Analysis of bimodal thermally-induced denaturation of type I collagen extracted from calfskin

Staicu, Teodora; Cı̂rcu, Viorel; Ioniţă, Gabriela; Ghica, C.; Popa, Vlad Tudor; Micutz, Marin

doi:10.1039/c5ra02708j

Cited by 16 publications

(11 citation statements)

References 97 publications

(133 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…In addition, a secondary exothermal peak (32.9 ± 0.31 °C) was identified in the DSC thermogram (Figure 3B). It was consistent with our observation on the viscosity changes in T. flavidus collagen (Figure 3A), indicating a partial denaturation of collagen supramolecular structure due to defibration of thermally unstable hydroxyproline-free sequence in collagen triple helices [28].…”

Section: Resultssupporting

confidence: 92%

See 1 more Smart Citation

Electrodialysis Extraction of Pufferfish Skin (Takifugu flavidus): A Promising Source of Collagen

Chen

et al. 2019

Marine Drugs

View full text Add to dashboard Cite

Collagen is widely used in drugs, biomaterials, foods, and cosmetics. By-products of the fishing industry are rich sources of collagen, which can be used as an alternative to collagen traditionally harvested from land mammals. However, commercial applications of fish-based collagen are limited by the low efficiency, low productivity, and low sustainability of the extraction process. This study applied a new technique (electrodialysis) for the extraction of Takifugu flavidus skin collagen. We found electrodialysis to have better economic and environmental outcomes than traditional dialysis as it significantly reduced the purification time and wastewater (~95%) while maintaining high extraction yield (67.3 ± 1.3 g/100 g dry weight, p < 0.05). SDS-PAGE, amino acid composition analysis, and spectrophotometric characterization indicated that electrodialysis treatment retained the physicochemical properties of T. flavidus collagen. Heavy metals and tetrodotoxin analyses indicated the safety of T. flavidus collagen. Notably, the collagen had similar thermal stability to calf skin collagen, with the maximum transition temperature and denaturation temperature of 41.8 ± 0.35 and 28.4 ± 2.5 °C, respectively. All evidence suggests that electrodialysis is a promising technique for extracting collagen in the fishing industry and that T. flavidus skin collagen could serve as an alternative source of collagen to meet the increasing demand from consumers.

show abstract

Section: Resultssupporting

confidence: 92%

“…They have been reported to decrease the entropic cost of collagen folding by preorganizing individual poly-Pro II chain [27]. They can also stabilize collagen triple helices via interchain hydrogen bond through hydroxyl groups [28]. The content of imino acids is therefore an important factor modulating collagen thermal stability [27,29].…”

Section: Resultsmentioning

confidence: 99%

Electrodialysis Extraction of Pufferfish Skin (Takifugu flavidus): A Promising Source of Collagen

Chen

et al. 2019

Marine Drugs

View full text Add to dashboard Cite

show abstract

“…Thermograms for each collagen sample are shown in Figure . NC shows two characteristic peaks that were consistently observed in NC denaturation—a minor peak at 32–33°C and a major peak at 38–40°C, confirming the bimodal collagen denaturation observed by others . Data for denaturation temperature and enthalpy for all CO 2 ‐treated samples is shown in Table .…”

Section: Resultssupporting

confidence: 82%

“…The sample thermogram for NC‐U in Figure a suggests a bimodal denaturation process; this was also observed recently by Staicu et al under similar conditions. The smaller initial peak is caused by the disassembly of supramolecular complexes (that is, separation of different collagen molecules from each other) and the large second peak indicates the unfolding of each individual triple helical collagen molecule into a random coil formation.…”

Section: Discussionsupporting

confidence: 86%

Eliminating glutaraldehyde from crosslinked collagen films using supercritical CO₂

Casali

Yost

Matthews

2017

J Biomedical Materials Res

View full text Add to dashboard Cite

Collagen has received considerable attention as a biomaterial for tissue engineering because of its low immunogenicity, controllable biodegradation, and ability to influence cell growth and proliferation. Frequently, collagen scaffolds require crosslinking to improve mechanical strength, requiring agents like glutaraldehyde that have high residual cytotoxicity. A novel method for extracting residual glutaraldehyde from crosslinked collagen films with supercritical carbon dioxide (CO 2 ) is presented. CO 2 is a nontoxic, nonflammable substance that is relatively inert and can be used to process biomaterials at mild pressures and physiologic temperatures. In this work, it was first determined that type I collagen is chemically compatible with both liquid and supercritical CO 2 . Treated collagen showed minimal changes in physicochemical properties as determined by differential scanning calorimetry, gel electrophoresis, and circular dichroism. CO 2 was subsequently used to extract residual glutaraldehyde from crosslinked collagen films. Glutaraldehyde concentration was reduced by over 95%, from over 20 ppm before treatment to about 1 ppm, in only 1 h. CO 2 treatment caused negligible alteration of thermal stability but did significantly increase film stiffness and tensile strength. However, these changes were minor compared to heat-based removal of glutaraldehyde.

