Gelatin

Keenan, Thomas

doi:10.1002/0471238961.0705120111050514.a01

Cited by 10 publications

(4 citation statements)

References 24 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Electrospinning can be applied to both synthetic and natural polymers, including polysaccharides and proteins, with collagen, silk fibroin, and gelatin being the most studied ones. Gelatin is known to have biocompatibility and biodegradability similar to collagen . In fact, it is easily obtained by partial hydrolysis of collagen from animal tissues such as skin, muscle, and bone.…”

Section: Introductionmentioning

confidence: 99%

Electrospinning of gelatin fibers using solutions with low acetic acid concentration: Effect of solvent composition on both diameter of electrospun fibers and cytotoxicity

Erencia

Cano

Tornero

et al. 2015

J of Applied Polymer Sci

104

View full text Add to dashboard Cite

Gelatin fibers were prepared by electrospinning of gelatin/acetic acid/water ternary mixtures with the aim of studying the feasibility of fabricating gelatin nanofiber mats at room temperature using an alternative benign solvent by significantly reducing the acetic acid concentration. The results showed that gelatin nanofibers can be optimally electrospun with low acetic acid concentration (25% v/v) combined with gelatin concentrations higher than 300 mg/ml. Both gelatin solutions and electrospun gelatin mats (prepared with different acetic acid aqueous solutions) were analyzed by FTIR and DSC techniques in order to determine the chemical and structure changes of the polymer. The electrospun gelatin mats fabricated from solutions with low acetic acid content showed some advantages as the maintenance of the decomposition temperature of the pure gelatin (~230ºC) and the reduction of the acid content on electrospun mats, which allowed to reach a cell viability upper than 90% (analyzed by cell viability test using human dermal fibroblast and embryonic kidney cells). This study has also analyzed the influence of gelatin and acetic acid concentration both on the solution viscosity and the electrospun fiber diameter, obtaining a clear relationship between these parameters.

show abstract

Section: Introductionmentioning

confidence: 99%

Electrospinning of gelatin fibers using solutions with low acetic acid concentration: Effect of solvent composition on both diameter of electrospun fibers and cytotoxicity

Erencia

Cano

Tornero

et al. 2015

J of Applied Polymer Sci

104

View full text Add to dashboard Cite

show abstract

“…The latter is also the case since gelatin is frequently employed in various food, pharmaceutical, and photographic applications in order to tune properties such as emulsion stability and viscosity. 4,5 Second, gelatin forms helical structures in a temperature-dependent manner, and gelatin gel networks have previously been found to form with various crystalline (helical) contents depending on the origin of the gelatin as well as the gel formation conditions. 6,7 The interfacial behavior of gelatin can be anticipated to show an analogous behavior which, 8,9 in turn, could be expected to influence the susceptibility of gelatin for enzymatic degradation.…”

Section: Introductionmentioning

confidence: 99%

Ellipsometry and TIRF Studies of Enzymatic Degradation of Interfacial Proteinaceous Layers

et al. 2001

View full text Add to dashboard Cite

Ellipsometry and total internal reflectance fluorescence spectroscopy (TIRF) have been employed to investigate the layer structure of gelatin adsorbed from aqueous solutions onto silica/glass and methylated silica/glass, as well as the effects of addition of the proteolytic enzymes krillase and trypsin, in relation to temperature, enzyme concentration, and enzymatic activity. The results for the hydrophilic substrates show that homogeneous and heterogeneous exchange occurs readily, as does autolysis of trypsin at the interface. At the hydrophobic substrates, the effect of exchange is limited and a residual gelatin fraction is present at the interface throughout. The interfacial behavior of gelatin above and below the helix formation temperature (T helix) shows that more extended surface layers are formed at both substrates below T helix. At the hydrophilic substrates, the higher adsorbed layer thickness below T helix is mainly due to the adsorption of more gelatin than at the higher temperature, whereas, at the hydrophobic substrates, the increase in layer thickness below T helix is due to a decrease in packing density. Enzyme addition to preadsorbed gelatin at methylated silica results in the transition to a thinner and denser layer that contains both residual gelatin and proteolytic enzymes (i.e., krillase or trypsin). At hydrophobic surfaces, a faster and more extensive degradation of the gelatin layer is observed with increasing krillase concentration, the effect of which is similar above and below T helix. The effect of trypsin addition to preadsorbed gelatin is enhanced at T < T helix, which is somewhat counterintuitive considering the structure of gelatin in relation to temperature. Quantitatively, the degree of gelatin degradation after addition of trypsin at T < T helix was found to be higher than after addition of a 500 times higher concentration at T > T helix. Finally, the exposure of preadsorbed gelatin to inactivated krillase showed a nearly complete elimination in the effects observed upon addition of intact krillase. This indicated that the enzymatic activity of krillase in its native form plays a major role for the interaction between krillase and preadsorbed gelatin.

show abstract

“…99.4%) and the exo (ca. 0.6 %) 24. The ratio of the total peak integral of the olefinic H to the total peak integral of aliphatic H was found to be 0.25 (0.250 calculated from the formula of the salt, NaOOCDCPDCOONa).…”

Section: Resultsmentioning

confidence: 90%

Thermally reversible covalently bonded linear polymers prepared from a dihalide monomer and a salt of dicyclopentadiene dicarboxylic acid

Chen

Ruckenstein

2000

J. Polym. Sci. A Polym. Chem.

View full text Add to dashboard Cite

Gelatin

Cited by 10 publications

References 24 publications

Electrospinning of gelatin fibers using solutions with low acetic acid concentration: Effect of solvent composition on both diameter of electrospun fibers and cytotoxicity

Electrospinning of gelatin fibers using solutions with low acetic acid concentration: Effect of solvent composition on both diameter of electrospun fibers and cytotoxicity

Ellipsometry and TIRF Studies of Enzymatic Degradation of Interfacial Proteinaceous Layers

Thermally reversible covalently bonded linear polymers prepared from a dihalide monomer and a salt of dicyclopentadiene dicarboxylic acid

Contact Info

Product

Resources

About