Impact of polymorphism of the regulatory subunit of the μ-calpain (CAPN1S) on the proteolysis process and meat tenderness of young cattle

Abstract

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.

The relationship between protein changes in porcine longissimus muscle at different courses of meat tenderisation

“…There was also better tenderness of the bovine longissimus dorsi muscle of four cattle breeds (Polish Holstein-Friesian, Polish Red, Hereford and Limousine). It was characterised by the largest percentage of MHC isoform type IIa as well as the effect of the µ-calpain (CAPN1S) gene as a factor determining meat tenderness [24]. Differences in MHC isoforms may also be related to changes in the waterholding capacity of meat [18].…”

“…Usually the tenderisation process is described as the result of protein changes which take place during storage [2,4,9,10,29,30,36,42]. It is evident from literature data that the rate of muscle protein degradation depends on a number of factors, such as the age of animals [21], their genotype [11,24,27,43,45] and meatiness [38,50] as well as the proximate composition of muscles [6-8, 34, 41], being the most important ones. These changes can be associated with breeding and rearing conditions [18,27,54].…”

Polymorphisms of the CAPN1, CAST and MSTN Genes, and Their Association with Histological and Textural Parameters of Beef from Polish Holstein-Friesian Cattle

“…In researches of Iwanowska et al [13] the changes in the tenderness score following varying intervals after the slaughter (48, 96 and 240 h), taking into account the genotype were determined. Based on an analysis of the shear force, it was determined that animals with two C alleles were characterised by the lowest meat tenderness.…”

Theories concerning natural tenderization processes in post mortem meat

“…Wskazuje się również na to, że geny kodujące ww. enzymy (jako geny kandydujące) mogą być rów-nież zmiennymi kruchości mięsa [11,31,35].…”