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Katsuyoshi Nishinari - One of the best experts on this subject based on the ideXlab platform.
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Co-Gelation of gluten and gelatin as a novel functional material formation method
Journal of Food Science and Technology, 2019Co-Authors: Marta Wesołowska-trojanowska, Marta Tomczyńska-mleko, Maciej Nastaj, Siemowit Muszynski, Konrad Terpiłowski, Katsuyoshi Nishinari, Stanisław MlekoAbstract:Gelatin solution was added to the gluten dispersion to obtain 25% protein from gluten and 0, 0.3, 0.6 and 1.0% of gelatin. Heat-induced gels were formed. The gelatin was leached by immersing the gel straps in distilled water at 45 °C for 2 h. Incorporation of gelatin into the gluten gel matrix resulted in its strengthening. Increase in elastic properties with the increasing amount of gelatin was also found for the macerated gels. The tangent delta showed the minimum for the leached gel with the initial concentration of gelatin 0.6%, so probably at this concentration there was some reinforcement of gluten, or the structure of gluten matrix was formed with the best ability to include gelatin inside. FTIR (Fourier transform infrared spectroscopy) results showed, that at the 0.6% gelatin concentration more gelatin was present in the leached samples than in the 1% gelatin added samples. Gelatin gels can act as an active filler reinforcing the gluten microstructure. Leaching of gelatin from the mixed gel matrix resulted in the microstructure with visible phase separation. Generally gelatin addition gave a surface smoothing effect and lower surface roughness of the obtained gels. Pure gluten gels soaking in hot water resulted in the decreased roughness. Possibility of manipulation with gluten gels surface roughness by co-gelling with gelatin can have an influence on the application of such gels as matrices for active ingredients.
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protein polysaccharide cogel formation based on gelatin and chemically modified schizophyllan
Biomacromolecules, 2005Co-Authors: Yapeng Fang, Rheo Takahashi, Katsuyoshi NishinariAbstract:In the work, aldehyde groups were quantitatively introduced into schizophyllan (SPG) side chains through periodate oxidation. The periodate-oxidized SPG (POSPG) forms an elastic gel with gelatin. The cogel formation is based on the Schiff-base reaction between the amino groups of gelatin chains and the aldehyde groups of POSPG chains. The POSPG/gelatin cogel has an elastomeric character with a very small value of loss tangent. The Gelation kinetics and gel properties were discussed as a function of POSPG concentration, gelatin concentration, oxidation degree, temperature, and pH. This method can be used to design a large variety of cogels between SPG and proteins.
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Protein/polysaccharide cogel formation based on gelatin and chemically modified schizophyllan.
Biomacromolecules, 2005Co-Authors: Yapeng Fang, Rheo Takahashi, Katsuyoshi NishinariAbstract:In the work, aldehyde groups were quantitatively introduced into schizophyllan (SPG) side chains through periodate oxidation. The periodate-oxidized SPG (POSPG) forms an elastic gel with gelatin. The cogel formation is based on the Schiff-base reaction between the amino groups of gelatin chains and the aldehyde groups of POSPG chains. The POSPG/gelatin cogel has an elastomeric character with a very small value of loss tangent. The Gelation kinetics and gel properties were discussed as a function of POSPG concentration, gelatin concentration, oxidation degree, temperature, and pH. This method can be used to design a large variety of cogels between SPG and proteins.
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Rheological and DSC study of sol-gel transition in aqueous dispersions of industrially important polymers and colloids
Colloid and Polymer Science, 1997Co-Authors: Katsuyoshi NishinariAbstract:Gelation kinetics, mechanical spectra, thermal scanning rheology (TSR), and differential scanning calorimetry (DSC) in aqueous solutions of gelling polymers and colloids such as seaweed polysaccharides (agarose, carrageenans), microbial polysaccharides (gellan, curdlan), plant polysaccharides (methylcellulose), globular proteins (casein, glycinin, β -conglycinin), fibrous proteins (gelatin, fibrin), and polyvinyl alcohol, which are related to foods, cosmetics, biomedical and pharmaceutical applications, are described. Some Gelation processes at a constant temperature have been treated successfully by an equation of first order kinetics or by other modified equations, and the molecular mechanism of gel formation is discussed briefly. For water-soluble polymers, the criterion of the gel or sol based on the frequency dependence of storage and loss moduli gives valuable informations. TSR and DSC are complementary, and the combination of these methods has been proved to be useful.
