Aging of the Collagen Fiber

Verzár, F.

doi:10.1016/b978-1-4831-6751-0.50012-4

Cited by 143 publications

(41 citation statements)

References 101 publications

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“…The increase in retardations concerned with intrinsic birefringence suggests enhancement of crystal linity in aging tendons, which is in accordance with reports based on wide-angle X-ray findings (Sinex, 1968). Although collagen content and intramolecular bondings have been assumed not to significantly vary with age in tendons (Kohn and Rollerson, 1959;Bakermann, 1964), there is a continuous and increasing number of intermolecular cross-links in aging collagen (Bakermann, 1964;Verzar, 1964), the fibrils of the collagen bundles becoming more crystalline with the passage of time {Sinex, 1968).…”

Section: Discussionmentioning

confidence: 99%

Change with Age of Anisotropic Properties of Collagen Bundles

Mello¹,

Vidal²,

Carvalho³

et al. 1979

Gerontology

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Form birefringence curves and linear dichroic properties of aging rat tendons are different from those of adult controls. The steepness of the form birefringence curves and the increased retardations found in aging tendons are ascribed to an increase in collagen aggregation accompanied by loss of tissue water. Based on increase of retardations due to intrinsic birefringence, a rise in crystallinity levels is suggested for the collagen bundles of aging tendons. The inversion of the dichroism signs and the change in the d_∣_∣ (collagen fibers oriented parallel) and d₁ (collagen fibers oriented perpendicular) spectral absorption profiles, mainly at the absorption peaks for sections stained with toluidine blue solutions at pH 4.0 and 5.0, indicate modifications at the acid glycosaminoglycan molecular orientation level with advancing age.

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Section: Discussionmentioning

confidence: 99%

Change with Age of Anisotropic Properties of Collagen Bundles

Mello¹,

Vidal²,

Carvalho³

et al. 1979

Gerontology

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“…This may occur due to two reasons. Firstly already enough of hydroxyproline was solubilised by 0.1% acetic acid (Verzar 1964) due to pressure cooking (Macfarlane and McKenzie 1976) and as frying as heating causes increased solubilisation of collagen (Laakhonen et al 1970;Marjorie and Bernadine 1975). Secondly, sugars (specially glucose) has been reported to be responsible for inhibition of formation of soluble hydroxyproline by way of forming additional cross linkages of collagen molecules (Webster et al 1986).…”

Section: Tba Valuesmentioning

confidence: 99%

Shelf life study of hurdle treated ready-to-eat spiced buffalo meat product stored at 30 ± 3 °C for 7 weeks under vacuum and aerobic packaging

Malik

Sharma

2011

J Food Sci Technol

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Shelf stable ready to eat spiced pickle type buffalo meat product was prepared after desorbing in infusion solution (glycerol 3.5%, sodium chloride 5.0%, honey2.0%, mango powder 2.2%, spices 1.0%, sodium nitrite 0.015%, phosphate 0.2%, Sorbic acid 0.2%.and acetic acid 1%), pressure cooking of meat in infusion solution for 20 min followed by frying for 2 min in mustard oil and mixing with prefried condiments and spices. The physico-chemical properties i.e. pH, water activity, proximate composition, FFA, Soluble hydroxyproline, TBA values, nitrite content, protein solubility, shear force value, haempigments, microbiological and sensory quality of the product remained good and hygienically safe and almost comparable in aerobic PET jars and multilayered nylon barrier pouches stored at 30±3°C for 7 weeks .It can be suggested that storage of such product may be conveniently done even in food grade PET jars without going for vacuum packaging which is a bit costly.

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“…It has been established by several workers that the properties of collagen change with age. Verzar [14] attri buted these changes to an accumulation of covalent crosslinks. The increase in the amount of covalent crosslinks within the collagen fibres resulted in an increase in thermostability of the latter and could be expressed in terms of changes occurring in the percentual weight loss of the samples between 450 °C and 800 °C.…”

Section: Discussionmentioning

confidence: 99%

Thermoanalytical Investigations on the Age-Related Changes in Articular Cartilage, Meniscus and Tendon

Bihari-Varga

Bı́ró

1971

Gerontology

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A complex thermoanalytical method, the derivato-graphy, has been applied for the study of age-related changes in the composition and structural stability of human articular hyaline cartilage, meniscus and tendon. Structurally bound water content in all the three types of tissues, as well as the concentration of sulfated acid glycosaminoglycans in cartilage and meniscus were found to decrease significantly with age; the amount of keratan sulfate showed increasing tendency. Correlation could be demonstrated between the accumulation of covalent crosslinks in the aging structural proteins and the thermostability of the samples between 450°C and 800°C. Structural differences as well as differences in the rate of maturation of cartilage, meniscus and tendon tissues resulted in alterations in their thermal decomposition.

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Aging of the Collagen Fiber

Cited by 143 publications

References 101 publications

Change with Age of Anisotropic Properties of Collagen Bundles

Change with Age of Anisotropic Properties of Collagen Bundles

Shelf life study of hurdle treated ready-to-eat spiced buffalo meat product stored at 30 ± 3 °C for 7 weeks under vacuum and aerobic packaging

Thermoanalytical Investigations on the Age-Related Changes in Articular Cartilage, Meniscus and Tendon

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