{"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.","authors":"Zhen Song, Inho Hwang","doi":"10.5713/ab.24.0376","DOIUrl":null,"url":null,"abstract":"<p><strong>Objective: </strong>Type I and III collagen content exert contrasting influences on meat tenderness. μ-calpain autolysis has shown a correlation with beef tenderness. Thus, the study was designed to determine the changes in these proteins.</p><p><strong>Methods: </strong>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 SDS-PAGE, and μ-calpain activity was determined using casein zymography. Proteins involved in proteolysis were analysed by LC-MS/MS.</p><p><strong>Results: </strong>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 BF and DP muscles, a similar decreasing 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 and being identified.</p><p><strong>Conclusion: </strong>The ageing times significantly affect the ratio of type I and III collagen, which coincided with the rate of μ-calpain autolysis 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.</p>","PeriodicalId":7825,"journal":{"name":"Animal Bioscience","volume":" ","pages":""},"PeriodicalIF":2.4000,"publicationDate":"2024-10-25","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Animal Bioscience","FirstCategoryId":"97","ListUrlMain":"https://doi.org/10.5713/ab.24.0376","RegionNum":2,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q1","JCRName":"AGRICULTURE, DAIRY & ANIMAL SCIENCE","Score":null,"Total":0}
引用次数: 0
Abstract
Objective: Type I and III collagen content exert contrasting influences on meat tenderness. μ-calpain autolysis has shown a correlation with beef tenderness. Thus, the study was designed 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 SDS-PAGE, and μ-calpain activity was determined using casein zymography. Proteins involved in proteolysis were analysed by LC-MS/MS.
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 BF and DP muscles, a similar decreasing 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 and being identified.
Conclusion: The ageing times significantly affect the ratio of type I and III collagen, which coincided with the rate of μ-calpain autolysis 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.
目的Ⅰ型和Ⅲ型胶原蛋白含量对肉质嫩度的影响截然不同。因此，本研究旨在确定这些蛋白质的变化：方法：研究人员对 324 头汉和牛（包括母牛和阉牛）和八块肌肉进行了干老化期间蛋白质分解的评估。通过对 SDS-PAGE 分解的条带进行密度扫描，测定 I 型和 III 型胶原蛋白的比例，并使用酪蛋白酶谱测定μ-钙蛋白酶的活性。用 LC-MS/MS 分析参与蛋白水解的蛋白质：结果：每块肌肉中 I 型和 III 型胶原蛋白的比例随着老化时间的增加而出现显著差异（p < 0.05）。在阉牛中，该比率随着老化时间的延长而下降；在奶牛中，除 BF 和 DP 肌肉外，也观察到类似的下降趋势。在相同的老化时间内，奶牛不同肌肉中 I 型和 III 型胶原蛋白的比例存在显著差异（p < 0.05），但在相同的老化时间内，阉牛肌肉中没有发现显著差异（p > 0.05）。酪蛋白酶图结果显示，每块肌肉的 pH 值和μ-钙蛋白酶自溶之间存在反比关系。随着老化时间的延长，所有肌肉中的μ-钙蛋白酶活性都明显降低，而在相同老化时间内，不同肌肉的自溶率差别很大（p < 0.05）。有趣的是，电泳图分析表明，奶牛肌肉的μ-钙蛋白酶活性高于骏马肌肉。老化时间对蛋白质分解有明显影响，有 24 种蛋白质发生明显变化并被鉴定出来：结论：老化时间对 I 型和 III 型胶原蛋白的比例有明显影响，这与μ-钙蛋白酶在阉牛中的自溶速度一致。I型和III型胶原蛋白的比例在奶牛的老龄化过程中发生了显著变化，这可能与胶原蛋白的交联量有关。
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