Postmortem Degradation of Titin and Nebulin of Beef Steaks Varying in Tenderness

Anderson, Timothy J.; Parrish, F. C.

doi:10.1111/j.1365-2621.1989.tb04695.x

Cited by 44 publications

(29 citation statements)

References 12 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…(1997). The previous work of Anderson and Parrish (1989) demonstrated that the degradation of titin and nebulin coincided with increased tenderness because their degradation may alter the integrity of muscle cell (Robson et al. 1991) and decrease the myofibrillar strength (Horowits et al.…”

Section: Discussionmentioning

confidence: 99%

Postmortem Changes in Myofibrillar Proteins of Goat Skeletal Muscles

Nagaraj

Santhanam

2005

Journal of Food Biochemistry

View full text Add to dashboard Cite

Postmortem changes at 5C in myofibrillar proteins of longissimus dorsi (LD), biceps femoris (BF), semimembranosus (SM) and semitendinosus (ST) muscles and myofibrillar structure of LD muscle of goat were investigated. Muscle samples were immediately collected after killing, and from carcasses stored at 5C for 3, 6, 9, 12 and 20 days. The sodium dodecyl sulfate‐polyacrylamide gel electrophoresis of myofibrils indicated the appearance of a 30 kDa component, depending on the type of the muscles. A new 55 kDa component appeared in BF and SM muscles during postmortem. Titin I and nebulin also disappeared during storage. The disappearance of titin 1 and nebulin and the appearance of a 30 kDa component were confirmed by Western blot analysis. The Transmission Electron Microscopy studies showed that after 3 days postmortem, Z‐disks stayed unaltered. After 6 days postmortem, a little ultrastructural alteration was observed, and at 12 days postmortem a considerable degradation of Z‐disk ultrastructure was shown. The Z‐disk degradation, which results in the fragmentation of myofibrils and the appearance of 30 kDa components, is the major change observed in goat skeletal muscles during postmortem.

show abstract

Section: Discussionmentioning

confidence: 99%

Postmortem Changes in Myofibrillar Proteins of Goat Skeletal Muscles

Nagaraj

Santhanam

2005

Journal of Food Biochemistry

View full text Add to dashboard Cite

show abstract

“…In addition, other myofibrillar proteins such as titin and nebulin are also implicated in post mortetn weakening of fish (Tsuchiya et al 1992) and meat muscle (Anderson and Parrish 1989). Another study (Astier et a1 1991) using dorado myofibrils showed complete aactinin release and marked titin and nebulin cleavage.…”

Section: Introductionmentioning

confidence: 93%

Post mortem Release of Fish White Muscle α-Actinin as a Marker of Disorganisation

Papa

Álvarez

Verrez‐Bagnis

et al. 1996

J. Sci. Food Agric.

View full text Add to dashboard Cite

“…The fact that titin serves such a critical structural role strongly argues that titin degradation may occur more rapidly in muscle tissue of more tender retail cuts than those that are less tender and may be a more useful predictor of tenderness. Although previous studies have evaluated the role of titin in postmortem proteolysis and tenderness development (Anderson and Parrish, 1989;Fritz et al, 1993;Huff-Lonergan et al, 1996), the relationship between proteolysis of this protein and 989 sarcomere length has not been adequately addressed. Therefore, the aim of this work was to determine the role of sarcomere length on the postmortem degradation of titin.…”

Section: Introductionmentioning

confidence: 96%

Postmortem titin proteolysis is influenced by sarcomere length in bovine muscle1

England

Fisher

Wells

et al. 2012

Journal of Animal Science

View full text Add to dashboard Cite

The calpain protease system, in particular, μ-calpain is involved in the disassembly of specific myofibrillar proteins, resulting in tenderization of meat postmortem. Given the size, complexity, and integral nature of titin to the structure of the sarcomere, it is plausible that the length of a sarcomere may alter the susceptibility of various domains of titin to cleavage by the calpains. Therefore, we hypothesized titin degradation differs in a sarcomere-length-dependent manner in beef. After slaughter, beef carcasses were split and sides were either suspended by the Achilles tendon (normal suspension, NS) or by the aitchbone (hip suspension, HS). Immediately after suspension, samples were dissected from the LM, psoas major (PM), and semitendinosus (STN) muscles to serve as 0-d controls. After 24 h, 4 steaks were removed from each muscle and randomly assigned to 1-, 4-, 7-, or 10-d aging treatments. After the assigned aging period, myofibrils were purified for determination of sarcomere length. Warner-Bratzler shear force analysis was also performed to evaluate differences in tenderness. Muscle proteins were solubilized and subjected to SDS-VAGE (vertical agarose gel electrophoresis) to evaluate titin degradation. Sarcomere lengths differed (P < 0.0001) between contralateral muscles of NS and HS carcasses. Quantification of SDS-VAGE gels revealed less (P < 0.05) intact titin in the PM muscle of NS carcasses at each aging period compared with the PM of HS carcasses. No significant differences (P > 0.05) were detected in the disappearance of intact titin among suspension methods in the LM or STN. These data demonstrate that suspension method alters proteolysis of titin and suggest an increase in sarcomere length may contribute to the susceptibility of titin to postmortem proteolysis in beef.

show abstract

Postmortem Degradation of Titin and Nebulin of Beef Steaks Varying in Tenderness

Cited by 44 publications

References 12 publications

Postmortem Changes in Myofibrillar Proteins of Goat Skeletal Muscles

Postmortem Changes in Myofibrillar Proteins of Goat Skeletal Muscles

Post mortem Release of Fish White Muscle α-Actinin as a Marker of Disorganisation

Postmortem titin proteolysis is influenced by sarcomere length in bovine muscle1

Contact Info

Product

Resources

About