214 research outputs found
Effects of ambient temperature on growth performance, slaughter traits, meat quality and serum antioxidant function in Pekin duck
The present study investigated the effects of temperature on growth performance, slaughtering traits, meat quality and antioxidant function of Pekin ducks from 21โ42โd of age. Single factor analysis of variance was used in this experiment, 144 21โd-old Pekin ducks were randomly allotted to 4 environmentally controlled chambers: T20 (20ยฐC), T23 (23ยฐC), T26 (26ยฐC) and T29 (29ยฐC), with 3 replicates in each group (12 ducks in each replicate), the relative humidity of all groups is 74%. During the 21-day trial period, feed and water were freely available. At 42โd, the BW (body weight) and ADG (average daily gain) of T26 were significantly lower than T20 (p <โ0.05), and the T29 was significantly lower than T20 and T23 (p <โ0.05). The ADFI (average daily feed intake) of T26 and T29 were significantly lower than T20 and T23 (p <โ0.05). Compared to the T29, the T20 showed a significant increase oblique body length and chest width, and both the keel length and thigh muscle weight significantly increased in both the T20 and T23, while the pectoral muscle weight increased significantly in other groups (pโ<โ0.05). The cooking loss of the T29 was the lowest (pโ<โ0.05). The T-AOC (total antioxidant capacity) of T29 was significantly higher than the other groups (pโ<โ0.05), the SOD (superoxide dismutase) in the T29 was significantly higher than the T23 and T26 (pโ<โ0.05). In conditions of 74% relative humidity, the BW and ADFI of Pekin ducks significantly decrease when the environmental temperature exceeds 26ยฐC, and the development of body size and muscle weight follows this pattern. The growth development and serum redox state of Pekin ducks are more ideal and stable at temperatures of 20ยฐC and 23ยฐC
Carcass and Meat Quality Traits in an EmbdenรToulouse Goose Cross Raised in Organic Dehesa
his study assessed the influence of genetic type (Embden-Anser anser, EE; Toulouse-Anser anser, TT and F1 cross, ET) for meat characteristics (carcass, meat quality and fatty acid (FA) profiles), of domestic geese โAnser anser domesticusโ raised in dehesa as an alternative, organic feeding system. Carcass and breast muscle weight (p<0.01) were greater for the ET group at the same live weight. None of the groups showed differences in the production of fatty liver with this type of feeding. Higher values were found for maximum WarnerโBratzler shear force (between 7.62 and 8.87 kg/cm2), which implies the improvement of this parameter. High levels of oleic FAs were obtained, especially for the TT group. The polyunsaturated/saturated FA ratio was highest for the ET group (p<0.001), reflecting the optimum nutritional values as a component of a healthy consumer die
Selection-driven chicken phenome and phenomenon of pectoral angle variation across different chicken phenotypes
An appreciation of the synergy between genome and phenome of poultry breed is essential for a complete understanding of their biology. Phenotypic traits are shaped under the influence of artificial, production-oriented, selection that often acts contrary to that which would occur during natural selection. In this comparative study, we analysed the phenotypic diversity of 39 chicken breeds and populations that make up a significant part of the world gene pool. Grouping patterns of breeds found within the traditional, phenotypic models of their classification/clustering required in-depth analysis using sophisticated mathematical approaches. As a result of studying performance and conformation phenotypes, a phenomenon of previously underestimated variability in pectoral angle (PA) was revealed. Moreover, patterns of PA relationship with productive traits were analysed. We propose using PA measurement as a promising new auxiliary index for selecting hens and roosters of breeding flocks in egg production improvement programs
