2001
DOI: 10.1016/s0309-1740(01)00044-4
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Influence of weak organic acids and salts on the denaturation characteristics of intramuscular connective tissue. A differential scanning calorimetry study

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Cited by 43 publications
(48 citation statements)
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“…() observed a strong increase in mechanical strength of connective tissue and a large decrease in denaturation temperature of intramuscular collagen. Atkas and Kaya () also reported a large decrease in denaturation temperature of bovine longissimus dorsi intramuscular connective tissue incubated in 0.34, 0.68, and 1.03 M NaCl for 24 to 72 hr compared to control samples incubated in a phosphate buffer. These molecular‐level changes are probably the cause of the changes in endomysial and perimysial morphology observed here.…”
Section: Resultsmentioning
confidence: 91%
See 1 more Smart Citation
“…() observed a strong increase in mechanical strength of connective tissue and a large decrease in denaturation temperature of intramuscular collagen. Atkas and Kaya () also reported a large decrease in denaturation temperature of bovine longissimus dorsi intramuscular connective tissue incubated in 0.34, 0.68, and 1.03 M NaCl for 24 to 72 hr compared to control samples incubated in a phosphate buffer. These molecular‐level changes are probably the cause of the changes in endomysial and perimysial morphology observed here.…”
Section: Resultsmentioning
confidence: 91%
“…It is generally accepted that fibrillar collagen and elastin are neither soluble in cold water nor in salt solution. However, increasing the ionic strength of meat products changes the conformational stability of the intramuscular connective tissue, as shown by differential scanning calorimetry (Aktas & Kaya, ; Chang, Wang, Zhou, Xu, & Li, ). After marinating bovine semitendinosus muscle samples for 24 hr in a 2% NaCl brine (0.34 M NaCl), Chang et al.…”
Section: Resultsmentioning
confidence: 99%
“…Bailey and Light (1989) reported that the To is considered to describe the least stable collagen and the Tp is a measure of the average stability of collagen. Kijowski and Mast (1988) reported a Tp of 65.3°C (heating rate 10°C/min) in isolated intramuscular connective tissue of chickens; Aktas and Kaya (2001) found a Tp of 69.2°C (heating rate 5°C/min) in that of old cows. It was reasonable that Tp is different for different muscles and animal species.…”
Section: Heat-insoluble Collagen Content and Dscmentioning
confidence: 99%
“…In addition, acid solubilisation of collagen may occur (44). It has been demonstrated that if the pH falls below the isoelectric point of the muscle protein, solubilisation of the protein is higher producing fi rmer sausages (45).…”
Section: Resultsmentioning
confidence: 99%