Influence of transport conditions and pre‐slaughter water shower spray during summer on protein characteristics and water distribution of broiler breast meat

This study investigated the effects of pre‐slaughter transport during summer and subsequent water shower spray on broiler meat quality and protein characteristics. Arbor Acres broiler chickens (n = 126, 42 days old, mixed sex, 2.5‐3 kg) were randomly categorized into three treatments: (i) control group without transport (C); (ii) 30 min transport (T); and (iii) 30 min transport followed by 10 min water shower spray and 20 min lairage (T/W). Each treatment consisted of six replicates with seven birds each. Ambient temperature was 32‐35°C during transportation. Results indicated that transport during high ambient temperature denatured myosin and sarcoplasmic proteins, led to decreased protein solubility and resulted in glycogen phosphorylase precipitated to the myofibrillar fraction. Furthermore, meat quality in the transport group showed a pale, soft and exudative (PSE)‐like syndrome. Water shower spray during lairage after transport reduced the degree of protein denaturation and lessened the deterioration of meat quality.     

Inosine‐5'‐monophosphate is a candidate agent to resolve rigor mortis of skeletal muscle

The object of the present study was to reveal the action of inosine‐5'‐monophosphate (IMP) toward myofibrils in postmortem muscles. IMP solubilized isolated actomyosin within a narrow range of KCl concentration, 0.19‐0.20 mol/L, because of the dissociation of actomyosin into actin and myosin, but it did not solubilize the proteins in myofibrils with 0.2 mol/L KCl. However, IMP could solubilize both proteins in myofibrils with 0.2 mol/L KCl in the presence of 1 m mol/L pyrophosphate or 1.0–3.3 m mol/L adenosine‐5'‐diphosphate (ADP). Thus, we presumed that pyrophosphate and ADP released thin filaments composed of actin, and thick filaments composed of myosin from restraints of myofibrils, and then both filaments were solubilized through the IMP‐induced dissociation of actomyosin. Thus, we concluded that IMP is a candidate agent to resolve rigor mortis because of its ability to break the association between thick and thin filaments.     

Ontogeny of the stomach in yellow catfish (Pelteobagrus fulvidraco): detection and quantifictation of pepsinogen and H+/K+‐ATPase gene expression

Yellow catfish (Pelteobagrus fulvidraco) is an important commercial species with high aquaculture potential in China. To better understand the process of digestive functioning of gastric gland development during the larval from 1 dph (day post‐hatching) to 30 dph, real‐time PCR was used to detect and quantify the pepsinogen and H⁺/K⁺‐ATPase gene expression in P. fulvidraco. These data were also compared with the adult situation. The results showed that the expression of pepsinogen and H⁺/K⁺‐ATPase genes in P. fulvidraco larvae both started at 1 dph, though the expression level was very low until 3 dph. The quantification of pepsinogen gene expression increased significantly from 4 to 8 dph, increased fluctuantly from 8 to 23 dph and rose sharply from 23 to 30 dph. In comparison with adult fish, there were no significant differences with larvae at 5 and 23 dph. However, data of 10 and 30 dph larvae were obviously higher than those of adult group. H⁺/K⁺‐ATPase gene expression increased linearly from 1 to 30 dph. However, it was significantly lower than that of adult. The results show that P. fulvidraco larvae have an earlier functional stomach, though the function of the stomach is still not perfect. There is a gradual acidification environment within the stomach during the P. fulvidraco larvae development. Based on these results, we suggest that the weaning time for P. fulvidraco larvae would be much better after 23 dph.     

Myosin substitution rate is affected by the amount of cytosolic myosin in cultured muscle cells

In striated muscles, approximately 300 myosin molecules form a single thick filament in myofibrils. Each myosin is continuously displaced by another myosin to maintain the thick filament structure. Our previous study using a fluorescence recovery after photobleaching (FRAP) technique showed that the myosin replacement rate is decreased by inhibition of protein synthesis, but myosin is still exchangeable. This result prompted us to examine whether myosin in the cytoplasm is involved in myosin replacement in myofibrils. To address this, FRAP was measured in green fluorescent protein (GFP)‐tagged myosin heavy chain 3 (Myh3) expressing myotubes that were treated with streptolysin‐O (SLO), which forms pores specifically in the plasma membrane to induce leakage of cytoplasmic proteins. Our biochemical data demonstrated that the cytoplasmic myosin content was reduced in SLO‐permeabilized semi‐intact myotubes. Furthermore, FRAP experiments showed a sluggish substitution rate of GFP‐Myh3 in SLO‐permeabilized myotubes. Taken together, these results demonstrate that the myosin substitution rate is significantly reduced by a decreased amount of myosin in the cytoplasm and that cytoplasmic myosin contributes to myosin replacement in myofibrils.     

