Hollow chitosan microspheres prepared by an oil1-in-water-in-oil2 double emulsion method
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Genipin
Surface-area-to-volume ratio
We investigated the temperature-responsive gelation of collagen/genipin solutions using pepsin-solubilized collagen (PSC) and acid-solubilized collagen (ASC) as substrates. Gelation occurred in the PSC/genipin solutions at genipin concentrations 0–2 mM under moderate change in temperature from 25 to 37°C. The PSC/genipin solutions exhibited fluidity at room temperature for at least 30 min, whereas the ASC/genipin solutions rapidly reached gel points. In specific cases PSC would be preferred over ASC as an injectable gel system. The temperature-responsive gelation of PSC/genipin solutions was due to temperature responses to genipin crosslinking and collagen fibril formation. The elastic modulus of the 0.5% PSC/genipin gel system could be adjusted in a range of 2.5 to 50 kPa by the PSC and genipin concentrations, suggesting that a PSC/genipin solution is a potential injectable gel system for drug and cell carriers, with mechanical properties matching those of living tissues.
Genipin
Collagen fibril
Type I collagen
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Genipin
Gardenia jasminoides
Gelatin
Biocompatibility
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Chitosan and gelatin have good biocompatibility.However,sometimes their mechanical performances cannot match the requirement for medical implanted materials.Crosslinking is a usual effective method to enhance the mechanical strength of polymers.The conventional crosslinkers of chitosan or gelatin are aldehydes,but their physiological toxicities limit the application of chitosan and gelatin.Here genipin, a biocrosslinker,was selected to take the place of aldehyde.The crosslinking mechanism and kinetics of chitosan and genipin were investigated by UV spectra, and the corresponding models were established especially.The mechanical properties,swelling degree and degradation behaviors of the chitosan-genipin and chitosan-gelatin-genipin gels were also researched.Results show that the mechanical performance of chitosan-gelatin complex system crosslinked by genipin could be improved in a certain range by changing the crosslinking degree.
Genipin
Gelatin
Biocompatibility
Mechanical strength
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Genipin
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Genipin
Gelatin
Glutaraldehyde
Thermal Stability
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To review the application of genipin for the modification of natural biomaterials as a crosslinking agent and progress in research.Domestic and foreign literature on application of genipin for the modification of natural biomaterials as a crosslinking agent was thoroughly reviewed. Results Genipin is an effective natural crosslinking agent with a very low level of cytotoxicity compared with conventional synthetic crosslinking agents. Tissues fixed with genipin can maintain a high level of stability as well as resistance to enzymatic degradation.Genipin is a promising substitute for conventional synthetic crosslinking agents, which has offered an alternative for modification of natural biomaterials for tissue engineering.
Genipin
Natural polymers
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Genipin
Gelatin
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Abstract Genipin is known to polymerize under basic conditions, and the obtained genipin oligomers might have an impact on the chemical and physical properties of the crosslinked materials. In this study, we intend to mimic the experimental condition in which genipin is used as a chemical crosslinker. We focus on the degradation of genipin at neutral and slightly acidic conditions using NMR. We report genipin polymerization at neutral and acidic conditions. Unlike dialdehyde crosslinkers, genipin requires heating to promote its crosslinking activity. We found that elevated temperatures enhance the degradation of genipin and promote its polymerization.
Genipin
Degradation
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Genipin blue is a pigment prepared from the reaction of genipin with amino acid. We describe herein a new method used to prepare genipin blue, water-soluble blue pigments, through the reaction of hen egg protein with genipin. The effects of reaction time, reaction temperature, the pH value of the solution and the mass ratio of the reactants on the preparation are studied. One part of genipin reacted with eight parts of hen egg protein (w/w) in water (pH value of reaction system 7.5) at 60°C for 96 h and gave blue pigments with the maximum colour value of 146.2. The blue pigments showed identical absorption activity in UV spectroscopy (λ max = 584 nm) to that of gardenia blue pigments, which were prepared from the reaction of genipin with amino acid.
Genipin
Gardenia
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