal and undernourished rat pups

2000 ◽  
Vol 278 (4) ◽  
pp. R845-R854 ◽  
Author(s):  
Marta L. Fiorotto ◽  
Teresa A. Davis ◽  
Peter J. Reeds
Keyword(s):  
Protein Synthesis ◽  
Protein Turnover ◽  
Myofibrillar Protein ◽  
Synthesis Rate ◽  
Protein Synthesis Rate ◽  
Myofibrillar Proteins ◽  
Sarcoplasmic Proteins ◽  
Rat Pups ◽  
Sarcoplasmic Protein ◽  
Degradation Rates

The study tested the hypothesis that a higher rate of myofibrillar than sarcoplasmic protein synthesis is responsible for the rapid postdifferentiation accumulation of myofibrils and that an inadequate nutrient intake will compromise primarily myofibrillar protein synthesis. Myofibrillar (total and individual) and sarcoplasmic protein synthesis, accretion, and degradation rates were measured in vivo in well-nourished (C) rat pups at 6, 15, and 28 days of age and compared at 6 and 15 days of age with pups undernourished (UN) from birth. In 6-day-old C pups, a higher myofibrillar than sarcoplasmic protein synthesis rate accounted for the greater deposition of myofibrillar than sarcoplasmic proteins. The fractional synthesis rates of both protein compartments decreased with age, but to a greater degree for myofibrillar proteins (−54 vs. −42%). These decreases in synthesis rates were partially offset by reductions in degradation rates, and from 15 days, myofibrillar and sarcoplasmic proteins were deposited in constant proportion to one another. Undernutrition reduced both myofibrillar and sarcoplasmic protein synthesis rates, and the effect was greater at 6 (−25%) than 15 days (−15%). Decreases in their respective degradation rates minimized the effect of undernutrition on sarcoplasmic protein accretion from 4 to 8 days and on myofibrillar proteins from 13 to 17 days. Although these adaptations in protein turnover reduced overall growth of muscle mass, they mitigated the effects of undernutrition on the normal maturational changes in myofibrillar protein concentration.

CHARACTERISTICS OF SARCOPLASMIC PROTEINS AND THEIR INTERACTION WITH MYOFIBRILLAR PROTEINS

2005 ◽  
Vol 29 (5) ◽  
pp. 517-532 ◽  
Author(s):  
YOUNG S. KIM ◽  
JIRAWAT YONGSAWATDIGUL ◽  
JAE W. PARK ◽  
SUPAWAN THAWORNCHINSOMBUT
Keyword(s):  
Myofibrillar Proteins ◽  
Sarcoplasmic Proteins

scholarly journals Residues of Fluoroquinolone Antibiotics Induce Carbonylation and Reduce In Vitro Digestion of Sarcoplasmic and Myofibrillar Beef Proteins

Foods ◽  
2020 ◽  
Vol 9 (2) ◽  
pp. 170 ◽  
Author(s):  
Johana Márquez-Lázaro ◽  
Darío Méndez-Cuadro ◽  
Erika Rodríguez-Cavallo
Keyword(s):  
Nutritional Value ◽  
In Vitro Digestion ◽  
Myofibrillar Proteins ◽  
Maximum Residue Limit ◽  
Carbonyl Index ◽  
Sarcoplasmic Proteins ◽  
Fluoroquinolone Antibiotics ◽  
Vitro Effect ◽  
The Impact

Although the impact of oxidation on human health has been of growing interest, the oxidation of proteins, major component of meat, has received little attention. This paper describes the in vitro effect of five fluoroquinolones (FQs) on carbonylation of sarcoplasmic and myofibrillar proteins of beef when found at concentrations close to the maximum residue limit (MRL). Samples were treated individually with the FQs, determining in each protein fraction the carbonyl index, protein content and oxidized proteins identification, using 2,4-dinitrophenyhydrazine (DNPH) alkaline assay, Western blot and Bradford methods, and mass spectrometry, respectively. Besides, the in vitro effect of these residues on gastric and duodenal digestion of proteins was evaluated. The carbonylation induced by FQs affected both protein fractions being significant with respect to the blank in 73.3% of cases. This damage was correlated with loss of solubility and digestibility, with sarcoplasmic proteins the most affected. Danofloxacin and enrofloxacin were the FQs with greatest oxidant effects, especially affecting glycolysis and glycogen proteins. Our results suggest that these residues induce irreversible oxidative damage on the main beef proteins and could affect their nutritional value.

Phosphorylation modification of myofibrillar proteins by sodium pyrophosphate affects emulsion gel formation and oxidative stability under different pH conditions

2019 ◽  
Vol 10 (10) ◽  
pp. 6568-6581 ◽  
Author(s):  
Jinyu Chen ◽  
Yunxia Ren ◽  
Kunsheng Zhang ◽  
Jinping Qu ◽  
Fangyang Hu ◽  
...  
Keyword(s):  
Oxidative Stability ◽  
Sodium Pyrophosphate ◽  
Myofibrillar Proteins ◽  
Gel Formation ◽  
Gel Properties ◽  
Emulsion Gel ◽  
Ph Conditions

The work explored the mechanisms responsible for the enhanced emulsion gel properties of myofibrillar proteins by phosphorylation modification.

Muscle Proteins of the Coelacanth Latimeria Chalumnae Smith

1973 ◽  
Vol 53 (4) ◽  
pp. 763-784 ◽  
Author(s):  
G. Hamoir ◽  
A. Piront ◽  
Ch. Gerday ◽  
P. R. Dando
Keyword(s):  
Ionic Strength ◽  
Gel Electrophoresis ◽  
White Muscle ◽  
Protein Composition ◽  
Myofibrillar Proteins ◽  
Starch Gel Electrophoresis ◽  
High Concentration ◽  
Sarcoplasmic Proteins ◽  
Starch Gel ◽  
Muscle Types

Although the anatomy of the coelacanth muscles has been examined very thoroughly, their protein composition has, until recently, not been investigated. Thanks, however, to the 1972 British–French–American expedition to the Comores, frozen material has been made available and some results on myoglobin and four glycolytic enzymes have already been published. We have carried out a comparison of the sarcoplasmic proteins of red and white muscle by starch-gel electrophoresis. The ninhydrin-positive dialysable constituents and the myofibrillar proteins of white muscle have also been examined.A few puzzling results obtained with the white muscle extracts have been related to the occurrence of o.1 M ammonia, due presumably to the splitting of urea by a bacterial urease, and to an alteration of the active thiol groups of GAPDH and PK. If due account is taken of these unusual post-mortem changes, the extractability of the proteins and their properties are strikingly similar to those of teleosteans. The comparison of the sarcoplasmic proteins of white and red muscle by starch-gel electrophoresis revealed also that the differentiation observed in the coelacanth was similar to that occurring in the carp. A study of the low-molecular-weight proteins, or parvalbumins, of white muscle and of the myofibrillar proteins also shows the expected differences between the two muscle types.The only abnormal features observed in this study were the high concentration of parvalbumins, 1.5–2 times that found in other species examined, and the occurrence of an unusual globulin fraction which was easily extracted at ionic strength 0.5 and insoluble at ionic strength 0.35 and neutral pH.

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