Muscle protein expression of pikeperches (Stizostedion lucioperca and S. volgense)

The purpose of the present study was to investigate the muscle protein expression in two pikeperches (Stizostedion lucioperca and S. volgense) through intra‐ and intermyomeric composition of white muscles. Using denaturing 10% sodium dodecylsulfate‐polyacrylamide gel electrophoresis, muscle protein expression was studied in relation to within‐ and between‐species morphological development, sex, maturity and age of pikeperches. Myosin, actin and troponin have a distinct role in the contraction and length tension of muscle fibers of these species. No obvious intramyomeric differences were found in the myosin heavy chain of both species. Myosin light chains (15–38 kDa) have different expression in different age groups. The muscle protein of the fingerling and adult S. lucioperca had high molecular weight (50 kDa) myosin in contrast to the other Percid species. The molecular weight of actins increased comparatively in low‐age‐group fish. ATP is stored in myosin and released to cause contraction when myosin comes in contact with actin of the experimental fish. Troponin regulates increasing concentration of light‐chain myosin in mature fish. Because troponin T has been implicated in the regulation of skeletal muscle kinetics, muscle contraction kinetics was predicted in different age groups. The muscle proteins of both sexes of these species have polymorphism in various age groups but have no difference in similar aged fish. No muscle protein dimorphism was found in these Percid species. The white muscle protein composition and contractile properties affect power production during fast, unsteady movement and swimming.     

Physicochemical properties of the thermal gel of water-washed meat in the presence of the more soluble fraction of porcine sarcoplasmic protein

We investigated the physicochemical properties of the thermal gel of water‐washed pork meat (WWM) in the presence of the soluble fraction of porcine sarcoplasmic protein (SP) obtained with ammonium sulfate at 75 percent saturation. Two precipitated fractions of SP were obtained at 0–50 percent and 50–75 percent saturation, named SP‐f1 and SP‐f2, respectively, and the soluble fraction obtained at 75 percent saturation, SP‐f3, was used. Sodium dodecyl sulfate‐polyacrylamide gel electrophoresis showed that SP‐f3 contained mainly glyceraldehyde‐3‐phosphate dehydrogenase (GAPDH), while SP‐f1 and SP‐f2 had other SPs such as phosphorylase b, enolase, actin and phosphoglycerate mutase. The gel strength of WWM was greater when SP‐f3 rather than one of various animal proteins such as bovine plasma (BP), egg white, or whey protein isolates (WPI), was added and SP‐f3 had a gel‐enhancing effect as good as that of polyphosphate (PP). The gel strength of WWM with added SP‐f3 increased significantly with NaCl at 0.15 mol/L or more, but not in the absence of NaCl (0 mol/L). The effect of SP‐f3 was evident at neutral pH and maximum gel strength was obtained at a pH above 6.0. Differential scanning calorimetric (DSC) analysis showed that an endothermic peak corresponding to myosin heads in WWM shifted to a lower temperature with the addition of SP‐f3, as in the case of PP, though there was no such shift in the presence of other animal proteins (BP, egg white and WPI), suggesting that SP‐f3 increases the gel strength of WWM through the dissociation of actomyosin similar to PP. Scanning electron microscopy (SEM) revealed wall‐like structures among the protein strands in the WWM gel matrix in the presence of SP‐f3. The results of DSC and SEM indicated that the formation of a gel network in meat products is reinforced with GAPDH in SP after the interaction between GAPDH and myofibrillar protein.     