Duck and Goose Meat Product Processing Technology
200 pages, illustrations (some color)
๋์ฅ ์ ์ฅ ์ค ๋ญ๊ณผ ์ค๋ฆฌ์ ๊ณจ๊ฒฉ๊ทผ์์ ๋จ๋ฐฑ์ง ๋ถํด๋ก ์์ฑ๋ ํฉํ์ด๋ ๋ฐ ์ก์ง ๋ณ
ํ์๋
ผ๋ฌธ(์์ฌ) -- ์์ธ๋ํ๊ต๋ํ์ : ๊ตญ์ ๋์
๊ธฐ์ ๋ํ์ ๊ตญ์ ๋์
๊ธฐ์ ํ๊ณผ, 2021.8. Gap-Don Kim.Proteolysis, a phenomenon in which a protein is automatically broken down
by the endogenous proteolytic enzymes in meat, and its relationship with meat
quality characteristics have been fully studied in beef and pork. However, this
topic has not fully dealt with poultry meat, such as chicken and duck. Moreover,
previous studies mainly focused on the effect of proteolysis in meat
tenderization resulting in degradation of myofibrillar proteins, such as myosin,
actin, troponins, desmin, nebulin, etc. Although most meat proteins including
sarcoplasmic proteins as well as myofibrillar proteins are affected by the
endogenous proteolytic enzymes during meat storage, degradation of whole
proteins has not specifically been elucidated on until now. Therefore, this study
was conducted to evaluate the degradation of whole proteins in chicken and
duck skeletal muscles during cold storage by analyzing proteolysis-induced peptides. In addition, the study evaluated the influence of protein degradation
(peptide production) by proteolysis on the change of poultry meat quality.
In the first study, the proteolysis trends and meat quality of the chicken
pectoralis major (PM) and iliotibialis (IL) muscles stored at 4ยบC for seven days
were investigated. Chicken PM had a lower moisture and fat content than the
IL muscle (P < 0.05). The changes of pH, shear force, lightness, and
yellowness of both muscles showed the same tendencies during storage (P <
0.05). After storage, it was found that the purge loss was higher (P < 0.05) in
PM than IL muscle, whereas redness was not different between the two
muscles (P > 0.05). The different composition of muscle fibers between PM
(100% fast type) and IL (88.85% fast and 11.15% slow types) led to differences
in proteolysis. A total of 3,468 peptides were detected and derived from 33
proteins of aged chicken PM, and for aged chicken IL muscle, 3,589 peptides
were identified from 37 proteins. Quantitative changes in peptides originated
from pyruvate kinase, L-lactate dehydrogenase, fructose-bisphosphate
aldolase, beta-enolase, creatine kinase M-type, and hemoglobin subunit alpha,
and were closely related with changes in meat quality during cold storage.
In the second study, proteolysis-induced peptides were quantified from
duck PM and IL during 10 days of cold storage. In addition, protease activity
(calpains, cathepsins L and B, proteasome 20S, and caspase-3) and meat
quality characteristics were evaluated. Duck IL had a higher pH and lightness but lower cooking loss than those of PM (P < 0.05). During the 10-day cold
storage, the pH value of PM declined significantly (P < 0.05), while the meat
quality traits of IL were not affected by storage (P > 0.05). In PM, the redness
increased from day one to day five, while cooking loss showed a lower rate on
day 10 compared with that on day five (P < 0.05). For the protease activities,
there were no significant differences in the activities of cathepsin B and
proteasome 20S during cold storage (P > 0.05). Significantly, the activity of
calpains declined gradually after aging (P < 0.05), and that of PM showed a
higher activity than that of IL (P < 0.05). The cathepsin L activity of IL and the
caspase-3 activity of PM decreased after five days (P < 0.05). A total of 5,155
peptides were detected and derived from 34 proteins of aged duck PM, and 247
peptides were derived from myoglobin. For 32 proteins of IL, there were 4,222
quantitated peptides, most of which were degraded by the actin. Furthermore,
the correlation between degraded protein, meat quality characteristics, and
proteolytic enzyme activity was determined via principal component analysis.
