Meat Science 2015-12-01

Modification of mature non-reducible collagen cross-link concentrations in bovine m. gluteus medius and semitendinosus with steer age at slaughter, breed cross and growth promotants.

B C Roy, G Sedgewick, J L Aalhus, J A Basarab, H L Bruce

Index: Meat Science 110 , 109-17, (2015)

Full Text: HTML

Abstract

Increased meat toughness with animal age has been attributed to mature trivalent collagen cross-link formation. Intramuscular trivalent collagen cross-link content may be decreased by reducing animal age at slaughter and/or inducing muscle re-modeling with growth promotants. This hypothesis was tested in m. gluteus medius (GM) and m. semitendinosus (ST) from 112 beef steers finished at either 12 to 13 (rapid growth) or 18 to 20 (slow growth) months of age. Hereford-Aberdeen Angus (HAA) or Charolais-Red Angus (CRA) steers were randomly assigned to receive implants (IMP), ractopamine (RAC), both IMP and RAC, or none (control). RAC decreased pyridinoline (mol/mol collagen) and IMP increased Ehrlich chromogen (EC) (mol/mol collagen) in the GM. In the ST, RAC increased EC (mol/mol collagen) but decreased EC (nmol/g raw muscle) in slow growing CRA steers. Also, IMP increased ST pyridinoline (nmol/g raw muscle) of slow-growing HAA steers. Results indicated alteration of perimysium collagen cross-links content in muscle in response to growth promotants. Copyright © 2015 Elsevier Ltd. All rights reserved.

Related Compounds

Structure Name/CAS No. Articles
beta-Estradiol Structure beta-Estradiol
CAS:50-28-2
Heptafluorobutyric acid Structure Heptafluorobutyric acid
CAS:375-22-4
Progesterone Structure Progesterone
CAS:57-83-0
L-pyroglutamic acid beta-naphthylamide Structure L-pyroglutamic acid beta-naphthylamide
CAS:22155-91-5
cis-4-Hydroxyproline Structure cis-4-Hydroxyproline
CAS:2584-71-6
L-Hydroxyproline Structure L-Hydroxyproline
CAS:51-35-4