Disaccharide combinations and the expression of enolase3 and plasma membrane Ca2+ ATPase isoform in sturgeon sperm cryopreservation

Acipenser sinensis and Acipenser dabryanus are critically endangered species, so germplasm conservation via cryopreservation of sperm is necessary. Disaccharides can act as membrane‐impermeable cryoprotectants, and enolase3 (ENO3) and plasma membrane Ca²⁺ ATPase isoform (PMCA2) are proteins associated with sperm quality. We considered seven characteristics of sperm quality in cultured brood stock from A. sinensis and A. dabryanus. We tested use of sucrose or trehalose alone and in combination at different concentrations for cryopreservation of A. dabryanus sperm. A low concentration of sucrose plus trehalose (S₁₅T₁₅) was optimal. Mixing of the extender with sucrose, lactose, or trehalose alone or with pairwise mixtures revealed that a mixture of lactose and trehalose (L₁₅T₁₅) gave the best results for both A. sinensis and A. dabryanus. Enolase3 and PMCA2 expression levels were measured in cryopreserved A. sinensis sperm via Western blotting. Relative ENO3 and PMCA2 expression levels were examined, and the relationship between disaccharide composition, sperm quality and protein expression was explored in A. sinensis. The results showed that relative ENO3 and PMCA2 expression levels were the highest at L₁₅T₁₅ in cryopreserved A. sinensis sperm. There were significant positive correlations between ENO3 expression and percentage membrane integrity, and between PMCA2 expression and sperm motility parameters (percentage of motile sperm, curvilinear velocity, straight‐line velocity and average path velocity; p < .05) in cryopreserved A. sinensis sperm. Our results indicate the optimal disaccharide combination and concentrations for cryopreservation of A. sinensis and A. dabryanus sperm and suggest that ENO3 and PMCA2 expression levels could serve as a valuable indicator of sperm quality in A. sinensis.     

The effect of inulin supply to high‐fat diet rich in saturated fatty acids on pork quality and profile of sarcoplasmic protein in meat exudate

The aim of the study was to evaluate the influence of inulin supply to high‐fat diet rich in saturated fatty acids (SFA) on pork quality and profile of sarcoplasmic protein in drip loss. At 50 days of age, twenty cross‐bred pigs (gilts) were randomly allotted to four groups: the control (C) group fed a standard diet, and three experimental (D1, D2 and D3) groups fed a high‐fat diet rich in SFA. Moreover, pigs from the groups D2 and D3 consumed an extra inulin supply (7% of daily feed intake) from 85 to 120 days of age (for 5 weeks) and from 50 to 120 days of age (for 10 weeks) respectively. The addition of inulin to the diet reduced meaty odour and flavour significantly, improved tenderness and overall sensory quality of pork and additionally influenced ultimate pH, L* colour parameter, lactate level and protein content in meat. The diets also affected the profile of sarcoplasmic proteins. Significant effects were observed for the following enzymes—PK/PGI (pyruvate kinase/phosphoglucose isomerase) and ALD (aldolase), which are related to the intensity of post‐mortem glycolysis. Presented data indicate that long‐term inulin supply to high‐fat diet has a positive effect on technological and sensory quality as well as protein profile of pork.     

Improvement of the gelling properties of meat emulsion gel by the addition of porcine sarcoplasmic proteins

The effects of porcine sarcoplasmic proteins (SP) on the physicochemical properties of meat emulsion gel were examined. Meat emulsion was prepared from water‐washed pork meat (WWM), corn oil and SP. Whole SP (W‐SP) enhanced the breaking stress of the WWM emulsion gel as well as other animal proteins in the presence of 0.2 mol/L NaCl. The breaking stress of the emulsion with W‐SP increased with an increase in corn oil content. Furthermore, this tendency was more noticeable at a lower NaCl concentration (0.15 mol/L) rather than at 0.45 mol/L NaCl. Ammonium sulfate (AS) treatment fractionated W‐SP into three portions (SP‐f1, SP‐f2 and SP‐f3), which were the precipitates at 0–50% and 50–75% AS saturation and the supernatant at 75% AS saturation, respectively. The fractions SP‐f2 and SP‐f3 increased the gel strength more than W‐SP. In particular, the fraction SP‐f3 increased the gel strength approximately 10‐fold compared to the control. Sodium dodecyl sulfate‐polyacrylamide gel electrophoresis analysis showed that SP‐f3 had several kinds of proteins and a main protein with a molecular mass of 35 kDa, which corresponded to glyceraldehyde 3‐phosphate dehydrogenase. These results indicate that the influence of SP should not be ignored when processing of low‐salt meat products and the fraction SP‐f3 has a gel‐enhancing factor for myofibrillar proteins.     

