Effect of cyclic freeze–thawing process on the structure and properties of collagen

Ding, Chaoliang; Zhang, Min; Li, Guoying

doi:10.1016/j.ijbiomac.2015.06.047

Cited by 25 publications

(9 citation statements)

References 30 publications

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“…Thus, the peaks at 200 • C suggest that the phase transition of dry collagen is more probably a denaturation than a melting process of the stable crystalline structure of collagen. The value of activation energy confirms that dry denaturation is a complex process, which probably consists in a rate-limited reversible step leading to an irreversibly denatured state of the proteins [64].…”

Section: Multi-frequency Tensile and Compressive Loading Of Nssupporting

confidence: 57%

Thermo-Mechanical Behaviour of Human Nasal Cartilage

et al. 2020

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The aim of this study was to undergo a comprehensive analysis of the thermo-mechanical properties of nasal cartilages for the future design of a composite polymeric material to be used in human nose reconstruction surgery. A thermal and dynamic mechanical analysis (DMA) in tension and compression modes within the ranges 1 to 20 Hz and 30 °C to 250 °C was performed on human nasal cartilage. Differential scanning calorimetry (DSC), as well as characterization of the nasal septum (NS), upper lateral cartilages (ULC), and lower lateral cartilages (LLC) reveals the different nature of the binding water inside the studied specimens. Three peaks at 60–80 °C, 100–130 °C, and 200 °C were attributed to melting of the crystalline region of collagen matrix, water evaporation, and the strongly bound non-interstitial water in the cartilage and composite specimens, respectively. Thermogravimetric analysis (TGA) showed that the degradation of cartilage, composite, and subcutaneous tissue of the NS, ULC, and LLC take place in three thermal events (~37 °C, ~189 °C, and ~290 °C) showing that cartilage releases more water and more rapidly than the subcutaneous tissue. The water content of nasal cartilage was estimated to be 42 wt %. The results of the DMA analyses demonstrated that tensile mode is ruled by flow-independent behaviour produced by the time-dependent deformability of the solid cartilage matrix that is strongly frequency-dependent, showing an unstable crystalline region between 80–180 °C, an amorphous region at around 120 °C, and a clear glass transition point at 200 °C (780 kJ/mol). Instead, the unconfined compressive mode is clearly ruled by a flow-dependent process caused by the frictional force of the interstitial fluid that flows within the cartilage matrix resulting in higher stiffness (from 12 MPa at 1 Hz to 16 MPa at 20 Hz in storage modulus). The outcomes of this study will support the development of an artificial material to mimic the thermo-mechanical behaviour of the natural cartilage of the human nose.

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Section: Multi-frequency Tensile and Compressive Loading Of Nssupporting

confidence: 57%

Thermo-Mechanical Behaviour of Human Nasal Cartilage

et al. 2020

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“…Several explanations are possible including destruction of the collagenous structure due to formation of ice lenses or disruption of the structure by destruction of the residential cells in the tendon. Ding et al[19] were able to show that multiple freeze-thaw-cycles applied to collagen solution led to formation of a microporous structure in which the pores were mainly filled with water during the frozen storage. The porous network appeared to become smaller and more regular applying more freezing cycles, which could be due to increasing number of entanglement points during the freezing process.…”

Section: Discussionmentioning

confidence: 99%

Cryopreservation of tendon tissue using dimethyl sulfoxide combines conserved cell vitality with maintained biomechanical features

et al. 2019

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Biomechanical research on tendon tissue evaluating new treatment strategies to frequently occurring clinical problems regarding tendon degeneration or trauma is of expanding scientific interest. In this context, storing tendon tissue deep-frozen is common practice to collect tissue and analyze it under equal conditions. The commonly used freezing medium, phosphate buffered saline, is known to damage cells and extracellular matrix in frozen state. Dimethyl sulfoxide, however, which is used for deep-frozen storage of cells in cell culture preserves cell vitality and reduces damage to the extracellular matrix during freezing. In our study, Achilles tendons of 26 male C57/Bl6 mice were randomized in five groups. Tendons were deep frozen in dimethyl sulfoxide or saline undergoing one or four freeze-thaw-cycles and compared to an unfrozen control group analyzing biomechanical properties, cell viability and collagenous structure. In electron microscopy, collagen fibrils of tendons frozen in saline appeared more irregular in shape, while dimethyl sulfoxide preserved the collagenous structure during freezing. In addition, treatment with dimethyl sulfoxide preserved cell viability visualized with an MTT-Assay, while tendons frozen in saline showed no remaining metabolic activity, indicating total destruction of cells during freezing. The biomechanical results revealed no differences between tendons frozen once in saline or dimethyl sulfoxide. However, tendons frozen four times in saline showed a significantly higher Young’s modulus over all strain rates compared to unfrozen tendons. In conclusion, dimethyl sulfoxide preserves the vitality of tendon resident cells and protects the collagenous superstructure during the freezing process resulting in maintained biomechanical properties of the tendon.

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“…On the one hand, collagen is signi cant to build up the tenacity of muscles and bones, especially for those who have been su ering from lumbar debility and physically weak bodies and on the other hand, collagen ensures that adolescents grow healthy and elderly people su er less from osteoporosis. Moreover, it can accelerate wound healing [9]. In addition, beef tendon foods can be used as additives, nutrition enhancers, etc.…”

Section: Introductionmentioning

confidence: 99%

Effects of Various Processing Methods on the Ultrastructure of Tendon Collagen Fibrils from Qinchuan Beef Cattle Observed with Atomic Force Microscopy

Wan

Song

et al. 2018

Journal of Food Quality

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Atomic force microscopy was utilized to study the e ects of ultrasound oscillation, microwave heating, water bath cooking, and acidbase soaking on the ultrastructure of collagen brils of Qinchuan beef cattle tendons. D-spacing length and roughness of collagen brils always showed a 1.02% increment in the group which was processed for 20 min rather than for 10 min under di erent ultrasound frequencies. Microwave heating had a slight impact on D-spacing length and roughness at lower power (140-560 W), and collagen brils always showed a 1.02% increment for 20 min. en, visible changes were noted with increasing power and time. D-spacing length reduced by 1.01% at 50°C for treatment periods of 10 min, 20 min, and 30 min, and there was no obvious change at 60°C; the periodic structure disappeared after cooking for 20 min, when brils had become gelatinized at 70°C. Collagen brils became disorganized at pH 3, following acid-base soaking. e present study indicated that acid-base soaking had an outstanding e ect on the ultrastructure of collagen brils, especially in an acidic environment in consideration of the special structure of collagen.

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Effect of cyclic freeze–thawing process on the structure and properties of collagen

Cited by 25 publications

References 30 publications

Thermo-Mechanical Behaviour of Human Nasal Cartilage

Thermo-Mechanical Behaviour of Human Nasal Cartilage

Cryopreservation of tendon tissue using dimethyl sulfoxide combines conserved cell vitality with maintained biomechanical features

Effects of Various Processing Methods on the Ultrastructure of Tendon Collagen Fibrils from Qinchuan Beef Cattle Observed with Atomic Force Microscopy

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