Iline Steyaert - One of the best experts on this subject based on the ideXlab platform.
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gelatin nanofibers analysis of triple helix dissociation temperature and cold water solubility
Food Hydrocolloids, 2016Co-Authors: Iline Steyaert, Hubert Rahier, Sandra Van Vlierberghe, Jos Olijve, Karen De ClerckAbstract:Abstract Gelatin nanofibrous structures, characterized by high specific surface area and high porosity, have been widely researched for biomedical and food applications. The present paper researches the potential of electrospinning to produce a nanofibrous cold-gelling (or instant) gelatin product. Our results show that gelatin nanofibers are cold-water-soluble due to their high surface-to-volume ratio, facilitating easy water penetration and dissolution, and this for several gelatin types. Additionally, fast Gelation after dissolution in cold water indicates that the electrospinning process does not significantly reduce the gelatin molecular weight, nor compromise triple helix formation. These conclusions were supported by thorough investigation of the internal gelatin structure, using a new approach based on modulated temperature scanning calorimetry. Oscillation rheology revealed that the nanofiber-based gels have moduli comparable to powder-based gels. Gelatin nanofibers can thus be used as instant gelatin product, without the drawbacks of traditional amorphous instant gelatins such as sensitivity to moisture, low wettability and low modulus of the cold gel. Using the approach reported here, every electrospinnable, but non-cold-water-soluble gelatin can be transformed into a cold-water-soluble variant, regardless of the type or modification. Electrospinning can thus offer enormous flexibility in materials selection, enabling the production of cold gels loaded with temperature-sensitive components, UV-cross-linkable cold gels, etc.
Zong Cai Tu - One of the best experts on this subject based on the ideXlab platform.
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Effect of extraction temperature on the gelling properties and identification of porcine gelatin
Food Hydrocolloids, 2019Co-Authors: Zi-zi Hu, Yun-hua Ye, Huang Xu, Zong Cai TuAbstract:Abstract High-performance liquid chromatography (HPLC) and linear-ion trap (LTQ)/Orbitrap high-resolution mass spectrometry were used to identify porcine gelatins extracted at different temperatures. Moreover, shear stress rheological detection techniques and a texture analyzer were applied to evaluate the gelling properties of various porcine gelatins. The results showed that, with an increased in the extraction temperature, the gel strength, Gelation point and melting point of the porcine gelatin gradually decreased, indicating that the temperature significantly affected the gelling properties of gelatin. HPLC- LTQ/Orbitrap high-resolution mass spectrometry indicated that porcine gelatins prepared at different extraction temperatures also showed internal uniqueness, namely, diverse marker peptides for gelatin identification. Compared with the established theoretical sequence fragment database of porcine gelatin and bovine gelatin, 64, 74 and 71 tryptic porcine peptides in gelatins were extracted at 55 °C, 65 °C and 75 °C, respectively. Notably, regardless of the extraction temperature, 47 common peptides were detected in the tryptic hydrolysates of porcine gelatins. Using these common tryptic peptides can effectively improve the accuracy of the porcine gelatin identification.
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rheological behavior emulsifying properties and structural characterization of phosphorylated fish gelatin
Food Chemistry, 2018Co-Authors: Tao Huang, Zong Cai Tu, Xinchen Shangguan, Hui Wang, Nidhi BansalAbstract:Rheological, microstructural and emulsifying properties of fish gelatin phosphorylated using sodium trimetaphosphate (STMP) were studied. Phosphorylation was carried out at 50 °C for 0, 0.5, 1 or 2 h. Rheological behaviors indicated that phosphorylation decreased Gelation rate constant (k ) and apparent viscosity of gelatin solutions. Phosphorylation time was inversely proportional to tan δ; gelling and melting points of fish gelatin gels; however gel properties could be improved by short time of phosphorylation. Scanning electron microscopy and atomic force microscopy revealed that longer time of phosphorylation resulted in looser gel network with more aggregation. Longer phosphorylation time could stabilize fish gelatin emulsions, and endowed emulsions with smaller particle size and lower coefficient viscosity, but higher ζ-potential values. These results suggested that phosphorylation could be applied to obtain fish gelatin with varying functional properties suitable for numerous industrial applications.