The effect of weight loss on protein profiles of gastrocnemius muscle in rabbits: a study using 1D electrophoresis and peptide mass fingerprinting

The study of physiological changes occurring during selection contributes to an improved understanding of relationships leading to efficiencies in animal production. To investigate the effects of food restriction in gastrocnemius muscle protein expression, 20% weight reduction was induced in New Zealand White (meat producing) and wild rabbits, using one‐dimensional gel electrophoresis and peptide mass fingerprinting. Lower expression levels of myosin heavy chains were found in the Wild Rabbits Restricted Group, while myosin light chain and α‐crystallin proteins were not detected in restricted groups. Glyceraldeyde‐3‐phosphate dehydrogenase and glycogen phosphorylase expression levels were similar for all experimental groups. Phosphopyruvate hydratase β was not detected in the wild rabbit restricted diet group. Pyruvate kinase levels were 50% lower in the New Zealand Restricted group. LIM protein detection was absent in the control New Zealand group. Results also show relevance of actin in preserving muscle structure in depressed food availability, the sensitivity of both myosin light chain and α‐crystallin protein to restricted feed and the role of PK in the resistance of New Zealand rabbits to food restriction.     

Effect of chopping time and heating on 1H nuclear magnetic resonance and rheological behavior of meat batter matrix

The effect of chopping time and heating on physicochemical properties of meat batters was investigated by low‐field nuclear magnetic resonance and rheology technology. Cooking loss and L* increased while texture profile analysis index decreased between chopping 5 and 6 min. The relaxation time T₂₁ (bound water) and its peak area ratio decreased, while the ratio of T₂₂ peak area (immobilized water) in raw meat batters gradually increased with the extension of chopping time. However, T₂₂ was opposite after being heated and a new component T₂₃ (free water) appeared (T_2i is the spin – spin relaxation time for the ith component.). The initial damping factor (Tan δ) gradually decreased and there were significant difference between 4 and 5 min of chopping time. There were significantly positive correlations between the ratio of peak area of T₂₂ and chopping time, the storage modulus (G′), cooking loss, and L*, respectively. Continued chopping time could improve the peak area proportion of T₂₂ in raw meat batters. Further, the higher the peak area proportion of T₂₂ in raw meat batters, the cooking loss of heated meat gel was higher. Also, the stronger the mobility of immobilized water in meat batter, the higher the L* of the fresh meat batters. Thus, it is revealed that the physicochemical properties of meat batter are significantly influenced by chopping time which further affects the water holding capacity and the texture of emulsification gel.     

Proteome analysis of whole and water‐soluble proteins in masseter and semitendinosus muscles of Holstein cows

To assess both quantitative and qualitative differences between the slow‐ and fast‐type muscles, masseter (slow) and semitendinosus (fast) from four Holstein cows were analyzed by two‐dimensional difference gel electrophoresis (2D DIGE) and mass spectrometry. The proteome analysis identified 27 spots as 20 proteins in the whole protein fraction extracted with 8 mol/L urea solution, and 16 spots were identified as 11 proteins in the water‐soluble protein fraction. Two slow‐type myofibrillar proteins (myosin light chain‐1 slow‐b and myosin light chain‐2 slow), and aconitase‐2 mitochondria were present at higher levels in the masseter muscle (P < 0.05). Four fast‐type myofibrillar proteins (myosin light chain‐1 fast, myosin light chain‐2 fast, myosin light chain‐3 fast and tropomyosin‐1), and three enzymes of glycolytic pathway (enolase‐3, aldolase‐A and triosephosphate isomerase), were present at higher levels in the semitendinosus muscle (P < 0.05). Our proteome analysis showed that the composition of sarcoplasmic proteins as well as myofibrillar proteins was clearly different between slow‐ and fast‐type muscles.     

Influence of stewing time on the texture,ultrastructure and in vitro digestibility of meat from the yellow‐feathered chicken breed

This study assessed the influence of stewing (1, 2 or 3 h) on the texture, ultrastructure and in vitro digestibility of meat from the yellow‐feathered chicken, which is a popular broiler chicken in Asia. Results indicated that longer stewing considerably increased cooking loss of the chicken carcass and tenderness of thigh meat. After 3 h of stewing, protein digestibility decreased from 90.5% to 80.3% and fiber diameter decreased by 8.63 μm. The shear force value of breast meat decreased from 32.34 N at 1 h to 10.29 N at 2 h, and then increased to 39.98 N at 3 h. The texture profile of breast meat remarkably decreased during stewing. Moreover, increased stewing time induced longitudinal and transversal shrinkage of muscle fibers and the degradation of the myosin heavy chain. These findings suggested that prolonged stewing (3 h) resulted in decreased meat qualities, based on the changes in cooking loss, digestibility and texture profile, but that stewing for 2 h increased thigh and breast tenderness. Producers could utilize this information to stew yellow‐feathered chicken meat with desirable qualities.     

