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Demystifying differences in meat quality between slow-growing and fast-growing broilers using the phosphorylome

 Last Update: 2022-08-30
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The increased growth rate and breast muscle yield of broilers is accompanied by a deterioration in meat quality
.
On October 16, 2021, the international food journal Food Chemistry (IF 9.
231) published online the innovative research results "Comparative phosphoproteomic provides insights into meat quality differences between slow- and fast-growing broilers" by the team of Yangzhou University Professor Chen Guohong and Associate Professor Xu Qi
.
This study explored the mechanisms leading to the quality difference between slow and fast broilers through phosphorylation proteomics, providing important information for genetic improvement of chicken quality
.
Among them, Zhongke New Life provides phosphorylated proteome detection services
.

Research materials
Snow pheasant and Ross 308 broiler

Technical route
Step 1: There are significant differences in meat quality and muscle fiber properties between the slow broiler (SG) group and the fast broiler (FG) group;
Step 2: List the identified phosphorylated proteins and map the phosphorylation site;
step 3: identification and comparison of differentially abundant phosphorylated peptides;
step 4: functional enrichment analysis of differentially phosphorylated proteins
.

Results

1.
There were significant differences in meat properties and muscle fiber properties between the SG group and the FG group.

By comparing some key physical properties, it was found that the meat redness, yellowness, shear force, pH24h and protein content of SG were better than those of FG, while the pressure loss , IMF and moisture content were lower than FG meat
.
Although there was no difference in muscle fiber type, the cross-sectional area of SG was larger than that of FG (Fig.
1)
.

Figure 1 Differences in meat quality and muscle fiber properties between SG and FG

2.
List the identified phosphorylated proteins and map the phosphorylation sites
.
Quantitative phosphorylation proteomic detection was performed using 6-label TMT.
The results showed that the distribution of phosphorylation sites in broiler proteins was diverse
.
Among the 3895 phosphorylation sites, 2799 (71.
86%) occurred on serine, 829 (21.
28%) on threonine, and 267 (6.
86%) on tyrosine residues (Fig.
2C)
.
To further understand the upstream pathways of differentially phosphorylated proteins, 20 possible phosphorylation motifs were identified by motif analysis, including 17 serine motifs and 3 threonine motifs (Fig.
2F)
.
Taken together, phosphorylated proteins play an important role in the difference in meat quality between SG and FG
.

Figure 2 Phosphoproteins and phosphate sites

3.
Identification and comparison of differentially abundant phosphorylated peptides
Through differential analysis, 595 phosphorylated peptides with significant differences were found in SG and FG.
Compared with FG, SG had 114 up-regulated and 481 down-regulated (Fig.
3)
.
Most of the up-regulated phosphorylated peptides are related to actin binding, muscle fiber development-related proteins, such as OBSL1, MYH1E, MYH1F, TNNT3, MRC2 involved in collagen binding and SLC7A5 involved in amino acid transport are the top 5 upregulated phosphorylation Peptides
.
Among the 481 down-regulated phosphorylated peptides, PHKB, MAP2k6, GPI, GAPDH, CASQ2, CAMK2D were significantly different, and CRAT and AUP1 were also detected (Table 1)
.
In conclusion, the up-regulated phosphopeptides were related to myofibrillar proteins, proteins involved in collagen binding and amino acid transport, and the down-regulated phosphopeptides were related to protein kinases, glycolytic enzymes, calcium release, and proteins involved in lipid metabolism
.

Table 1 Compared with FG, the phosphorylation sites of SG key regulated phosphorylated proteins and their related signaling pathways

Figure 3 Comparative analysis of significantly differentially phosphorylated peptides

4.
Functional enrichment analysis of differentially phosphorylated proteins
Through GO enrichment analysis, KEGG pathway analysis and protein interaction network analysis, it was found that myofibrils, calcium-related proteins involved in muscle binding and contraction, and glycolytic enzymes involved in energy metabolism interact and play an important role in SG and FG succulents (Fig.
4)
.

Figure 4 Functional enrichment analysis of differentially phosphorylated proteins in SG and FG meat

In this study, using phosphorylation modification omics analysis, some phosphorylated proteins were found to have positive effects on protein and IMF deposition in two broiler lines
.
Upregulation of SG phosphorylated myofibrillar proteins resulted in larger, more tightly packed fibers, and lower pressure loss and tenderness; whereas downregulation of partially phosphorylated proteins indicated a lower degree of glycolysis and metabolism
.

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