» Articles » PMID: 29293748

Effect of Brahman Genetics on Myofibrillar Protein Degradation, Collagen Crosslinking, and Tenderness of the Longissimus Lumborum

Overview
Journal J Anim Sci
Date 2018 Jan 3
PMID 29293748
Citations 9
Authors
Affiliations
Soon will be listed here.
Abstract

The objective of this study was to examine the effect of percent Brahman genetics on Warner-Bratzler shear force (WBSF), desmin and troponin-T (TnT) degradation, hydroxylysyl pyridinoline (HP) crosslink content, and perimysial collagen melting temperature. Steers ( = 131) produced in 2012 and 2013 were harvested at 1.27 cm of visual s.c. back fat thickness. Steers were divided into 4 genetic categories consisting of steers that contained 6/32 or less Brahman genetics, 12/32 Brahman genetics, 14/32 to 18/32 Brahman genetics, and 23/32 to 32/32 Brahman genetics. Twenty-four hours after harvest, a 7.62-cm piece of the longissimus lumborum beginning at the 13th rib was collected and aged for 14 d. Following aging, three 2.54-cm steaks were cut for WBSF, trained sensory panel, and laboratory analyses. Laboratory analyses steaks were used to determine protein degradation, HP crosslink analysis, and perimysial collagen melting temperature. Data were analyzed using a polynomial regression for unequally spaced treatments. As the percent Brahman genetics increased, WBSF increased (linear, = 0.01). As percent Brahman genetics increased, tenderness score decreased (less tender) and connective tissue score increased (more connective tissue; linear, = 0.01). As the percentage of Brahman genetics increased, the amount of degraded desmin (38 kDa) and TnT (34 and 30 kDa) decreased (linear, < 0.03) whereas the amount of immunoreactive 36 kDa TnT increased (linear, = 0.04). Percent Brahman genetics had no effect ( = 0.14) on HP crosslink content but did tend to increase ( = 0.07) perimysial collagen melting temperature as the percent Brahman increased. The percentage of Brahman genetic influence was positively correlated to WBSF ( = 0.25), 36 kDa immunoreactive TnT ( = 0.26), and perimysial collagen melting temperature ( = 0.25, = 0.01). Sensory panel tenderness ( = -0.44), juiciness ( = -0.26), and connective tissue scores ( = -0.63); 38 kDa degraded desmin ( = -0.34), 34 ( = -0.36) and 30 kDa degraded TnT ( = -0.29); and HP collagen crosslinks ( = -0.20) were negatively correlated to percent Brahman genetic influence ( < 0.03). Increasing Brahman genetic influence in steers negatively affects tenderness, partially through a reduction in degradation of desmin and TnT. Although HP collagen crosslinks are unaffected by Brahman genetics, a tendency for increased perimysium melting temperature indicates that other collagen-stabilizing crosslinks may be affected.

Citing Articles

Quality Enhancement Techniques for Cow Meat: Current Approaches and Future Directions.

Kim H, Park J, Song S, Cheng H, Baek J, Kim G Food Sci Anim Resour. 2025; 45(1):185-198.

PMID: 39840238 PMC: 11743845. DOI: 10.5851/kosfa.2024.e125.


Breed of origin analysis in genome-wide association studies: enhancing SNP-based insights into production traits in a commercial Brangus population.

Zayas G, Rodriguez E, Hernandez A, Rezende F, Mateescu R BMC Genomics. 2024; 25(1):654.

PMID: 38956457 PMC: 11218112. DOI: 10.1186/s12864-024-10465-1.


A single-cell atlas of bovine skeletal muscle reveals mechanisms regulating intramuscular adipogenesis and fibrogenesis.

Wang L, Gao P, Li C, Liu Q, Yao Z, Li Y J Cachexia Sarcopenia Muscle. 2023; 14(5):2152-2167.

PMID: 37439037 PMC: 10570087. DOI: 10.1002/jcsm.13292.


Genome-wide association studies on collagen contents trait for meat quality in Hanwoo.

Won K, Kim D, Hwang I, Lee H, Oh J J Anim Sci Technol. 2023; 65(2):311-323.

PMID: 37093907 PMC: 10119448. DOI: 10.5187/jast.2022.e110.


Carcass and meat quality traits in Brangus steers.

Rodriguez E, Hamblen H, Flowers S, Leal J, Carr C, Scheffler T Transl Anim Sci. 2023; 7(1):txad021.

PMID: 36970314 PMC: 10032192. DOI: 10.1093/tas/txad021.


References
1.
McCormick R . Extracellular modifications to muscle collagen: implications for meat quality. Poult Sci. 1999; 78(5):785-91. DOI: 10.1093/ps/78.5.785. View

2.
Lonergan S, Huff-Lonergan E, Rowe L, Kuhlers D, Jungst S . Selection for lean growth efficiency in Duroc pigs influences pork quality. J Anim Sci. 2001; 79(8):2075-85. DOI: 10.2527/2001.7982075x. View

3.
Miller M, Carr M, Ramsey C, Crockett K, Hoover L . Consumer thresholds for establishing the value of beef tenderness. J Anim Sci. 2002; 79(12):3062-8. DOI: 10.2527/2001.79123062x. View

4.
Rhee M, Wheeler T, Shackelford S, Koohmaraie M . Variation in palatability and biochemical traits within and among eleven beef muscles. J Anim Sci. 2004; 82(2):534-50. DOI: 10.2527/2004.822534x. View

5.
Melody J, Lonergan S, Rowe L, Huiatt T, Mayes M, Huff-Lonergan E . Early postmortem biochemical factors influence tenderness and water-holding capacity of three porcine muscles. J Anim Sci. 2004; 82(4):1195-205. DOI: 10.2527/2004.8241195x. View