In both PM and IL, the caspase-3 activity was related to the hemoglobin alpha
A subunit. In addition, the meat color traits of both muscles were correlated
with the glucose-6-phosphate isomerase and glyceraldehyde-3-phosphate
dehydrogenase. These findings indicate that there are many proteins affected
by proteolysis, and glucose-6-phosphate isomerase and glyceraldehyde-3-
phosphate dehydrogenase can be useful markers for predicting or controlling
duck meat quality characteristics.์์ก ๋ด์ ์กด์ฌํ๋ ๋ค์ํ ์ข
๋ฅ์ ๋จ๋ฐฑ์ง ๋ถํดํจ์์ ์์ฉ์ผ๋ก
์์ฐ์ ์ผ๋ก ๋จ๋ฐฑ์ง์ด ๋ถํด๋๋ ํ์์ธ ๋จ๋ฐฑ์ง ์๊ฐ๋ถํด(proteolysis)
์์ฉ๊ณผ ๊ทธ๋ก ์ธํ ์ก์ง ํน์ฑ ๋ณํ์ ๋ํ ์ฐ๊ตฌ๋ ์ฐ์ก ๋ฐ ๋์ก์์ ๋ง์ด
์ํ๋์ด ์๋ค. ๊ทธ๋ฌ๋ ๋ญ ๋ฐ ์ค๋ฆฌ์ ๊ฐ์ ๊ฐ๊ธ๋ฅ์์๋ ์ด๋ฌํ ์ฐ๊ตฌ๊ฐ
๋ง์ด ์ํ๋์ง ์์๊ณ , ๋์ฑ์ด ์์ก์ ์ฐ๋ ํฅ์๊ณผ ๊ด๋ จ์ด ํฐ
๊ทผ์์ฌ์ ๋จ๋ฐฑ์ง(myosin, actin, troponins, desmin, nebulin ๋ฑ)์ ๋ถํด์
๊ตญํ๋ ์ฐ๊ตฌ๊ฐ ์ฃผ๋ฅผ ์ด๋ฃจ๊ณ ์๋ค. ์์ก ๋ด ๋จ๋ฐฑ์ง ๋ถํดํจ์์ ์์ฉ์
๊ทผ์์ฌ์ ๋จ๋ฐฑ์ง๋ฟ๋ง ์๋๋ผ ๊ทผ์ฅ๋จ๋ฐฑ์ง์ ํฌํจํ ๋๋ถ๋ถ์
์์ก๋จ๋ฐฑ์ง์ ์ํฅ์ ๋ฏธ์นจ์๋ ๋ถ๊ตฌํ๊ณ ์ ์ฒด ๋จ๋ฐฑ์ง์ ๋ํ
๋ถํด์์ฉ์ ๋ณด๋ค ์ธ์ธํ๊ฒ ๊ท๋ช
๋์ง ๋ชปํ๋ค. ๋ฐ๋ผ์, ๋ณธ ๋ญ๊ณผ ์ค๋ฆฌ ๊ณจ๊ฒฉ๊ทผ์์ ๋จ๋ฐฑ์ง ์๊ฐ๋ถํด ์์ฉ์ผ๋ก ์์ฑ๋ ํฉํ์ด๋
๋ถ์์ ํตํด ๋จ๋ฐฑ์ง ๋ถํด์์ฉ์ ๊ท๋ช
ํ๊ธฐ ์ํ์ฌ ์ํ๋์๋ค. ๋ํ, ๋จ๋ฐฑ์ง ์๊ฐ๋ถํด(ํฉํ์ด๋ ์์ฑ) ์์ฉ์ด ๊ฐ๊ธ๋ฅ ์์ก์ ํ์ง ๋ณํ์
๋ฏธ์น๋ ์ํฅ๋ ๋ถ์ํ์๋ค. ์ฒซ ๋ฒ์งธ ์ฐ๊ตฌ์์๋ ๋ญ์ ํ๊ทผ(M. pectoralis major)๊ณผ ์ฅ๊ฒฝ๊ทผ(M.
