Shrinkage of collagen fibres: A differential scanning calorimetric study

Finch, Arthur; Ledward, D.A.

doi:10.1016/0005-2795(72)90003-7

Cited by 95 publications

(33 citation statements)

References 13 publications

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“…In solution denaturation temperature ranges have been found to vary from 37°C to 72°C, primarily depending on the heating rate applied 31,32 . Using microscopy, most authors observed denaturation temperatures in the range between 57°C and 65°C in tendons and skin [33][34][35] .…”

Section: Thermal-induced Changes In Muscle Proteinsmentioning

confidence: 99%

Second Harmonic Generation Microscopy: A Tool for Spatially and Temporally Resolved Studies of Heat Induced Structural Changes in Meat

et al. 2009

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Myofibers and collagen show non-linear optical properties enabling imaging using second harmonic generation (SHG) microscopy. The technique is evaluated for use as a tool for real-time studies of thermally induced changes in thin samples of unfixed and unstained pork. The forward and the backward scattered SHG light reveal complementary features of the structures of myofibers and collagen fibers. Upon heating the myofibers show no structural changes before reaching a temperature of 53°C. At this temperature the SHG signal becomes extinct. The extinction of the SHG at 53°C coincides with a low-temperature endotherm peak observable in the differential scanning calorimetry (DSC) thermograms. DSC analysis of epimysium, the connective tissue layer that enfold skeletal muscles, produces one large endotherm starting at 57°C and peaking at 59.5°C. SHG microscopy of collagen fibers reveals a variability of thermal stability. Some fibers show severe shrinkage at 57°C, before the signal for most of them vanishes between 59°C and 61°C and thus coinciding with the endotherm of the thermograms. However, in some areas, strong SHG signals from collagen can be visualized even after prolonged heating to 67°C and thus indicating regions of much higher thermal stability. It is seen that the benefits of the structural and temporal information available from SHG microscopy reveals complementary information to a traditional DSC measurement and enables a more complete understanding of the thermal denaturation process.

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Section: Thermal-induced Changes In Muscle Proteinsmentioning

confidence: 99%

Second Harmonic Generation Microscopy: A Tool for Spatially and Temporally Resolved Studies of Heat Induced Structural Changes in Meat

et al. 2009

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“…Although tropocollagen may be stabilized mainly by intramolecular hydrogen bonds and(or) hydrogen bonds from the adjacent regular water structure, the cross-linked fibers are additionally stabilized by hydrophobic bonds, the concentration or strength of these bonds being greater in dry than swollen fiber. 19 40 can be explained by hydrogen and(or) hydrophobic-bond cleavage resulting from the swelling of the fibers with the increase in water content. On this theoretical basis, the graph in Figure 1 Owing to a fast exchange 22 between at least two water fractions ("free" and "bound" water), native collagen-water system was at all MC values studied…”

Section: Native Collagenmentioning

confidence: 99%

Effect of thermal denaturation on water-collagen interactions: NMR relaxation and differential scanning calorimetry analysis

Rochdi¹,

Foucat²,

Renou³

1999

Biopolymers

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“…However, since the best estimate for the denaturation temperature of a protein is given by T o , 24) T o was adopted as the denaturation temperature in the present study. Decreasing the sorbed water content from about 89% to 50% resulted in T o of the -conglycinin and glycinin preparations gradually increasing, then markedly increasing below about a 30-40% sorbed water content, and increasing even more below a content of about 10-20% (Fig.…”

Section: Water Sorption Behaviormentioning

confidence: 99%

Effect of Sorbed Water on the Thermal Stability of Soybean Protein

Tsukada

Takano

Hattori

et al. 2006

Bioscience, Biotechnology, and Biochemistry

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A soybean protein isolate (SPI), and its -conglycinin and glycinin componets were obtained from defatted soybean flour by applying dissolution and precipitation based on the difference in their solubility depending on each isoelectric point. The purity evaluated by SDS-PAGE of the -conglycinin and glycinin preparations was about 84% and 80%, respectively, resulting in a clear difference in the pH dependence on solubility. A BET plot derived from the water sorption isotherm at 25 C showed that the amount of the monolayer adsorption of these preparations was about 6-9%, the value for the -conglycinin preparation being about 1.5 times higher than that for the glycinin preparation. The -conglycinin and glycinin preparations were respectively denatured at around 75 C and 86 C in the presence of excess water, whereas the denaturation temperature of both preparations was markedly increased by decreasing sorbed water content below 40%, corresponding well with the unfrozen water content.Key words: soybean protein isolate; water sorption isotherm; thermal stability; unfrozen water; differential scanning calorimetry Soybean protein, the abundant commercially available vegetable protein, is widely used as an ingredient of various food products due to its manifold functional properties and low cost. Heat treatment is well known in food processing to be an essential operation, and results in the denaturation of protein depending on the heating conditions. Denaturation often causes substantial change in such functional characteristics as solubility, digestibility, biological activity, rheological properties, emulsifying properties, and gelling properties. In particular, drying, extrusion cooking, and dry heating are generally performed at a relatively high temperature or pressure, so that close attention needs to be paid to controlling the denaturation of protein.It is also known that a soybean protein isolate composed of the two major proteins, -conglycinin and glycinin, denatures at about 76 C and 91 C, respectively, in a 10% dispersion, 1) that environmental conditions such as the pH value, 1) salt, 2) and protein concentration 3) affect the denaturation behavior, and that a heat treatment has a negative effect on the solubility and water absoption.4) Since the thermal denaturation of such other proteins as myoglobin, 5) lysozyme, 6) collagen, bovine serum albumin, 7) ovalbumin, 8) and keratin 9) is greatly affected by the water content, the water content is considered to be one of the most fundamental factors controlling denaturation. In respect of soybean protein, Sheard et al.3) were first to report the denaturation temperatures of soybean isolates (7S and 11S proteins, i.e., -conglycinin and glycinin) containing from 5% to 94% moisture (about 5.3% to 1,600% on a dry basis). They showed that the denaturation temperatures of -conglycinin and glycinin almost linearly increased from about 72 C to 102 C and from about 89 C to 129 C, respectively, as peak values evaluated by differential scanning calorimetry with a decreasi...

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Shrinkage of collagen fibres: A differential scanning calorimetric study

Cited by 95 publications

References 13 publications

Second Harmonic Generation Microscopy: A Tool for Spatially and Temporally Resolved Studies of Heat Induced Structural Changes in Meat

Second Harmonic Generation Microscopy: A Tool for Spatially and Temporally Resolved Studies of Heat Induced Structural Changes in Meat

Effect of thermal denaturation on water-collagen interactions: NMR relaxation and differential scanning calorimetry analysis

Effect of Sorbed Water on the Thermal Stability of Soybean Protein

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