Postmortem Tenderization Research Articles

Involvement of MMP-9 in collagen degradation of sea bass (Lateolabrax japonicus): Cloning, expression, and characterization.

Disintegration of intramuscular connective tissue is responsible for postmortem tenderization of fish muscles during chilled storage. Matrix metalloproteinase-9 (MMP-9) was reported to be involved in this process, whereas the mechanism has not been revealed. In the present study, purified type I and V collagens from the connective tissues of sea bass (Lateolabrax japonicus) muscles were first prepared. These two kinds of collagens comprise three polypeptide chains (α), forming a typical triple-helical domain as determined by circular dichroism. The complete coding region of MMP-9 containing an open reading frame of 2070bp encoding 689 amino acid residues was then cloned. The recombinant MMP-9 catalytic domain (rcMMP-9) was expressed in Escherichia coli and exhibited high hydrolyzing activity toward gelatin. Besides, rcMMP-9 was effective in degrading type V collagen rather than type I collagen at 4°C. The enzymatic activity of rcMMP-9 was highly pH-dependent, and its enzymatic activity under neutral and basic conditions was higher than that under acidic conditions. Metal ion Ca2+ was necessary for the maintenance of rcMMP-9 activity, whereas Zn2+ inhibited its activity. Our present study indicated that MMP-9 is responsible for the disintegration of intramuscular connective tissues by cleaving type V collagen during postmortem tenderization of fish muscle. PRACTICAL APPLICATION: Elucidation the involvement of MMP-9 in collagen degradation will deliver a reference for the prevention of muscular protein decomposition during chilled storage of fish fillets.

ITRAQ-based proteomic analysis reveals the underlying mechanism of postmortem tenderization of refrigerated porcine Longissimus thoracis et lumborum muscle

The isobaric tags for relative and absolute quantitation (iTRAQ) technology was used for differential proteomic analysis of refrigerated porcine Longissimus thoracis et lumborum (LTL) muscle at different time points postmortem (45 min, 4 h, 8 h, 12 h, 24 h, 48 h, 72 h and 96 h) to mechanistically elucidate the postmortem tenderization. Compared with the proteins identified in porcine LTL muscle at 45 min postmortem (control), 862 proteins were significantly expressed at 4 h, 8 h, 12 h, 24 h, 48 h, 72 h and 96 h postmortem. Moreover, clustering and path analysis showed that the quality traits of porcine LTL muscle, including pH, shear force, myofibril fragmentation index, correlated significantly with 2, 6 and 6 differentially expressed proteins, respectively, with the lowest or highest expression at 8 h or 12 h postmortem. Overall, the tenderness of refrigerated porcine LTL muscle might be significantly affected by changes in quality traits at 8 h and 12 h postmortem.

Comparison of oxidative stress-mitochondria-mediated tenderization in two different bovine muscles during aging

The aim of this study was to investigate the differences in the effects of mitochondria-involved energy metabolism and caspases activation on postmortem tenderness in different muscle fiber types. Beef Longissimus thoracis (LT) and Psoas major (PM) muscles showed significant difference in mitochondrial function. Our data revealed that PM suffered from higher levels of reactive oxygen species (ROS) earlier than LT, causing faster mitochondrial swelling and rupture. Additionally, faster metabolism of ATP-related compounds and activation of caspase-9 appeared in PM, but the activity of caspase-3 in PM was lower than that in LT. Differences in myofibril fragmentation index (MFI) of LT and PM at different aging stages suggested that energy metabolism and caspases activities may play a role in tenderness at different aging stages. These results indicated that oxidative stress-mitochondria-mediated tenderization process could be muscle-specific.

Effects of oxidation on the physicochemical properties and degradation of mutton myofibrillar proteins

