Proteolytic changes of myofibrillar proteins in Podolian meat during aging: focusing on tenderness

被引:35
|
作者
Marino, R. [1 ]
della Malva, A. [1 ]
Albenzio, M. [1 ]
机构
[1] Univ Foggia, Dept Agr Food & Environm Sci, I-71121 Foggia, Italy
关键词
beef muscles; desmin; Podolian breed; post mortem aging; tenderness; troponin T; WATER-HOLDING CAPACITY; BOVINE MUSCLE; POSTMORTEM PROTEOLYSIS; BIOCHEMICAL TRAITS; SARCOMERE-LENGTH; BEEF MUSCLES; PSOAS-MAJOR; MU-CALPAIN; QUALITY; FRAGMENTATION;
D O I
10.2527/jas.2014-8351
中图分类号
S8 [畜牧、 动物医学、狩猎、蚕、蜂];
学科分类号
0905 ;
摘要
The aim of this study was to understand the relationship between changes in postmortem degradation of myofibrillar proteins and tenderness development in 3 different muscles from 10 Podolian young bulls aged 1, 7, 14, and 21 d. Psoas major (PM), longissimus dorsi (LD), and semitendinosus muscle (STD) were removed from each half carcass 24 h postmortem. Meat chemical composition, Warner-Bratzler shear force (WBSF), myofibril fragmentation index (MFI), total collagen content, and changes in myofibrillar proteins were estimated in triplicate at each aging time. A significant muscle effect was found on meat chemical composition. Semitendinosus muscle showed the lowest intramuscular fat percentage (P < 0.01) and the highest total collagen content (P < 0.01) with respect to LD and PM. Warner-Bratzler shear force decreased during aging in all muscles (P < 0.001), and semitendinosus was the toughest muscle whereas PM was the most tender (P < 0.001). Myofibril fragmentation index significantly increased (P < 0.001) in LD and PM meat throughout aging time whereas in semitendinosus it increased from 14 d of aging. Proteolysis was investigated by SDS-PAGE, western blotting, and 2-dimensional electrophoresis. Throughout postmortem aging, some structural proteins changed in intensity in all muscles analyzed. The blotting profile highlighted that desmin and troponin-T (TnT) bands were affected by both muscle and aging effects. Desmin degradation was more intense and faster in LD muscle than in semitendinosus and PM muscles. A progressive increase of the degraded isoforms of TnT (33 and 30 kDa polypeptides) was found during aging in LD, while, in PM these bands appeared earlier showing a greater intensity from 1 d. During aging, 2-dimensional gel electrophoresis (2DE) image analyses results showed a significant increase of the total number of spots reaching the highest value in the LD muscle at 21 d of aging (P < 0.01). Proteins separation also revealed differences in the spot number and expression patterns of myosin light chain (MLC) isoforms among muscles. A principal components analysis applied to meat chemical composition, tenderness, and myofibrillar proteins accounted for approximately 96.09% of total variance. Data highlight that aging affects the meat tenderness and proteolysis with different intensities in each muscle. These results provide knowledge about the tenderness mechanism in different muscles from a rustic breed and could be useful for the development of muscle specific strategies for improving the quality and value in different commercial cuts.
引用
收藏
页码:1376 / 1387
页数:12
相关论文
共 50 条
  • [31] Mechanism of rheological changes in poultry myofibrillar proteins during gelation
    Lesiów, T
    Xiong, YLL
    AVIAN AND POULTRY BIOLOGY REVIEWS, 2001, 12 (04): : 137 - 149
  • [32] Calcium supplementation in low nutrient density diet for meat ducks improves breast meat tenderness associated with myocyte apoptosis and proteolytic changes
    Huaiyong Zhang
    Quifeng Zeng
    Shiping Bai
    Jianping Wang
    Xuemei Ding
    Yue Xuan
    Zhuowei Su
    Joris Michiels
    Keying Zhang
    Animal Nutrition, 2022, 9 (02) : 49 - 59
  • [33] Changes of meat proteins during processing and their impacts on meat quality
    李春保
    何静
    周光宏
    Science Foundation in China, 2018, 26 (01) : 84 - 91
  • [34] Changes in tenderness and cathepsins, activity during post mortem ageing of yak meat
    Tian, Jia-Chun
    Han, Ling
    Yu, Qun-Li
    Shi, Xi-Xiong
    Wang, Wen-Ting
    CANADIAN JOURNAL OF ANIMAL SCIENCE, 2013, 93 (03) : 321 - 328
  • [35] Changes in meat quality traits and sarcoplasmic proteins during aging in three different cattle breeds
    Marino, R.
    Albenzio, M.
    della Malva, A.
    Caroprese, M.
    Santillo, A.
    Sevi, A.
    MEAT SCIENCE, 2014, 98 (02) : 178 - 186
  • [36] MEAT AGING AND FREEZING - POST-MORTEM CHANGES IN THE WATERSOLUBLE PROTEINS OF BOVINE SKELETAL MUSCLE DURING AGING AND FREEZING
    KRONMAN, MJ
    WINTERBOTTOM, RJ
    JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY, 1960, 8 (01) : 67 - 72
  • [37] Influence of Ultrasound and Proteolytic Enzyme Inhibitors on Muscle Degradation, Tenderness, and Cooking Loss of Hens During Aging
    Xiong, Guo-yuan
    Zhang, Li-li
    Zhang, Wei
    Wu, Juan
    CZECH JOURNAL OF FOOD SCIENCES, 2012, 30 (03) : 195 - 205
  • [38] Difference in tenderness and pH decline between water buffalo meat and beef during postmortem aging
    Neath, K. E.
    Del Barrio, A. N.
    Lapitan, R. M.
    Herrera, J. R. V.
    Cruz, L. C.
    Fujihara, T.
    Muroya, S.
    Chikuni, K.
    Hirabayashi, M.
    Kanai, Y.
    MEAT SCIENCE, 2007, 75 (03) : 499 - 505
  • [39] The effect of ageing on changes in myofibrillar protein in selected muscles in relation to the tenderness of meat obtained from cross-breed heifers
    Moczkowska, Malgorzata
    Poltorak, Andrzej
    Wierzbicka, Agnieszka
    INTERNATIONAL JOURNAL OF FOOD SCIENCE AND TECHNOLOGY, 2017, 52 (06): : 1375 - 1382
  • [40] Effect of a low-voltage electrical stimulation on yak meat tenderness during postmortem aging
    Chen, Meng-Yin
    Tian, Yuan
    Yu, Qun-Li
    Han, Ling
    Zhao, Suo-Nan
    Song, Ren-De
    ANIMAL SCIENCE JOURNAL, 2020, 91 (01)