Meat Tenderness Factors, Determination of Collagen in Raw and Cooked Beef from Two Muscles by Alkali-Insoluble, Autoclave-Soluble Nitrogen and by Hydroxyproline Content

Ritchey, S. J.; Cover, Sylvia

doi:10.1021/jf60119a013

Cited by 11 publications

(4 citation statements)

References 3 publications

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“…Results given by Adams and Arthaud (1963), Wipf et al (1964) and Field et al (1965) suggest that an age gradient may exist in quality factors of bulls. Linke et al (1967) and Pelczynska (1970) found that bull muscle contained more connective tissue than cow muscle, but the differences were not high; however, Wilson et al (1954) and Richey and Cover (1962) found no relationship between connective tissue and sex of animals. Boccard et al (1979) investigated the influence of sex on the amount of total and soluble collagen in various beef muscles.…”

Section: Cattlementioning

confidence: 97%

Utilization of the Intact Male for Red Meat Production: A Review

Seideman¹,

Cross²,

Oltjen³

et al. 1982

Journal of Animal Science

272

119

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Section: Cattlementioning

confidence: 97%

Utilization of the Intact Male for Red Meat Production: A Review

Seideman¹,

Cross²,

Oltjen³

et al. 1982

Journal of Animal Science

272

119

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“…'Chemical analyses for collagen by the hydroxyproline procedure of Ritchey and Cover (1962) I\-ere made on raw steaks and on steaks cooked to 61, 80, and 100°C (Table 2). These data were collected on some of the animals in lots 1, 5, and 6 ( Table 1).…”

Section: Methodsmentioning

confidence: 99%

“…It seems unlikely that collagen is in a form more resistant to heat in BF than in LD, for the losses (percent of total collagen in raw) were similar for the two muscles at each of the internal temperatures. This was true not only when collagen tests were based on the hydrosyproline method but also when they were based on alkali-insoluhle autoclave-soluble nitrogen (Ritchey and Cover, 1962;Irvin and Cover, 1959). Moreover, when the collagen content in both muscles was too low to be measured accurately (at lOO'C>, the scores for both muscles were similar.…”

Section: Tenderness Of Beef Imentioning

confidence: 99%

Tenderness of Beef.

Cover

Ritchey

Hostetler

1962

Journal of Food Science

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SUMMARY Panel scores for juiciness and six components of tenderness were considered in relation to possible multiple causes of tenderness or toughness and to certain histological, chemical, and physical data. One‐inch steaks from Longissimus dorsi and biceps femoris from 180 young cattle in nine lots were eooked to 61°C (rare) and to 80°C (well‐done) by dry heat, and to 100°C by moist heat. Connective tissue in longissimus dorsi was scored tender at 61°C, and was tendered only slightly by increases in temperature, whereas in biceps femoris it was scored tough at 61°C and became progressively more tender at 80 and 100°C. Collagen content was greater in biceps femoris than in Longissimus dorsi at 61 and 80°C, but there was little difference in the two muscles at 100°C; the losses in both muscles increased with increasing meat temperatures. The relation of panel scores for tenderness of connective tissue to collagen content and to the loss of collagen on heating is discussed.

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“…40, 9.34, 12.64, and 36.26 for the 10, 20, and 30 min boiling water cooking and the pressure cooking processes, respectively. The loss in collagen during the cooking of beef muscle may vary widely -57% (Ritchey and Cover, 1962), 38.5-75.7% (Ritchey et al, 1963), and 67.9% (McClain et al, 1964) -depending on the method of cooking. The difference between the percent loss of collagen in chicken breast meat and that of the beef muscle may be due to the difference in the meat type as well as the cooking methods.…”

Section: Effect Of Cooking On Collagen Content Of Chicken Breast Meatmentioning

confidence: 99%

Collagen Contents of Chicken Gizzard and Breast Meat Tissues as Affected by Cooking Methods

Ruantrakool

Chen

1986

Journal of Food Science

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The changes in collagen contents of chicken gizzard and breast meat during boiling water and pressure cooking were investigated. The loss of collagen in both tissues increased as the cooking time or temperature increased. The percent of collagen in acid-and salt-soluble forms in gizzard was lower than that of the breast meat. The acid-and saltsoluble collagen from water cooked gizzard were lower than those of the pressure cooked gizzard. Cooking gizzard in boiling water containing 0.5% acetic acid or papain significantly (p

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Meat Tenderness Factors, Determination of Collagen in Raw and Cooked Beef from Two Muscles by Alkali-Insoluble, Autoclave-Soluble Nitrogen and by Hydroxyproline Content

Cited by 11 publications

References 3 publications

Utilization of the Intact Male for Red Meat Production: A Review

Utilization of the Intact Male for Red Meat Production: A Review

Tenderness of Beef.

Collagen Contents of Chicken Gizzard and Breast Meat Tissues as Affected by Cooking Methods

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