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Collagen Films (collagen + film)

Distribution by Scientific Domains
Chemistry57%

Selected Abstracts

Influence of cosolvents and in situ forming hydroxyapatite on the mechanical characteristics of collagen films

JOURNAL OF BIOMEDICAL MATERIALS RESEARCH, Issue 1 2002
Hsiu-O Ho
Abstract Collagen was processed into films in mixtures containing various ratios of water, propylene glycol, and ethanol. An experimental mixture design was applied to characterize the effects of individual solvents and their interactions on the mechanical properties of collagen films. Scanning electron microscopy (SEM) was used to examine the surface properties of collagen films. The ultimate tensile strength (UTS) and related characteristics of collagen films were also evaluated with dynamic mechanical analysis. The effect of in situ forming hydroxyapatite (HAP) within collagen films at a concentration of 10 mM on the physical characteristics of these films was evaluated by the same methods. With X-ray and SEM examinations, it was confirmed that HAP was formed inside the collagen film. However, the UTS of collagen films without HAP was 4,5 times higher than that with HAP. This was probably due to the discontinuity of the film structure caused by HAP in the collagen films. The results of a statistical analysis of the experimental design revealed the influence of the solvent mixtures on the mechanical properties of the collagen films with and without HAP, showing similar responses for the UTS and modulus of elasticity. Both parameters showed a maximal response in the solvent range containing a lower percentage of ethanol with the desired percentage of propylene glycol to plasticize the collagen films. © 2002 Wiley Periodicals, Inc. J Biomed Mater Res 62: 22,29, 2002 [source]

Structural transition during thermal denaturation of collagen in the solution and film states,

CHIRALITY, Issue 1 2009
Ganesh Shanmugam
Abstract Temperature dependent vibrational circular dichroism (VCD) spectra of type I collagen, in solution and film states, have been measured. These spectra obtained for solution sample suggest that the thermal denaturation of collagen results in transition from poly- L -proline II (PPII) to unordered structure. The PPII structure of collagen is identified by the presence of negative VCD couplet in the amide I region, while the formation of unordered structure is indicated by the disappearance of VCD in the amide I region. The temperature dependent spectra obtained for the supported collagen film indicated a biphasic transition, which is believed to be the first vibrational spectroscopic report to support a biphasic transition during thermal denaturation of collagen film. The temperature dependent spectra of collagen films suggest that the thermal stability of collagen structure depends on its state and decreases in the order: supported film > free standing film > solution state. These observations are believed to be significant in the VCD spectroscopic analysis of secondary structures of proteins and peptides. Chirality, 2009. © 2008 Wiley-Liss, Inc. [source]

Solubility and mechanical properties of heat-cured whey protein-based edible films compared with that of collagen and natural casings

INTERNATIONAL JOURNAL OF DAIRY TECHNOLOGY, Issue 2 2007
S AMIN
Water solubility, tensile strength (TS), wet strength (WS) and elongation at break (%E) of whey protein isolate (WPI) films were compared to that of collagen films and natural casings. Increase in heat-curing temperature and time caused decreased (P < 0.001) water solubility and increased TS and WS of the films. Heat-cured WPI films with similar properties (solubility, TS, WS and %E) to collagen films were obtained by optimizing heat-curing conditions. Overall, natural casings had lower solubility, TS and %E but higher WS than collagen and heat-cured WPI films. Heat-cured WPI films have the potential as an alternative to collagen films and casings. [source]

Influence of cosolvents and in situ forming hydroxyapatite on the mechanical characteristics of collagen films

JOURNAL OF BIOMEDICAL MATERIALS RESEARCH, Issue 1 2002
Hsiu-O Ho
Abstract Collagen was processed into films in mixtures containing various ratios of water, propylene glycol, and ethanol. An experimental mixture design was applied to characterize the effects of individual solvents and their interactions on the mechanical properties of collagen films. Scanning electron microscopy (SEM) was used to examine the surface properties of collagen films. The ultimate tensile strength (UTS) and related characteristics of collagen films were also evaluated with dynamic mechanical analysis. The effect of in situ forming hydroxyapatite (HAP) within collagen films at a concentration of 10 mM on the physical characteristics of these films was evaluated by the same methods. With X-ray and SEM examinations, it was confirmed that HAP was formed inside the collagen film. However, the UTS of collagen films without HAP was 4,5 times higher than that with HAP. This was probably due to the discontinuity of the film structure caused by HAP in the collagen films. The results of a statistical analysis of the experimental design revealed the influence of the solvent mixtures on the mechanical properties of the collagen films with and without HAP, showing similar responses for the UTS and modulus of elasticity. Both parameters showed a maximal response in the solvent range containing a lower percentage of ethanol with the desired percentage of propylene glycol to plasticize the collagen films. © 2002 Wiley Periodicals, Inc. J Biomed Mater Res 62: 22,29, 2002 [source]

Structural transition during thermal denaturation of collagen in the solution and film states,

CHIRALITY, Issue 1 2009
Ganesh Shanmugam
Abstract Temperature dependent vibrational circular dichroism (VCD) spectra of type I collagen, in solution and film states, have been measured. These spectra obtained for solution sample suggest that the thermal denaturation of collagen results in transition from poly- L -proline II (PPII) to unordered structure. The PPII structure of collagen is identified by the presence of negative VCD couplet in the amide I region, while the formation of unordered structure is indicated by the disappearance of VCD in the amide I region. The temperature dependent spectra obtained for the supported collagen film indicated a biphasic transition, which is believed to be the first vibrational spectroscopic report to support a biphasic transition during thermal denaturation of collagen film. The temperature dependent spectra of collagen films suggest that the thermal stability of collagen structure depends on its state and decreases in the order: supported film > free standing film > solution state. These observations are believed to be significant in the VCD spectroscopic analysis of secondary structures of proteins and peptides. Chirality, 2009. © 2008 Wiley-Liss, Inc. [source]