ArticleAnimal bioscience2025
Type I and III collagen contents and μ-calpain autolysis as a function of dry ageing time for eight different muscles from Hanwoo cattle.
Article in Animal bioscience, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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1 citing paper in PubMed.
- Dry-Aged Beef: A Global Review of Meat Quality Traits, Microbiome Dynamics, Safety, and Sustainable Strategies.Journal of food science · 2025Review
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Abstract
objectiveType I and III collagen content exert contrasting influences on meat tenderness. μ-calpain autolysis correlates with beef tenderness. Thus, the study aimed to determine the changes in these proteins.
methodsThree hundred twenty-four Hanwoo cattle, including cows and steers, and eight muscles were evaluated for proteolysis during dry ageing period. The ratios of type I and III collagen were determined by densitometric scans of bands resolved by sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis (PAGE), and μ-calpain activity was determined using casein zymography. Proteins involved in proteolysis were analysed by liquid chromatography-tandem mass spectrometry.
resultsThe ratio of type I and III collagen in every muscle showed a significant difference with increasing ageing times (p<0.05). In steers, the ratio decreased with increased ageing time, and in cows, except for Biceps femoris and Diaphragm muscles, a similar trend was observed. Significant differences in the ratio of type I and III collagen were found between different muscles of cows at the same ageing time (p<0.05), but no significant differences were found in steer muscles at the same ageing time (p>0.05). Casein zymogram results showed an inverse relationship between pH values and μ-calpain autolysis in every muscle. A significant reduction in μ-calpain activity was observed in all muscles with extended ageing times, while the rate of autolysis differed greatly (p<0.05) between muscles at the same ageing time. Interestingly, electropherogram analysis showed that cow muscles had a higher μ-calpain activity than steer muscles. Ageing time significantly influenced proteolysis, with 24 proteins showing marked changes.
conclusionThe ageing times significantly affect the ratio of type I and III collagen, coinciding with μ-calpain autolysis rates in steers. The ratio of type I and III collagen had a significant changes during the ageing period from cows, which may be related to the amount of collagen cross-linking.
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