The influence of fig proteases on the inhibition of angiotensin I‐converting and GABA formation in meat

The purposes of this research were to use fig protease for texture tenderizing, and to inhibit angiotensin I‐converting enzyme (ACE) action and γ‐aminobutyric acid (GABA) formation of meat. Liberated peptides by the enzymatic action of fig protease in processing meat and free amino acids were determined and ACE inhibitory activity was assayed. Meat treated with fig protease became tender as indicated by shear force value (SFV) which was half of those of non‐fig treated meat during storage even at 5°C. Liberated peptides, free amino acids and GABA increased while extremely low levels of Glu were detected after storage. The optimal temperature of fig protease against meat was 80°C. However, the activity of fig protease decreased after pre‐heating more than 40°C. High ACE inhibitory activity of a mixture of fig and meat was found around 80°C, and the value corresponded to the amount of liberated peptide. A lot of liberated peptides were found at 60–80°C and pasterization of meat product becomes convenient to produce peptides. Production of ACE inhibitory peptides and GABA can be expected as the healthy functional meat product such as antihypertensive activity and improve brain function.     

N‐Acetyl‐d‐galactosamine prevents soya bean agglutinin‐induced intestinal barrier dysfunction in intestinal porcine epithelial cells

Soya bean agglutinin (SBA) is a glycoprotein and the main anti‐nutritional component in most soya bean feedstuffs. It is mainly a non‐fibre carbohydrate‐based protein and represents about 10% of soya bean‐based anti‐nutritional effects. In this study, we sought to determine the effects of N‐Acetyl‐D‐galactosamine (GalNAc or D‐GalNAc) on the damage induced by SBA on the membrane permeability and tight junction proteins of piglet intestinal epithelium (IPEC‐J2) cells. The IPEC‐J2 cells were pre‐cultured with 0, 0.125 × 10^?4, 0.25 × 10^?4, 0.5 × 10^?4, 1.0 × 10^?4 and 2.0 × 10^?4 mmol/L GalNAc at different time period (1, 2, 4 and 8 hr) before being exposed to 0.5 mg/ml SBA for 24 hr. The results indicate that pre‐incubation with GalNAc mitigates the mechanical barrier injury as reflected by a significant increase in trans‐epithelial electric resistance (TEER) value and a decrease in alkaline phosphatase (ALP) activity in cell culture medium pre‐treated with GalNAc before incubation with SBA as both indicate a reduction in cellular membrane permeability. In addition, mRNA levels of the tight junction proteins occludin and claudin‐3 were lower in the SBA‐treated groups without pre‐treatment with GalNAc. The mRNA expression of occludin was reduced by 17.3% and claudin‐3 by 42% (p < 0.01). Moreover, the corresponding protein expression levels were lowered by 17.8% and 43.5% (p < 0.05) respectively. However, in the GalNAc pre‐treated groups, occludin and claudin‐3 mRNAs were reduced by 1.6% (p > 0.05) and 2.7% (p < 0.01), respectively, while the corresponding proteins were reduced by 4.3% and 7.2% (p < 0.05). In conclusion, GalNAc may prevent the effect of SBA on membrane permeability and tight junction proteins on IPEC‐J2s.     

The solubilization of myofibrillar proteins of vertebrate skeletal muscle in water

Myofibrillar proteins of vertebrate skeletal muscles are insoluble in solutions of ionic strength that approximate physiological conditions. We established a method to solubilize more than 80% of chicken breast muscle myofibrillar proteins in water for the use of meat as a source of food protein. SDS‐polyacrylamide gel electrophoretic patterns of water‐soluble myofibrillar proteins demonstrated that all identified myofibrillar proteins except connectin/titin were soluble in water. A part of α‐actinin was released from myofibrils by repeated washing with 2.5 mmol/L NaCl and 5 mmol/L L‐histidine solution, and subsequent destruction of connectin/titin in washed myofibrils by ultrasonication resulted in solubilization of a large fraction of chicken breast muscle myofibrillar proteins in water. Myofibrillar proteins of chicken leg, pork loin, beef shoulder loin, and lamb were also solubilized in water using this procedure.     