Tenderness affects mutton quality and price, and the degradation of myofibrillar protein (MP) is critical to improve tenderness. We investigated the oxidative modification of mutton MP by hydroxyl radicals (OH) and the effects of this modification on the proteolysis of MP by µ-calpain. As the H2 O2 concentrations increased, the carbonyl and dityrosine contents and the surface hydrophobicity of MP all display an increasing trend, whereas the total sulfhydryl and intrinsic fluorescence intensity of MP declines significantly. SDS-PAGE electrophoresis indicates that disulfide bonds and other covalent bonds led to protein cross-linking and aggregation. After adding µ-calpain, with increasing oxidation, the degradation percentage of myosin heavy chain (MHC) increases considerably and actin degradation is promoted, while the proteolysis of troponin-T and desmin is inhibited. These data suggest that·OH can change MP physicochemical properties and its susceptibility to µ-calpain. Future investigations will focus on the effect of oxidation on the degradation of MP by other proteases, such as cathepsins and caspase and the effect of oxidation on these enzymes. PRACTICAL APPLICATION: The calpain system, particularly µ-calpain, plays a pivotal role in postmortem tenderization of meat. Protein oxidative modifications influence meat tenderness mainly by regulating proteolysis. An investigation of the effect of oxidation on the proteolytic susceptibility of MP to degradation by µ-calpain allows for the monitoring of the association between protein oxidation and meat tenderness.

Proteomic analyses of mitochondrial damage in postmortem beef muscles.

The objective of the study was to examine the expression profiles of mitochondrial proteins in at-death and 24 hpostmortem (PM) using tandem mass tag (TMT) approach to characterize the mitochondria possible mechanisms that are affiliated with tenderization. Results showed that the tender meat at 24 hPM emerged with more serious mitochondrial damage. Altogether 456 mitochondrial proteins were identified, including 442 down-regulated and 14 up-regulated proteins. These differentially-expressed proteins were primarily involved in the progress of PM energy metabolism, apoptosis, and the morphological alterations of mitochondrial. Among them, 47 subunits (such as NDUFA2, COX4I1, and ATP5PB) were annotated into the oxidative phosphorylation pathway. VDAC1, VDAC2, and VDAC3 involving in the damage of MPTP, and IMMT, CHCHD3, APOL and APOO modulating the morphology of mitochondria, and DIABLO and AIFM1 released from mitochondria affect caspase's activation. HSPD1 and HSPE1 involved in apoptosis, mitochondrial physiological and morphological alterations. The earlier-mentioned proteins were validated as potential indicators of tenderness regulated by mitochondrial damage. These results highlighted that mitochondrial damage possibly participate in PM tenderization of beef muscles by energy metabolism and cell apoptosis status. © 2022 Society of Chemical Industry.

Variations in Low Electrical Stimulator Voltage Settings Minimally Influence Beef Longissimus Muscle Slice Shear Force Values

The objective of the current study was to evaluate the effect of differing electrical stimulation (ES) voltage levels on beef longissimus muscle tenderness, postmortem temperature, pH decline, and carcass quality. Beef carcasses from 3 commercial beef processing plants (A, B, C) were exposed to 3 varying voltage levels: (1) control (no ES), (2) ES level 1 (ES1; 60 Hz for 17 s each at 16, 20, 24, and 28 V), and (3) ES level 2 (ES2; 60 Hz for 17 s each at 25, 35, 45, and 55 V) prior to chilling. Ninety beef carcasses were selected from each of the 3 plants, and within a carcass, paired sides were randomly assigned to one of 3 ES treatments (n = 60 sides/treatment/plant). The results indicated that ES affected (P < 0.05) muscle pH at 3 h postmortem in 2 of the 3 plants. However, ES did not affect (P > 0.05) pH at the time of grading (postrigor). Although the slice shear force (SSF) values were lower (P < 0.05) for ES steaks compared with controls, voltage did not affect (P > 0.05) SSF values. Variation in SSF was observed among the plants (P < 0.05), with steaks from Plant C having greater (P < 0.05) SSF values compared with steaks from Plants A and B, which exhibited similar (P > 0.05) SSF values. Overall, although ES steaks had lower SSF values compared with control steaks, the lack of difference in postmortem tenderness between ES1 and ES2 voltage settings indicated that the low ES voltages minimally influenced SSF values.

Effect of postmortem tenderization strategies (pretumbling, blade tenderization, moisture enhancement) on processing yield parameters and eating quality of selected hip and loin muscles from youthful and mature beef carcasses.