show abstract

“…The DSC curves show that every collagen samples exhibited a characteristic thermal denaturation peak. The minor endothermic peak (Tm 1 ) at low temperature was owing to a breakage of hydrogen bonds in the aggregates of collagen, which was apt to be neglected, and the major endothermic peak (Tm 2 ) at high temperature was initiated by the transition of triple helix to the random coil state [37,38]. Compared with Col, the thermal denaturation temperature of Col/ILs-soluble70% was reduced by 7.63°C, which is larger than the decrease of Colregenerated-35°C with 4.1°C reported by Hu et al [22] This showed the thermal stability decreased more significantly with [EMIM][Ac] concentration.…”

Section: Thermal Analysis Of Soluble Collagenmentioning

confidence: 99%

Investigation of the solubility and dispersion degree of calf skin collagen in ionic liquids

2019

J Leather Sci Eng

View full text Add to dashboard Cite

The dissolution of collagen in ionic liquids (ILs) was highly dependent on the polarity of ILs, which was influenced by their sorts and concentrations. Herein, the solubility and dispersion degree of collagen in two sorts of ILs, namely 1-ethyl-methylimidazolium tetrafluoroborate ([EMIM][BF 4 ]) with low polarity and 1-ethyl-3methylimidazolium acetate ([EMIM][Ac]) with high polarity in a concentration range from 10% to 70% at 10°C were investigated. When 150 mg of collagen was added to 30 mg of ILs, the minimum soluble collagen concentration was 0.02 mg/mL in 70% [EMIM][BF 4 ] with lowest polarity and the maximum was 3.57 mg/mL in 70% [EMIM][Ac] with highest polarity, which indicates that soluble collagen and insoluble collagen fibers were both present. For insoluble collagens, differential scanning calorimetry showed that the thermal-stability was weakened when increasing the ILs concentration and polarity, and the fiber arrangement was looser with a more uniform lyophilized structure, observed by atomic force microscopy and scanning electron microscopy. For soluble collagens, electrophoresis patterns and Fourier transform infrared spectroscopy showed that no polypeptide chain degradation occurred during dissolution, but the thermal denaturation temperature decreased by 0.26°C~7.63°C with the increase of ILs concentrations, measured by ultra-sensitive differential scanning calorimetry. Moreover, the aggregation of collagen molecules was reduced when ILs polarity was increased as determined by fluorescence measurements and dynamic light scattering, which resulted in an increased loose fiber arrangement observed by atomic force microscopy. If the structural integrity of collagen needs to be retained, then the ILs sorts and concentrations should be considered.

show abstract

Analysis of bimodal thermally-induced denaturation of type I collagen extracted from calfskin

Abstract: DSC tracks of collagen in solution revealing a bimodal behaviour during its heat-induced denaturation.

Cited by 16 publications

References 97 publications

Electrodialysis Extraction of Pufferfish Skin (Takifugu flavidus): A Promising Source of Collagen

Electrodialysis Extraction of Pufferfish Skin (Takifugu flavidus): A Promising Source of Collagen

Eliminating glutaraldehyde from crosslinked collagen films using supercritical CO₂

Investigation of the solubility and dispersion degree of calf skin collagen in ionic liquids

Contact Info

Product

Resources

About

Analysis of bimodal thermally-induced denaturation of type I collagen extracted from calfskin

Abstract: DSC tracks of collagen in solution revealing a bimodal behaviour during its heat-induced denaturation.

Cited by 16 publications

References 97 publications

Electrodialysis Extraction of Pufferfish Skin (Takifugu flavidus): A Promising Source of Collagen

Electrodialysis Extraction of Pufferfish Skin (Takifugu flavidus): A Promising Source of Collagen

Eliminating glutaraldehyde from crosslinked collagen films using supercritical CO2

Investigation of the solubility and dispersion degree of calf skin collagen in ionic liquids

Contact Info

Product

Resources

About

Eliminating glutaraldehyde from crosslinked collagen films using supercritical CO₂