iliotibialis)์ 4โ์์ 7 ์ผ ๋์ ์ ์ฅํ๋ฉฐ ๋จ๋ฐฑ์ง ์๊ฐ๋ถํด ํ์๊ณผ ์ก์ง
๋ณํ๋ฅผ ๋ถ์ํ์๋ค. ํ๊ทผ์ ์ฅ๊ฒฝ๊ทผ๋ณด๋ค ๋ฎ์ ์๋ถ๊ณผ ์ง๋ฐฉ์ ํจ์ ํ๊ณ
์์๋ค(P < 0.05). ์ ์ฅ ๊ธฐ๊ฐ ๋์ pH, ์ ๋จ๊ฐ, ๋ช
๋ ๋ฐ ํฉ์๋ ๋ณํ๋ ๋
๊ทผ์ก์์ ์ ์ฌํ ๊ฒฝํฅ์ ๋ํ๋ด์๋ค. ํฌ์ฅ๊ฐ๋์ ์ฅ๊ฒฝ๊ทผ ๋ณด๋ค ํ๊ทผ์์
๋ ํฐ ๊ฐ์ ๋ํ๋์ง๋ง(P < 0.05), ์ ์๋๋ ๋ ๊ทผ์ก ๊ฐ ์ฐจ์ด๋ฅผ ๋ํ๋ด์ง
์์๋ค(P > 0.05). ๋ ๊ทผ์ก์ ์๋ก ๋ค๋ฅธ ๊ทผ์ฌ์ ์กฐ์ฑ์ ๋ํ๋ด์๋๋ฐ, ํ๊ทผ์ fast type ์ ๊ทผ์ฌ์ ๋ก๋ง ์ด๋ค์ง ๋ฐ๋ฉด, ์ฅ๊ฒฝ๊ทผ์ 88.85%์ fast
type ๊ณผ 11.15%์ slow type ์ผ๋ก ๊ตฌ์ฑ๋์ด ์์๊ณ , ์ด๋ฌํ ๊ทผ์ฌ์ ์กฐ์ฑ์
์ฐจ์ด๊ฐ ๋จ๋ฐฑ์ง ์๊ฐ๋ถํด ์์ฉ์์ ์๋ก ๋ค๋ฅธ ๊ฒฝํฅ์ ๋ํ๋ด๊ฒ ํ์๋ค. Pyruvate kinase, L-lactate dehydrogenase, fructose-bisphosphate aldolase,
beta-enolase, creatine kinase M-type ๋ฐ hemoglobin subunit alpha ์์
์ ๋ํ ํฉํ์ด๋์ ์ ๋์ ๋ณํ๋ ๋์ฅ ์ ์ฅ ์ค ๊ณ์ก ํ์ง์ ๋ณํ์ ๋งค์ฐ
๋ฐ์ ํ ์ฐ๊ด์ฑ์ ๋ํ๋ด์๋ค. ๋ฐ๋ผ์, ์ก์ง ๋ณํ์ ์ฐ๊ด์ฑ์ด ๋์ ๋จ๋ฐฑ์ง
๋๋ ๋จ๋ฐฑ์ง๋ก๋ถํฐ ์ ๋ํ ํฉํ์ด๋๋ ๊ณ์ก ํ์ง ์ฐ๊ด ์งํ๋ก ํ์ฉ์ด
๊ฐ๋ฅํ ๊ฒ์ด๋ค. ๋ ๋ฒ์งธ ์ฐ๊ตฌ๋ ์ค๋ฆฌ์ ํ๊ทผ๊ณผ ์ฅ๊ฒฝ๊ทผ์ 4โ์์ 10 ์ผ ๋์
์ ์ฅํ๋ฉด์ ํฉํ์ด๋์ ์ ๋์ ๋ณํ, ์ก์ง ํน์ฑ ๋ณํ ๋ฐ ๋จ๋ฐฑ์ง
๋ถํดํจ์(calpains, cathepsins L and B, proteasome 20S, and caspase-3)์
ํ์ฑ๋๋ฅผ ๋ถ์ํ์๋ค. ์ค๋ฆฌ์ ์ฅ๊ฒฝ๊ทผ์ ํ๊ทผ๋ณด๋ค pH์ ๋ช
๋๋ ๋์์ผ๋, ๊ฐ์ด๊ฐ๋์ ์ ์์ ์ผ๋ก ๋ฎ์๋ค(P < 0.05). 10 ๋์ ๋์ฅ ์ ์ฅ ์ค ํ๊ทผ์
pH ๊ฐ ์ ์์ ์ผ๋ก ๊ฐ์ํ์์ผ๋ ์ ์๋๋ ์ฆ๊ฐํ์๋ค(P < 0.05). ๊ทธ๋ฌ๋
์ฅ๊ฒฝ๊ทผ์ ๋์ฅ ์ ์ฅ์ผ๋ก ์ธํ ์ก์ง ๋ณํ๋ฅผ ๋ํ๋ด์ง ์์๋ค(P > 0.05).
