1970
DOI: 10.1111/j.1365-2621.1970.tb12133.x
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LOW‐TEMPERATURE, LONG‐TIME HEATING OF BOVINE MUSCLE 3. Collagenolytic Activity

Abstract: SUMMARY: Naturally occurring collagenolytic activity was found in the water‐soluble fraction of bovine muscle. General proteolytic activity determined with Azocoll indicated that this total activity was much greater than the collagenase activity specifically determined according to the method of Wünsch and Heidrich. The collagenase fraction was concentrated by polyacrylamide gel electrophoresis and the activity of the enzyme was studied under various pH and temperature conditions. This collagenase could remai… Show more

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Cited by 40 publications
(14 citation statements)
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“…Christensen et al (2013) is only marginal. This collagen denaturation is supported by a residual collagenase activity, which is able to unfold the collagen triple helix so that other proteins are able to degrade it, leading to a more tender meat (Baldwin, 2012;Ertbjerg, Christiansen, Pedersen, & Christensen, 2012;Laakonen, Sherbon, J.W., Wellington, G.H., 1970b;Penfield & Meyer, 1975). Studies on Cathepsin B and L activity demonstrated that these enzymes are able to weaken both collagen and myofibrillar structures (Agarwal, 1990;Baron, Jacobsen, & Purslow, 2004;Burleigh, Barrett, & Lazarus, 1974).…”
Section: Shear Forcementioning
confidence: 95%
“…Christensen et al (2013) is only marginal. This collagen denaturation is supported by a residual collagenase activity, which is able to unfold the collagen triple helix so that other proteins are able to degrade it, leading to a more tender meat (Baldwin, 2012;Ertbjerg, Christiansen, Pedersen, & Christensen, 2012;Laakonen, Sherbon, J.W., Wellington, G.H., 1970b;Penfield & Meyer, 1975). Studies on Cathepsin B and L activity demonstrated that these enzymes are able to weaken both collagen and myofibrillar structures (Agarwal, 1990;Baron, Jacobsen, & Purslow, 2004;Burleigh, Barrett, & Lazarus, 1974).…”
Section: Shear Forcementioning
confidence: 95%
“…Heating rates of cooking treatments were previously found to affect the rate of protein denaturation (myofibrillar proteins and collagen) and the properties of meat related to tenderness (Laakkonen et al, 1970;Aaslyng et al, 2003). In addition, both temperature and cooking times were found to strongly affect pork meat tenderness for heating temperature higher than 60°C (Bouton and Harris, 1972).…”
Section: Meat Texturementioning
confidence: 96%
“…Lower temperature cooking could reduce energy consumption but the final internal temperature of 65-85°C must to be reached to ensure hygienic safety of cooked meat (Laakkonen et al, 1970;Smith and LeBlanc, 1990). This could be beneficial not only to domestic cooking but also for food catering operations.…”
Section: Introductionmentioning
confidence: 99%
“…Changes in meat tenderness and juiciness during cooking strongly depend upon the cooking temperature and time applied, these factors determine collagen solubilization and myofibrilar proteins shrinkage (Christensen et al, 2013;Laakonen et al, 1970;Sa´nchez Del Pulgar et al, 2012). However, the subsequent changes in textural traits during the refrigerated storage of sous-vide cooked lamb meat as affected by the cooking conditions remain mostly unknown.…”
Section: Introductionmentioning
confidence: 98%