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Effects of pre‐slaughter nutritional condition on intramuscular collagen solubility, pyridinoline cross‐links and meat tenderness in aged goats
Author(s) -
SHIBA Nobuya,
MATSUZAKI Masatoshi,
TSUNEISHI Eisaku
Publication year - 2004
Publication title -
animal science journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.606
H-Index - 38
eISSN - 1740-0929
pISSN - 1344-3941
DOI - 10.1111/j.1344-3941.2004.00192.x
Subject(s) - pyridinoline , tenderness , meat tenderness , intramuscular fat , hay , zoology , chemistry , food science , biology , biochemistry , alkaline phosphatase , enzyme , osteocalcin
Effects of preslaughter nutritional condition on intramuscular collagen characteristics were studied, in order to clarify the potential of intensive feeding to aged animals in improving meat tenderness. Ten castrated male goats were assigned into one of two groups: one group was allowed ad libitum access to a concentrate diet (total digestible nutrients 70%, crude protein 15%) and Italian ryegrass hay (ADLIB‐group), and the other group was fed a restricted amount of their diet (concentrate diet 0.5% of bodyweight/day; hay 1.5% of bodyweight/day) to maintain their bodyweight (MAIN‐group). After 3 months of the experimental period, goats were slaughtered and meat samples were obtained immediately. Goats in ADLIB‐group had lower total and insoluble collagen concentrations, higher fat concentrations and collagen solubility than those in MAIN‐group, but soluble collagen concentrations of muscles were similar for both groups. Goats in ADLIB‐group had lower pyridinoline concentrations than those in MAIN‐group, in all muscles, but the differences of pyridinoline concentration between the groups were not statistically significant. Warner‐Bratzler shear force values of Longissimus and Biceps femoris muscles were lower in ADLIB‐group than in MAIN‐group. The increase of meat tenderness by preslaughter intensive feeding seemed to be associated with the increase in intramuscular fat deposition and high collagen solubility, and pyridinoline cross‐link appeared to be one of the factors related to collagen solubility.