๋จ๋ฐฑ์ง ๋ถํดํจ์ ์ค cathepsin B ์ proteasome 20S ์ ํ์ฑ๋๋ ๋์ฅ ์ ์ฅ
์ค ๋ณํ๋ฅผ ๋ํ๋ด์ง ์์์ผ๋(P > 0.05), calpains ์ ํ์ฑ๋๋ ์ ์ฐจ์ ์ผ๋ก
๊ฐ์ํ์๋ค(P < 0.05). ์ฅ๊ฒฝ๊ทผ์ cathepsin L ๊ณผ ํ๊ทผ์ caspase-3 ์
ํ์ฑ๋๋ ์ ์ฅ 5์ผ ํ ์ ์์ ์ผ๋ก ๊ฐ์ํ๋ ๊ฒฐ๊ณผ๋ฅผ ๋ํ๋ด์๋ค(P < 0.05).
์ค๋ฆฌ์ ํ๊ทผ์์๋ ์ด 37 ์ข
์ ๋จ๋ฐฑ์ง์์ 5,155 ๊ฐ์ ํฉํ์ด๋๊ฐ
ํ์ธ๋์๊ณ , ๊ทธ ์ค 247 ์ข
์ ํฉํ์ด๋๊ฐ myoglobin ์์ ์ ๋ํ์๋ค. ์ฅ๊ฒฝ๊ทผ์์๋ 32 ๊ฐ์ ๋จ๋ฐฑ์ง์์ 4,222 ๊ฐ์ ํฉํ์ด๋๊ฐ ํ์ธ๋์๊ณ , ๋ค์์ ํฉํ์ด๋๊ฐ actin ์์ ์ ๋ํ ๊ฒ์ผ๋ก ํ์ธ๋์๋ค. ๋ ๊ทผ์ก ๋ชจ๋
caspase-3 ์ ํ์ฑ๋์ hemoglobin alpha A subunit ์ ๋ ํฉํ์ด๋์ ์ ๋์
๋ณํ๊ฐ ๋งค์ฐ ๋ฐ์ ํ ์ฐ๊ด์ด ์๋ ๊ฒ์ผ๋ก ํ์ธ๋์๊ณ , ์ก์์ glucosephosphate isomerase ๋ฐ glyceraldehyde-3-phosphate dehydrogenase ์์
์ ๋ํ ํฉํ์ด๋์ ๋น์ทํ ๋ณํ ๊ฒฝํฅ์ ๋ณด์ฌ์ฃผ์๋ค. ์ด์์ ๊ฒฐ๊ณผ๋ ์ค๋ฆฌ
ํ๊ทผ๊ณผ ์ฅ๊ฒฝ๊ทผ์ ์๋ง์ ๋จ๋ฐฑ์ง์ด ์๊ฐ๋ถํด์์ฉ์ ์ํฅ์ ๋ฐ์ผ๋ฉฐ, ์ด๋ค
์ค ๋ช๋ช ๋จ๋ฐฑ์ง์ ์ค๋ฆฌ์ก์ ํ์ง ํน์ฑ์ ์์ธกํ๊ฑฐ๋ ์ ์ดํ๊ธฐ ์ํ
์งํ๋ก ์ ์ฉํ๊ฒ ํ์ฉ๋ ์ ์์์ ์๋ฏธํ๋ค.Chapter I General Introduction 1
1 Introduction 1
1.1 Research background 1
1.2 Purpose of this study 3
2 Literature Review 5
2.1 Proteolysis in meat 5
2.2 Influence of proteolysis on meat quality 8
2.3 Influence of proteolysis on proteome 9
2.4 Factors affecting proteolysis in meat 13
2.4.1 pH value 13
2.4.2 Ionic strength and concentration 14
2.4.3 Muscle fiber characteristics 14
2.4.4 Proteolytic enzymes 16
Chapter II Quantitative changes of proteolysis-induced peptides in relation to meat quality characteristics of chicken M pectoralis major and M. iliotibialis 20
1 Abstract 20
2 Introduction 22
3 Materials and methods 25
3.1 Sample preparation 25
3.2 Proximate composition 25
3.3 Meat quality characteristics 26
3.3.1 pH 26
3.3.2 Meat color 26
3.3.3 Water-holding capacity 26
3.3.4 Meat tenderness 27
3.4 Immunohistochemistry 27
3.5 Extraction of peptides 28
3.6 LCโMS/MS analysis and label-free quantification 29
3.7 Proteolytic enzymes 30
3.7.1 Activities of cathepsin B & L 30
3.7.2 Activities of calpain and proteasome 20S 31
3.7.3 Activity of caspase-3 32
3.8 Statistical Analysis 32
4 Results 34
4.1 Proximate composition of chicken skeletal muscles 34
4.2 Meat quality characteristics of chicken skeletal muscles 35
4.3 Muscle fiber characteristics (MFC) 37