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pectin and enzyme complex modified fish scales gelatin rheological behavior gel properties and nanostructure
Carbohydrate Polymers, 2017Co-Authors: Tao Huang, Zong Cai Tu, Xinchen Shangguan, Hui Wang, Lu Zhang, Nanhai Zhang, Nidhi BansalAbstract:The rheological behavior, gel properties and nanostructure of complex modified fish scales gelatin (FSG) by pectin and microbial transglutaminase (MTGase) were investigated. The findings suggested that MTGase and pectin have positive effect on the Gelation point, melting point, apparent viscosity and gel properties of FSG. The highest values of gel strength and melting temperature could be observed at 0.8% (w/v) pectin. Nevertheless, at highest pectin concentration (1.6% w/v), the gel strength and melting temperature of complex modified gelatin gels decreased. Atomic force microscopy (AFM) and scanning electron microscopy (SEM) analysis revealed that MTGase catalyzed cross-links among soluble fish scales gelatin – pectin complexes, which could be responsible for the observed increase in rheological behavior, gel strength and melting temperature of modified complex gels.
Ali Kamali - One of the best experts on this subject based on the ideXlab platform.
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Freeze-gelled alginate/gelatin scaffolds for wound healing applications: An in vitro, in vivo study
Materials science & engineering. C Materials for biological applications, 2020Co-Authors: Homa Afjoul, Amir Shamloo, Ali KamaliAbstract:Abstract In this study, fabrication of a three-dimensional porous scaffold was performed using freeze Gelation method. Recently, fabrication of scaffolds using polymer blends has become common for many tissue engineering applications due to their unique tunable properties. In this work, we fabricated alginate-gelatin porous hydrogels for wound healing application using a new method based on some modifications to the freeze-Gelation method. Alginate and gelatin were mixed in three different ratios and the resulting solutions underwent freeze Gelation to obtain 3D porous matrices. We analyzed the samples using different characterization tests. The scanning electron microscopy (SEM) results indicated that the freeze Gelation method was successful in obtaining porous morphologies for all the fabricated alginate-gelatin samples as previously was seen in single-polymer fabrication using this method. The alginate to gelatin ratio affected swelling, biodegradation, cell culture and mechanical properties of the matrices. The scaffold with the lowest content of gelatin had the highest swelling ratio while biodegradation and cell proliferation and viability were increased with the gelatin content. Regarding the mechanical properties, as the gelatin content increased, the scaffold became more ductile and showed higher tensile strength. The in-vivo results also showed the biocompatibility of the blend scaffold and its positive role in wound healing process in rats. The low-cost procedure used in this study to fabricate the porous alginate-gelatin scaffolds can be adapted and modified to suit different tissue engineering applications.
Vincent Ball - One of the best experts on this subject based on the ideXlab platform.
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Hofmeister Effects of Monovalent Sodium Salts in the Gelation Kinetics of Gelatin
Journal of Physical Chemistry B, 2019Co-Authors: Vincent BallAbstract:The Gelation kinetics of gelatin depends on the presence of electrolytes and the influence of cations with variable valency has been recently emphasized. However acquired knowledge shows that the nature of anions has more influence on various properties of aqueous solutions than the nature of the cations. It is shown herein, using sodium salts of monovalent anions, that the Gelation kinetics of gelatin is accelerated by the presence of highly kosmotropic anions like fluoride and strongly slowed down, eventually inhibited, by the presence of chaotropic anions like thiocyanate and perchlorate. Overall the parameter characterizing the Gelation kinetics, k, is a linear function of the polarizability of the used salt in aqueous solution, which has been quantified independently by refractometry and using the Lorentz-Lorenz formula. It is also found 2 that the same parameter characterizing the Gelation kinetics is a linear function of the viscosity B coefficient taken from the literature. The linear correlation coefficients are excellent in the case of halide anions (F-, Cl-, Br-, I-) but poorer when non spherical anions like NO 3-, SCN-and ClO 4-are considered.
