of the meat tenderness using canonical correlation analysis. Based on the percentage participation of the selected muscle tissue and centrifugal drip proteins and measurements of pH and EC at specified time pm it was possible to predict tenderness with a very high probability, even 89%.
The objective of this study was to estimate the impact of the polymorphism of μ-calpain (CAPN1S) gene on protein changes of the cattle muscle tissue and its tenderness during 10-day cold storage. The analysis was performed on the longest dorsal and lumbar muscles collected from 76 bulls 6 to 12 months of age. Polymorphism identification of the above-mentioned gene was conducted using the PCR-RFLP technique. Its effect on the course of the proteolysis process was assessed by monitoring changes in proportions of tissue proteins during 10-day process of meat ageing. Special attention was focused on changes in native titin (T1) share and products of its degradation (proteins of molecular weight (m.w.) of 2400 and 200 kDa), α-actinin and protein of 37 kDa as well as myosin heavy chains (MHC). In the case of the last proteins, their polymorphism was evaluated as well. Meat tenderness was estimated measuring the value of shear force and sensorially. The highest tenderness was ascertained for the heterozygote. Its improvement was associated with a significant decrease in proportions of proteins of molecular weight of approximately 37 kDa accompanied by an increase of those with 200 kDa molecular weight. Muscles derived from cattle of CT genotype were characterised by the highest proportions of type 2a MHC isoform. Value differences between proportions determined for the heterozygote and CC and TT homozygotes of the CAPN1S gene were statistically significant. Therefore, it can be presumed that the process of meat tenderisation was especially connected with MHC polymorphism.
Abstract. The aim of the investigations was to analyse the share of myosin heavy chains (MHC) isoforms (type I, IIa, IIb, and IIx) in the longissimus thoracis et lumborum muscle derived from pigs of different RYR1 genotypes (TT – homozygous negative, CT – heterozygous, CC – homozygous positive). The composition of the MHC isoforms in the muscle tissue of the examined animals was referred to selected meat quality traits. It was revealed that the animals with the CT and TT genotypes were characterized by a significantly (P≤0.05) lower share of the type I and higher share of the type IIb MHC isoform in comparison to homozygotes CC. Inferior tenderness and water holding capacity of meat obtained from pigs susceptible to stress (TT) at 144 h after slaughter could have been associated, among others things, with the increased share of MHC isoform type IIb. The composition of MHC isoforms might be a useful indicator in breeding work in the selection of animals carrying the gene of susceptibility to stress.
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