Several muscles from mature beef carcasses have been identified as failing to provide adequate tenderness required for a satisfactory consumer eating experience. Postmortem processing strategies can help improve the tenderness and subsequent eating quality of mature beef muscles. The current study was undertaken to investigate the impact of processing strategies (blade tenderization [BT], pretumbling [PT], and moisture enhancement [ME]), alone and in combination, on processing yield and eating quality-related parameters of selected loin and hip muscles (gluteus medius [GM], longissimus lumborum [LL], semimembranosus [SM], and biceps femoris [BF]) from youthful and mature beef cattle. Results indicate that muscles from mature beef were inherently less tender (P < 0.05), but some tenderization procedures produced meat that was similar in tenderness to that of youthful cattle. Of the different tenderization strategies evaluated, BT followed by ME (injection of a salt/phosphate solution) was the most effective strategy for improving (P < 0.05) tenderness of tougher muscle cuts such as BF and SM. Moisture enhancement alone improved tenderness (P < 0.05) and juiciness (P < 0.01) of SM, GM and LL, but with the exception of samples tenderized prior to injection, was not effective (P > 0.05) in BF muscles. No additional tenderization of GM and LL samples was observed (P > 0.05) by combining PT or BT with ME. Combining PT or BT with ME; however, was effective (P < 0.05) to control the increased purge loss observed following ME treatment in SM and LL muscles. Pretumbling as a single treatment was ineffective (P > 0.05) in all of the muscles, and only treatments that included BT were sufficient to effect an increase (P < 0.05) in tenderness of BF.

Tenderness-related index and proteolytic enzyme response to the marination of spent hen breast by a protease extracted from Cordyceps militaris mushroom.

ObjectiveThe effects of a crude protease extracted from Cordyceps militaris (CM) mushrooms on the postmortem tenderization mechanism and quality improvement in spent hen breast were investigated.MethodsDifferent percentages of the crude protease extracted from CM mushrooms were introduced to spent hen breast via spray marination, and its effects on tenderness-related indexes and proteolytic enzymes were compared to papain.ResultsThe results indicated that there was a possible improvement by the protease extracted from CM mushroom through the upregulation of endogenous proteolytic enzymes involved in the calpain system, cathepsin-B, and caspase-3 coupled with its nucleotide-specific impact. However, the effect of the protease extracted from CM mushroom was likely dose-dependent, with significant improvements at a minimum level of 4%. Marination with the protease extracted from CM mushroom at this level led to increased protein solubility and an increased myofibrillar fragmentation index. The sarcoplasmic protein and collagen contents seemed to be less affected by the protease extracted from CM mushroom, indicating that substrate hydrolysis was limited to myofibrillar protein. Furthermore the protease extracted from CM mushroom intensified meat product taste due to increasing the inosinic acid content, a highly effective salt that provides umami taste.ConclusionThe synergistic results of the proteolytic activity and nucleotide-specific effects following treatments suggest that the exogenous protease derived from CM mushroom has the potential for improving the texture of spent hen breast.

Lysosomal Fe2+contributes to myofibrillar protein degradation through mitochondrial-dysfunction-induced apoptosis

To verify the role of lysosomal Fe2+ in mitochondrial-dysfunction-mediated apoptosis and postmortem tenderization of bovine muscles, mitochondrial apoptotic factors, myofibrillar protein degradation, and μ-calpain activity were evaluated in the control group and the iron chelator desferrioxamine (DFO) group. The control group showed 1) increased mitochondrial swelling and lipid peroxidation by 47% and 36% at 72 h, respectively (P < 0.05), significantly higher than the DFO group at 12–24 h and 72–168 h (P < 0.05); 2) significantly increased mitochondrial Ca2+ influx at 12–24 h (P < 0.01); 3) a 15%, 24%, and 30% lower cytochrome c reduction level than the DFO group at 6–24 h (P < 0.01, P < 0.05); 4) a significantly increased caspase-3 expression level at 0–120 h (P < 0.05), where the caspase-3 activity was 30% and 49% higher than that of the DFO group at 12–24 h, respectively (P < 0.01); 5) an increased μ-calpain activity by 56% at 24–168 h (P < 0.05), and 6) 75% (P < 0.01) and 34% (P < 0.05) higher degradation of desmin and troponin-T than the DFO group at 168 h, respectively. In summary, lysosomal Fe2+ facilitates postmortem tenderization by promoting the mitochondrial-dysfunction-induced apoptosis of bovine muscle.