4.4 Proteolytic enzymesโ activity 39
4.5 Quantitative changes in proteolysis-induced peptides during cold storage 40
4.6 The relationship between proteolysis-induced peptides, meat quality characteristics, and proteolytic enzyme activity 47
5 Discussion 50
6 Conclusion 54
Chapter III Quantitative changes of proteolysis-induced peptides in relation to meat quality characteristics of duck M pectoralis major and M.iliotibialis 55
1 Abstract 55
2 Introduction 57
3 Materials and methods 59
3.1 Sample preparation 59
3.2 Proximate composition 59
3.3 Meat quality charicteristics 60
3.4 Immunohistochemistry 61
3.5 Quantification of peptides 62
3.6 Activity of proteolytic enzymes 63
3 .7 Statistical analysis 64
4 Results 66
4.1 Proximate composition of duck skeletal muscles 66
4.2 Meat quality of duck skeletal muscles 67
4.3 Muscle fiber characteristics (MFC) 69
4.4 Proteolytic enzyme activities 71
4.5 Quantitative changes in peptides during cold storage 72
4.6 The relationship between degraded protein, meat quality characteristics, and proteolytic enzymesโ activity 73
5 Discussion 81
6 Conclusion 84
Overall Conclusion 85
References 87
Abstract in Korean 108์
Rising Stars in Avian Physiology: 2022
We are delighted to present the inaugural Frontiers in Physiology โRising Stars in Avian Physiologyโ annual series of article collections. Recognizing the future leaders in avian physiology is fundamental to safeguarding tomorrow's driving force in innovation.
This Research Topic will showcase the high-quality work of up-and-coming researchers in the early stages of their careers. These are researchers within 10 years of their PhD or MD completion across the entire breadth of avian physiology, and present advances in theory, experiment and methodology with applications to compelling problems.
All Rising Star researchers will be suggested by the editorial office and established Editors within our board in recognition of their influence on the future directions in their respective fields. While future innovations in avian physiology are yet to be discovered, this Research Topic will give the community a hint at whom to follow.
