Type I and III collagen contents and μ-calpain autolysis as a function of dry ageing time for eight different muscles from Hanwoo cattle
Objective Type 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. Methods Three hundred twenty-four Hanwoo cattle, including cows and steers, and eight musc...
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Asian-Australasian Association of Animal Production Societies
2025-05-01
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| Series: | Animal Bioscience |
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| Online Access: | http://www.animbiosci.org/upload/pdf/ab-24-0376.pdf |
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| author | Zhen Song Inho Hwang |
| author_facet | Zhen Song Inho Hwang |
| author_sort | Zhen Song |
| collection | DOAJ |
| description | Objective Type 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. Methods Three 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. Results The 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. Conclusion The 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. |
| format | Article |
| id | doaj-art-7dc3dd51b2d94f98ac9aae5b7f024c5a |
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| issn | 2765-0189 2765-0235 |
| language | English |
| publishDate | 2025-05-01 |
| publisher | Asian-Australasian Association of Animal Production Societies |
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| series | Animal Bioscience |
| spelling | doaj-art-7dc3dd51b2d94f98ac9aae5b7f024c5a2025-08-20T02:16:10ZengAsian-Australasian Association of Animal Production SocietiesAnimal Bioscience2765-01892765-02352025-05-013851041105210.5713/ab.24.037625363Type I and III collagen contents and μ-calpain autolysis as a function of dry ageing time for eight different muscles from Hanwoo cattleZhen Song0Inho Hwang1 College of Animal Science and Technology, Henan University of Science and Technology, Luoyang, China Department of Animal Science, Chonbuk National University, Jeonju, KoreaObjective Type 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. Methods Three 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. Results The 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. Conclusion The 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.http://www.animbiosci.org/upload/pdf/ab-24-0376.pdfdry ageingtendernesstype i and iii collagenμ-calpain autolysis |
| spellingShingle | Zhen Song Inho Hwang Type I and III collagen contents and μ-calpain autolysis as a function of dry ageing time for eight different muscles from Hanwoo cattle Animal Bioscience dry ageing tenderness type i and iii collagen μ-calpain autolysis |
| title | Type I and III collagen contents and μ-calpain autolysis as a function of dry ageing time for eight different muscles from Hanwoo cattle |
| title_full | Type I and III collagen contents and μ-calpain autolysis as a function of dry ageing time for eight different muscles from Hanwoo cattle |
| title_fullStr | Type I and III collagen contents and μ-calpain autolysis as a function of dry ageing time for eight different muscles from Hanwoo cattle |
| title_full_unstemmed | Type I and III collagen contents and μ-calpain autolysis as a function of dry ageing time for eight different muscles from Hanwoo cattle |
| title_short | Type I and III collagen contents and μ-calpain autolysis as a function of dry ageing time for eight different muscles from Hanwoo cattle |
| title_sort | type i and iii collagen contents and μ calpain autolysis as a function of dry ageing time for eight different muscles from hanwoo cattle |
| topic | dry ageing tenderness type i and iii collagen μ-calpain autolysis |
| url | http://www.animbiosci.org/upload/pdf/ab-24-0376.pdf |
| work_keys_str_mv | AT zhensong typeiandiiicollagencontentsandmcalpainautolysisasafunctionofdryageingtimeforeightdifferentmusclesfromhanwoocattle AT inhohwang typeiandiiicollagencontentsandmcalpainautolysisasafunctionofdryageingtimeforeightdifferentmusclesfromhanwoocattle |