Changes in proteolytic enzyme activities, tenderness-related traits, and quality properties of spent hen meat affected by adenosine 5′-monophosphate during cold storage

A mechanism of postmortem tenderization by adenosine 5′-monophosphate (AMP) on spent hen meat was investigated. Breast meat samples were made into a rectangular size of 7.5 × 5 × 2 cm and grouped into 5 different treatments, followed by immersion for 24 h at 4 ± 2°C in AMP marinade solutions of 0, 15, 30, 45, and 60 mmol/L that dissolved in 0.9% (w/v) saline solution. To investigate the enzymatic changes and tenderness-related traits, samples were stored until day 5 at a temperature of 2 ± 2°C. Result showed that each increase of 15 mmol/L AMP within marinade solution remarkably improved the myofibril fragmentation index and texture properties. The upregulation of tenderness-related enzymes was found for caspase-3 at 1 to 20.4 fold and 1 to 1.2 fold higher for the cathepsin-B, while a slight effect on calpains enzyme was observed. When compared with day 0 as a reference sample, the activity of the caspase-3 enzyme was more stable, as was cathepsin-B on the ultimate storage day, while the calpains enzyme showed a declining activity even after treatment. The flavor enhancement of 2.16- to 5.10-fold seemed to be a consequence of the AMP conversion into IMP that was responsible for the intensification of the umami-like flavor. No adverse effect was observed for instrumental surface color during the postmortem period. Therefore, this study suggested that the synergistic results after AMP treatment strongly contributed to postmortem tenderization mainly through cathepsin-B and caspase-3 enzyme upregulation, which led to more myofibrillar fragmentation and structural alteration of myofibrillar protein.

Genetic diversity, population structure of seven Indian domestic goat breeds based SNPs identified in CAPN1 gene

The micromolar calcium-activated neutral protease (CAPN1) gene encodes μ-calpain that degrades myofibril proteins under the post-mortem conditions which appears to be the primary enzyme in the postmortem tenderization process, hence affecting the meat quality. Objective of this study was to analyze genetic polymorphism of the CAPN1 gene in seven diverse Indian goat breeds. Direct DNA sequencing was carried out to identify the genetic polymorphisms in 84 unrelated goats representing seven different goat breeds (Barbari, Beetal, Ganjam, Sirohi, Black Bengal, Osmanabadi and Malabari). Six single nucleotide polymorphisms (SNPs) were identified in CAPN1 gene intron 17. The observed heterozygosity (Ho) was highest (0.50) in Sirohi and Osmanabadi (0.42) breeds and lowest in Black Bengal (0.06) breed. The expected heterozygosity (He) was highest (0.45) in Sirohi followed by Osmanabadi (0.37), Barbari (0.34) and Beetal (0.37). The allele frequencies ranged from 0.083 to 0.917 and the major allele frequencies ranged from 0.595 (locus 6499 T/C) to 0.917 (locus 6529 T/C). In Black Bengal, polymorphism at all theloci was fixed with the exception of 6417 T/G and 6533C/G. The identity values oscillated from 0.7866 to 0.9593. The Nei's genetic distances were below 0.0294. Genetic diversity among different goat meat breeds indicates possible role in meat quality trait. Allelic diversity at this locus could be used in further for the association between gene polymorphism and enzyme activity as well as caprine meat quality traits.

Effect of wooden breast on postmortem changes in chicken meat

Wooden breast is a common problem in the poultry industry, occurring when broiler breast meat becomes rubber-like and extremely hard. Unclear points remain regarding the mechanical strength changes caused by post-mortem biochemical changes in wooden breasts. This study aimed to investigate this knowledge gap. We found endogenous protease activity to be high in wooden breasts and observed a 30 kDa fragment of troponin T (an indicator of postmortem tenderness) from day 1 postmortem. The amount of intramuscular connective tissue in wooden breasts was greater than that of normal breast meat, particularly in the perimysium. The intramuscular connective tissue structure and quantity significantly affect the mechanical strength of meat. It became clear that the wooden breasts are much more mechanically stronger than normal breasts at postmortem day 5 because the large amount of intramuscular connective tissue in the wooden breasts has hardly changed even 5 days postmortem.