This Research Topic is part of the Rising Stars in Physiology Serie
Genetic Diversity and Evolution of Yunnan Chicken Breeds of China
Chickens are the first type of bird that was domesticated and spread widely in the world to cover the growing demand for animal protein from meat and eggs, and it was cultivated from a wild ancestor known Red junglefowl (Gallus gallus). Yunnan Province is considered the most diverse in culture and biology among all the provinces of China. There are a total of more than 24 chicken breeds in Yunnan Province. These chickens are characterized by good quality of their meat and eggs, a good immune system against diseases, and the ability to adapt to various environmental and administrative conditions. Yunnan Province is one of the centers of domestication and evolutionary of chickens in the world. There are many studies that have been conducted to evaluate and study the genetic diversity and evolutionary relationship within and among chicken breeds in Yunnan Province and their relationship with wild chicken species and other chicken breeds using phenotypic markers, protein polymorphisms, SNPs marker, microsatellite marker, and mitochondrial DNA marker. However, there is no review that summarizes these studies, and most of these studies were authored in the Chinese language. Therefore, we have reviewed all studies that have been conducted on Yunnan chicken breeds diversity in Yunnan Province
Recent Advances in OMICs Technologies and Application for Ensuring Meat Quality, Safety and Authenticity
Consumers and stakeholders are increasingly demanding that the meat industry guarantees high-quality meat products with stable and acceptable sensory and safety properties. To do this, it is necessary to understand the mechanisms that underlie the conversion of muscle into meat, as well as the impact of pre- and post-harvest procedures on the final quality and safety of meat products. Over the last two decades, sophisticated OMICs technologiesโgenomics, transcriptomics, proteomics, peptidomics, metabolomics and lipidomics, also known as foodomicsโhave been powerful approaches that extended the scope of traditional methods and have established impressive possibilities of addressing meat quality issues. Foodomics were further used to elucidate the biological basis/mechanisms of phenotypic variation in the technological and sensory quality traits of meat from different species. Overall, these techniques aimed to comprehensively study the dynamic link(s) between the genome and the quality traits of the meat that we eat compared to traditional methods, hence improving both the accuracy and sensitivity thanks to the large quantities of data that can be generated. This Special Issue focused on the cutting-edge research applications of OMICs tools to characterize or manage the quality of muscle foods. The research papers applied transcriptomics, targeted and untargeted proteomics, metabolomics, and genomics, among others, to evaluate meat quality, determine the molecular profiles of meat and meat products, discover and/or evaluate biomarkers of meat quality traits, and to characterize the safety, adulteration, and authenticity of meat and meat products
Molecular mechanisms underlying the impact of muscle fiber types on meat quality in livestock and poultry
In the past, the primary emphasis of livestock and poultry breeding was mainly on improving the growth rate, meat production efficiency and disease resistance. However, the improvement of meat quality has become a major industrial focus due to the ongoing advancements in livestock and poultry breeding. Skeletal muscles consist of multinucleated myofibers formed through the processes of myoblast proliferation, differentiation and fusion. Muscle fibers can be broadly classified into two main types: slow-twitch (Type I) and fast-twitch (Type II). Fast-twitch fibers can be further categorized into Type IIa, Type IIx, and Type IIb. The proportion of Type I and Type IIa muscle fibers is positively associated with meat quality, while the presence of Type IIb muscle fibers in skeletal muscle tissue is inversely related to meat quality. Consequently, muscle fiber composition directly influences meat quality. The distribution of these fiber types within skeletal muscle is governed by a complex network, which encompasses numerous pivotal regulators and intricate signaling pathways. This article aims to succinctly outline the parameters utilized for assessing meat quality, elucidate the relationship between muscle fiber composition and meat quality as well as elaborate on the relevant genetic factors and their molecular mechanisms that regulate muscle fiber types in livestock and poultry. This summary will enrich our comprehension of how to improve meat quality in livestock and poultry, providing valuable insights for future improvements
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