Meat Tenderness, Relation between Hydroxyproline of Alkali-Insoluble Protein and Tenderness of Bovine Muscle

Loyd, E. J.; Hiner, R. L.

doi:10.1021/jf60106a010

Cited by 30 publications

(14 citation statements)

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“…No significant difference was found among the four age groups in collagen content of fresh biceps femoris. This is in agreement with Loyd and Hiner (1960), who also used a hydroxyproline technique for collagen determination, but disagrees with the findings of Wilson et al (1954), who fractionated the protein constituents of muscle on the basis of their solubility and used a nitrogen measurement for collagen determination. The collagen content of Group IV muscle had a high value because one of the two animals in this group had an abnormally high collagen content (over 2.5% on a freshweight basis).…”

Section: And Discussionsupporting

confidence: 72%

“…Reports by Adams et al (1960)) Loyd and Hiner (1960)) and Parrish et al (1961) indicate a negative association between collagen content and meat tenderness. The paradox presented by these reports, together with the results of Wilson et al (1954) showing a lower collagen content in the muscle of older animals, may indicate a structural change in collagen as an animal matures.…”

mentioning

confidence: 92%

“…Mackintosh et al (1936) and Mitchell and Hamilton (1933) found that meat from young steers contained less collagen and was more tender than meat from older animals. Hiner and Hankins (1950) and Jacobson and Fenton (1956) reported that Warner-Bratzler shear-force values tended to increase, representing decreased tenderness, during the maturation of bovine animals.…”

mentioning

confidence: 99%

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Age‐Associated Changes in Muscle Composition. The Isolation and Properties of a Collagenous Residue from Bovine Muscle^a

Goll

Bray

Hoekstra

1963

Journal of Food Science

159

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SUMMARY Age‐associated changes in the chemical composition of bovine biceps femoris muscle were studied. Veal muscle had significantly lower Kjeldahl nitrogen and higher moisture contents than muscle from the three older age groups studied. Muscle from veal and from the oldest group (cows, 10 years) possessed less fat than muscle from the two intermediate groups (steers, 1–2 years, and cows, 5 years). A modified procedure for determination of hydroxyproline and its use directly on mean hydrolysates are described. Use of this technique failed to reveal any significant differences in the hydroxyproline content, and presumably the connective‐tissue content, of muscle from the four groups. Warner‐Bratzler shear‐force values of cores from biceps femoris steaks from the three oldest groups indicated that tenderness decreased with age. A method is given for isolation of large quantities of connective tissue from biceps femoris. Chemical analyses of these connective‐tissue residues are presented, and the possibility is discussed that the veal connective tissue contains large amounts of reticulin.

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Section: And Discussionsupporting

confidence: 72%

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confidence: 92%

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confidence: 99%

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Age‐Associated Changes in Muscle Composition. The Isolation and Properties of a Collagenous Residue from Bovine Muscle^a

Goll

Bray

Hoekstra

1963

Journal of Food Science

159

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“…Although Go11 et al (1963), Herring et al (1967 and Kim et al 1967) found decreased tenderness in mature specimens, this was not universally related to corresponding increases in total collagen. Total intramuscular collagen has been shown to be negatively related to tenderness in studies by Husaini et al (1950)) Loyd et al (1959)) Adams et al (1960) andParrish et al (1962) in studies in which maturity was not a primary factor.…”

Section: Introductionmentioning

confidence: 97%

Tenderness and Maturity in Relation to Certain Muscle Components of White Leghorn Fowl

Wangen

Skala

1968

Journal of Food Science

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SUMMARY Tenderness of roasted and stewed pectoralis major and biceps femoris muscles (estimated by shear values) from White Leghorn female birds was studied in relation to maturity and composition at 4, 8, 12 and 18 months of age. Shear values of pectoralis major muscles did not change significantly with age or differ significantly between cooking methods. Shear values of biceps femoris muscles increased significantly with age of roasted specimens. No similar significant change occurred in stewed specimens. Roasted biceps femoris had significantly higher (P < 0.01) shear values than stewed samples at 12 months and more markedly at 18 months of age. No association was noticed between either intramuscular fat or moisture content and shear value trends. Hydroxyproline content (HOP) was determined in biceps femoris samples only. Total HOP content was significantly higher in more mature samples with a significant difference only at 12 months of age between cooking methods. Residual HOP content as a measure of collagen not converted to gelatin during cooking, showed a tendency to increase with age and differed significantly between cooking method only at 18 months of age. Total and residual HOP content of roasted biceps femoris were significantly correlated with shear values (r = 0.64 and 0.79, P < 0.01). The marked increase in residual HOP content at 18 months seemed to explain more satisfactorily the divergence in shear values.

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“…An aponeurosis presents a culinary challenge because it cannot be gelatinised without overcooking the adjacent muscle and aponeuroses are usually discarded by consumers. Much has been learned about intramuscular connective tissue as a source of meat toughness (Bailey & Sims, 1977;Dutson, Hostetler, & Carpenter, 1976;Loyd & Hiner, 1959;Smith & Judge, 1991), while aponeuroses on muscle surfaces have largely been ignored -despite their commercial importance.…”

Section: Introductionmentioning

confidence: 99%

Stratification of connective tissue toughness in beef roasts assessed by simultaneous fluorometry and penetrometry

Swatland

2006

Food Research International

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Meat Tenderness, Relation between Hydroxyproline of Alkali-Insoluble Protein and Tenderness of Bovine Muscle

Cited by 30 publications

References 2 publications

Age‐Associated Changes in Muscle Composition. The Isolation and Properties of a Collagenous Residue from Bovine Muscle^a

Age‐Associated Changes in Muscle Composition. The Isolation and Properties of a Collagenous Residue from Bovine Muscle^a

Tenderness and Maturity in Relation to Certain Muscle Components of White Leghorn Fowl

Stratification of connective tissue toughness in beef roasts assessed by simultaneous fluorometry and penetrometry

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Meat Tenderness, Relation between Hydroxyproline of Alkali-Insoluble Protein and Tenderness of Bovine Muscle

Cited by 30 publications

References 2 publications

Age‐Associated Changes in Muscle Composition. The Isolation and Properties of a Collagenous Residue from Bovine Musclea

Age‐Associated Changes in Muscle Composition. The Isolation and Properties of a Collagenous Residue from Bovine Musclea

Tenderness and Maturity in Relation to Certain Muscle Components of White Leghorn Fowl

Stratification of connective tissue toughness in beef roasts assessed by simultaneous fluorometry and penetrometry

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Age‐Associated Changes in Muscle Composition. The Isolation and Properties of a Collagenous Residue from Bovine Muscle^a

Age‐Associated Changes in Muscle Composition. The Isolation and Properties of a Collagenous Residue from Bovine Muscle^a