Investigation of the relationships between different enzymes and postmortem duck muscle tenderization

Postmortem tenderization is induced by the cooperation of various related enzymes. In this study, CaCl2 and MDL-28170 (Cbz-Val-Phe-H, a calpain inhibitor) were used to regulate the postmortem tenderization process of duck breast muscle. Then the relationship between muscle tenderness change and different enzymes was investigated. At day 0, day 1, and day 4 of the postmortem ageing, the shear force, myofibril fragmentation index (MFI), enzymatic activities of calpains, cathepsin-B, caspase-3, Na+/K+-ATPase, and Ca2+-ATPase were respectively determined. The results showed that duck muscle tenderness could be significantly raised by CaCl2 and reduced by MDL-28170, respectively (P < 0.05). The CaCl2 treatment did not promote the calpains activity as predicted (P > 0.05), but significantly up-regulated the activity of cathepsin-B (P < 0.05). The MDL-28170 significantly inhibited the activity of the calpain system at day 1 (P < 0.05) and raised the activities of the selected 3 apoptosis-related enzymes, including caspase-3, Na+/K+-ATPase, and Ca2+-ATPase, at both day 1 and day 4 (P < 0.05). These data indicated that in duck, the calpain system could be well activated after death, and cathepsin-B might also play an important role in postmortem muscle tenderization. The caspase-3, Na+/K+-ATPase, and Ca2+-ATPase probably have no significant effects on duck muscle tenderness. It might provide useful information for duck production and further research on postmortem muscle tenderization.

Application of proteomic to investigate the post-mortem tenderization rate of different horse muscles

The aim of this study was to evaluate the effect of post-mortem aging on tenderness development and proteolysis of myofibrillar proteins in 3 different horse muscles. Warner–Bratzler shear force decreased during aging in all muscles, showing the lowest values in longissimus lumborum (LL) in all sampling points. Myofibril fragmentation index significantly increased in LL and semimembranosus (SM) muscles throughout aging time whereas in semitendinosus (ST) it increased after 14 days of aging. Proteomics analysis revealed the major content of intact myofibrillar proteins with high molecular weight in ST muscle in the first phase of aging, while, after 14 days a higher accumulation of TnT-derived polypeptides and spots isoforms ascribed to MLC2 and MLC1 proteins were found. Data highlight that aging affects the meat tenderness and proteolysis with different intensities in each muscle and suggest that a more extensive post-mortem proteolysis occurred in ST muscle.

Effects of high-pressure processing on taste-related ATP breakdown compounds and aroma volatiles in grass-fed beef during vacuum aging.

ObjectiveThis study aimed to observe whether high-pressure processing (HPP) affected aroma development and the degradation rate of umami taste-related ATP breakdown products, specifically inosinic acid in grass-fed beef during vacuum aging.MethodsStrip loin (longissimus lumborum) cuts obtained from six grass-fed Friesian Holstein steers (32 months old) on day 4 post slaughter were vacuum-packed and subjected to pressurization at 300 and 500 MPa for 180 s at 15°C±2°C. The samples were then stored for 4 weeks at 5°C±0.5°C under vacuum and compared with the control (0.1 MPa).ResultsHPP increased the shear force value, promoted moisture loss and lipid oxidation, induced surface paleness, stabilized pH during aging, and reduced bacterial load and growth. The shear force value of 500 MPa-treated samples remained higher than the control after aging, while no significant differences were found between the control and 300 MPa-treated samples. Degradation of inosinic acid and inosine occurred during pressurization, resulting in an increase in hypoxanthine content. However, the degradation rate in HPP-treated samples during aging was slower; therefore, inosinic acid and inosine content remained higher than in control samples. No significant differences were found in hypoxanthine content at the end of aging. HPP intensified the levels of hexanal, octanal, 2-methylbutanal, 3-methylbutanal, benzaldehyde, and 2,5-dimethylpyrazine in cooked-aged beef samples.ConclusionHPP induced aroma development and delayed the degradation of inosinic acid. However, it also reduced the postmortem tenderization rate.

Effect of Proteolytic Enzymes and Ginger Extract on Tenderization of M. pectoralis profundus from Holstein Steer.

The effects of proteolytic enzymes (bromelain and bromelain+papain) and a ginger extract were assessed on collagen content and solubility, thermal shrinkage temperature of connective tissue, pH, cooking loss, drip loss, and Warner-Bratzler shear force (WBSF) of M. pectoralis profundus isolated from the beef brisket cut. Both proteolytic enzymes and ginger extract led to a significant increase in cooking loss and collagen solubility compared with untreated controls. On the other hand, the peak (Tp) thermal shrinkage temperature markedly decreased in all treatments compared with those in controls. Samples treated with bromelain, bromelain + papain, and ginger extract showed a significant decrease in WBSF by 36%, 40%, and 37%, respectively, compared with untreated controls. Our findings suggest that ginger extract are useful for postmortem tenderization of meat containing high levels of collagen, compared to control even though, bromelain and bromelain + papain treatments have higher collagen solubility than ginger extract.

