Relationship between tenderness of three beef Muscles

Dransfield, Eric; Jones, Rachael

doi:10.1002/jsfa.2740320316

Cited by 16 publications

(4 citation statements)

References 13 publications

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“…Over the last two decades, most investigations have been focused on the nature of the changes that occur at the level of myofibrils during meat aging and on the endogenous proteolytic systems which are very likely important causative agents (Penny 1980;Go11 et al 1983;Valin 1985). Several works have recently aroused considerable interest in the possible origins of the large viariability observed in meat conditioning between animal species and between muscles of the same animal (Ouali 1981;Dransfield and Jones 1981;Dransfield et al 1980-81a;Etherington er al. 1987), an unusual approach which might produce important new insights into our understanding of the mechanisms of meat tenderization.…”

Section: Introductionmentioning

confidence: 99%

“…It is recognized that meat tenderizing is a very variable process depending on a number of biological factors, i.e., animal age and sex (Buchter 1972;Mac-Dougall 1972;Purchas 1972;Valin et af. 1975;, muscle type (Ouali 1981;Dransfield and Jones 1981;Ouali et al 1983b;Quali et al 1988;Valin 1988;Monin and Quali 1989), animal species (Dransfield et al 1980-81b;Etherington et af. 1987), anabolic and repartitioning agents (Kopp et af.…”

Section: Introductionmentioning

confidence: 99%

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Meat Tenderization: Possible Causes and Mechanisms. A Review.

Ouali¹

1990

Journal of Muscle Foods

245

108

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The postmortem meat tenderizing process is complex and not fully understood. The nature of changes associated with the improvement in tenderness and the exact mechanisms involved are still unknown. Based on relevant evidence, old and new, this review attempts to clarify the statement of our knowledge of these aspects. Of the diflerent biochemical and ultrastructural changes occurring in meat, a key role of myofibril disruption taking place at the N2-line level in meat tenderization has been emphasized. This may be ascribed to the action of lyosomal enzymes, especially cathespin B and L. However, all the changes thus far identijied can be only explained by a synergistic action of lysosomal and calcium-dependent proteinases. Besides or together with proteolytic enzymes, weakening of myofibrils may also be mediated by the high ionic strength achieved in postmortem muscles. Both mechanisms possibly involved in the meat tenderizing process have been tentatively tested in relation with the large muscle variability in aging rate. It appears that some concepts are in conflict with the results presented. For instance, no direct relationship was found between aging rate and proteinase content of muscles. . Reglation of protein degradation in muscle by calcium. Evidence for enhanced nonlysosomal proteolysis associated with elevated cytosolic calcium. J. Biol. Chem. 260, 13619.

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Meat Tenderization: Possible Causes and Mechanisms. A Review.

Ouali¹

1990

Journal of Muscle Foods

245

108

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“…As far as chilling is concerned, it is clear that bull carcasses would cool more quickly than the fatter steer carcasses and be more susceptible to cold shortening toughness. The greater variability in texture both within (Dransfield and MacFie, 1980) and between (Dransfield and Jones, 1981) muscles is also indicative of cold shortening toughness and it was the large variability in bull m. longissimus dorsi (Reagan et al, 1971;Arthaud, Mandigo, Koch and Kotula, 1977) which was instrumental in the suggestion to downgrade bull beef (Reagan et al, 1971). Circumstantial evidence suggests that the major source of poor bull beef quality is due to the vagaries of carcass cooling.…”

Section: Discussionmentioning

confidence: 99%

Comparison of eating quality of bull and steer beef

Dransfield¹,

Nute²,

Francombe³

1984

Anim. Sci.

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Eating qualities of beef from entire and castrate male animals were compared using taste panel, objective texture and chemical measurements and a consumer panel. The eating quality of roast m. longissimus dorsi, casseroled m. supraspinatus, minced m. gastrocnemius and grilled m. psoas major from bull beef, slaughtered at 400 days was different (by triangular tests) from that of twin steer beef. The differences (attributed to flavour, texture and juiciness) were not substantiated using descriptive scaling tests when the only significant difference was that roast m. longissimus dorsi from bulls was slightly drier than that from steers. Tenderness, juiciness and flavour of roast m. longissimus dorsi from 71 bulls and 84 steers raised semi-intensively to 390 to 510 kg and slaughtered commercially were assessed using descriptive category scales and the instrumental toughness values. There was no significant difference in organoleptic qualities and the distributions of tenderness and juiciness within these populations were similar. Bull beef contained more connective tissue and had less intramuscular fat. Fatness was poorly related to tenderness (r = 0-3) and unrelated to juiciness or flavour. A consumer panel of 606 assessors showed that bull beef was not as pale as steer beef and found no difference in fatness of the cuts, flavour or juiciness. Fore-rib roasts of bull beef were marginally less tender than steer fore rib.

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“…This crosslink of connective tissue might have mainly contributed to the background of toughness of muscle food such as goat and pork meat. Dransfield and Jones (1981) have reported that LD muscle is more tender than SM or semitendinosus muscles. Results of the current study showed that PM muscle was tender than other muscles.…”

Section: Correlation Coefficients (R) Between Muscle Fiber Charactementioning

confidence: 99%