The effect of dietary supplementation with the natural carotenoids curcumin and lutein on pigmentation,oxidative stability and quality of meat from broiler chickens affected by a coccidiosis challenge

1. An experiment was performed to evaluate the effectiveness of the antioxidants curcumin (CRM) and lutein (LTN) on the quality of meat from coccidiosis-infected broilers. A total of 200 one-day-old Arbor Acre chicks were randomly assigned to a treatment group with 5 replicates. The treatments included a basal diet without carotenoid supplementation (control), with 300 mg/kg CRM, with 300 mg/kg LTN or with a combination (C + L) of 150 mg/kg CRM and 150 mg/kg LTN. All chickens were challenged with Eimeria maxima at 21 d old.

2. The results revealed that the coccidiosis reduced redness of meat, while supplementation with carotenoids improved the fresh meat’s redness (a*) and yellowness (b*) and contributed to colour stability maintenance after storage (1 month at ?18°C and 3 d at 4°C).

3. Coccidiosis did not produce lipid and protein oxidation in fresh meat, but after storage for one month, the malondialdehyde levels and carbonyl contents were lower in the CRM and C + L birds and the sulfhydryl contents were higher in C + L birds.

4. The sodium dodecyl sulphate–polyacrylamide gel electrophoresis banding pattern showed equivalent myosin chain fragmentations in all treatment groups, whereas lower intensity actin bands were observed in the control group (CONT). Moreover, myofibril protein denaturation (differential scanning calorimetry) profiles showed a reduction in the CONT myosin and actin peaks. Coccidiosis reduced the meat’s water holding capacity in non-supplemented chicken meat and was improved by natural carotenoid.

5. These results emphasise that coccidiosis did not decrease the eating quality of fresh meat, that natural carotenoids are efficient antioxidants and that CRM (300 mg/kg) fed individually or combined with LTN was the most effective supplemented antioxidant compound.     

Sarcoplasmic Reticulum Ca2+-ATPase Activity and Glycogen Content in Various Fiber Types after Intensive Exercise in Thoroughbred Horses

To find a new parameter indicating muscle fitness in Thoroughbred horses, we examined time-dependent recovery of glycogen content and sarcoplasmic reticulum (SR) Ca²⁺-ATPase activity of skeletal muscle after intensive treadmill running. Two repeated 50-sec running sessions (13 m/sec) were performed on a flat treadmill (approximately 90%VO₂max). Muscle samples of the middle gluteal muscle were taken before exercise (pre) and 1 min, 20 min, 60 min, and 24 hr after exercise. Muscle fiber type composition was determined in the pre muscle samples by immunohistochemical staining with monoclonal antibody to myosin heavy chain. SR Ca²⁺-ATPase activity of the muscle and glycogen content of each muscle fiber type were determined with biochemical analysis and quantitative histochemical staining, respectively. As compared to the pre value, the glycogen content of each muscle fiber type was reduced by 15–27% at 1 min, 20 min, and 60 min after the exercise and recovered to the pre value at 24 hr after exercise test. These results indicate that 24 hr is enough time to recover glycogen content after short-term intensive exercise. The mean value of the SR Ca²⁺-ATPase activity showed a slight decrease (not significant) immediately after exercise, and complete recovery at 60 min after exercise. There were no significant relationship between the changes in glycogen content of each muscle fiber type and SR Ca²⁺-ATPase. Although further studies are needed, SR Ca²⁺-ATPase is not a useful parameter to detect muscle fitness, at least in Thoroughbred horses.     

Effect of nano‐sized,elemental selenium supplement on the proteome of chicken liver

The nano‐sized (100–500 nm) selenium has higher bioavailability and relatively lower toxicity compared to other selenium forms. The objective of the present study was to compare liver proteome profiles of broiler chicken fed with control diet without Se supplementation and diet supplemented with nano‐Se with 4.25 mg/kg DM. Differential proteome analyses were performed by two‐dimensional gel electrophoresis (2D‐PAGE) followed by tryptic digestion and protein identification by liquid chromatography–mass spectrometry (LC‐MS). Seven hundred and eight spots were detected, and 18 protein spots showed significant difference in their intensity (p < 0.05) between the two groups. In response to nano‐Se supplementation, the expression of 8 proteins was higher, and 5 proteins were lower in nano‐Se supplemented group compared to control group. The functions of the differentially expressed proteins indicate that the high dose of selenium supplementation induced a dietary stress. Selenium supplementation may influence the metabolism of fatty acids and carbohydrates and antioxidant system, and increase the quantity of cytoskeletal actin and the expression of actin regulatory protein as well.