Effect of postmortem storage on shear force value and calpain/calpastatin activity in longissimus dorsi muscle of rusa deer (cervus timorensis)

The objective of this study was to determine the effects of aging period on shear force values and activities of calpain/calpastatin enzymes of the longissimus dorsi (LD) muscle from rusa deer (Cervus timorensis). The shear force values were measured with instron materials testing machine. Results showed that postmortem storage influenced meat tenderness with a highly significant reduction of shear force value from 9.01±0.83 kg/cm2 at day 1 to 4.34±0.10 kg/cm2 at day 21 (P&lt;0.01). Determination of the enzyme activities indicated that the μ-calpain activity decreased significantly from 1.50±0.42 to 0.19±0.28 units/g of meat (P&lt;0.01), whereas m-calpain activity (22.88±9.64 to 16.95±8.34 units/g of meat) and calpastatin activity (9.93±2.37 to 6.82±2.96 units/g of meat) slightly decreased (P&gt;0.05). Shear force values were significant correlated with higher levels of μ-calpain (r=0.915) and m-calpain (r=0.758), respectively. However, the values were not significant related to the calpastatin activity (r=0.462). Therefore, this study confirmed that in the case of rusa deer, μ-calpain is a key factor controlling postmortem meat tenderness compared to m-calpain and calpastatin. The results suggested that storage of the rusa deer meat for 7 days is enough to achieve aging of the LD muscle, which may help to reduce the cost of meat production.

Sarcoplasmic Reticulum Membrane Instability Caused by Dietary Fat Source May Affect Early Postmortem Tenderization of Beef

Sarcoplasmic Reticulum Membrane Instability Caused by Dietary Fat Source May Affect Early Postmortem Tenderization of Beef

Assessment of the textural variation of iced stored Anabas testudineus (Bloch, 1792) muscle tissue with emphasis on their collagen and myofibrillar protein content.

Post-mortem biochemical and physiological changes of climbing perch (Anabas testudineus) muscle evaluated during iced storage of 18days compared with muscle protein content. Changes in the protein fractions, rigor index, pH value, water holding capacity, expressible water content, cook loss, textural parameters, and histochemical properties of the post mortem fish muscle were studied. The whole fish were in full rigor condition till fifth day of storage. Initial muscle pH value of 6.97 was dropped to 6.90 when the fish reached in full rigor condition, this then increased to 7.10 on the final day of storage period. The myofibrillar protein decreased with an initial value of 29.76% and a final value of 13.49%. 40.27% decrease in total collagen content was observed during the storage period. The water holding capacity of fish muscle decreased when the fish muscle entered in post rigor stage while cook loss and expressible water content were significantly increased. The histochemical studies and textural profile analysis of fish muscle proved that the degradation of both collagen and myofibrillar protein induces the post-mortem tenderization and the resultant quality deterioration of iced stored Anabas testudineus fish.

Association analysis of g.68G → A SNP in CAPN1 gene with carcass and meat quality traits in goose raised in organic &amp;lt;i&amp;gt;dehesa&amp;lt;/i&amp;gt;

Abstract. Meat quality is an important concern for the poultry industry. Domestic geese products obtained from free-range systems usually have rather tough meat, and it is necessary to select them to improve meat tenderness. The relation of the calpain 1 (CAPN1) gene with the post-mortem tenderness process of meat has been demonstrated in several species. Thus, the objective of the present study was to identify polymorphisms in this gene and to perform an association analysis between these polymorphisms and related economic traits in goose raised in the dehesa ecosystem. For the analysis, 50 geese of 3 different subpopulations (20 Embden Anser anser; 20 Toulouse Anser anser; 10 F1 cross) were studied. The experimental protocols were followed complying with principles of animal welfare. A novel SNP was found in the CAPN1 gene, g.68G → A. This polymorphism was statistically associated with different carcass and meat quality traits such as thigh muscle width (P = 0.020) and the b* 10-day meat colour parameter (P = 0.024) for the global goose population. The association of this gene with meat tenderness (Warner–Bratzler shear force) was confirmed in the case of female individuals of the Toulouse breed (P = 0.043). The results suggest the possibility of using molecular markers in CAPN1 gene as a potential tool for improving carcass and meat quality traits in goose breeding programmes.