Structural properties of single and mixed milk/soya protein systems

Single-component gels were prepared by cold-setting aqueous preparations of thermally processed milk and soya proteins. Small deformation mechanical measurements on soya protein samples showed a strong elastic response (G′) even at the hydration temperature (50°C). Both proteins produced an initial monotonie increase in G′ on cooling, followed by a relatively constant modulus during a subsequent time sweep at the setting temperature (5°C). Networks were fully reversible on heating; the milk protein gels melting out completely at temperatures >60°C, whereas the soya protein gels maintained significant structure even at the highest accessible temperature (95°C). The lack of thermal hysteresis or of sharp, cooperative melting was also confirmed by differential scanning calorimetry. Further investigation of the macromolecular properties of the gels, comprising G′ dependence as a function of frequency of oscillation and creep experiments, suggests that gels remain stable within the time scale of the measurements (90 min). Finally, under increasing amplitude of oscillation, networks withstood structural breakdown up to strain levels of ~70%; behaviour anticipated for biopolymer gels. Mixed gels were studied using a fixed amount of milk protein (10% w/w) with soya protein concentrations from 6 (minimum gelling requirement) to 16% w/w (solubility limit). Comparison of melting profiles (G′ vs. T) for the phase separated systems with those obtained for the individual components indicated phase-inversion from a milk protein continuous network to a soya continuous system at a soya protein concentration of ~11%. Analysis of solvent partition between the constituent phases utilized classical theory of network deswelling for polymer combinations below the phase inversion point and phase equilibria treatment for the soya continuous network with milk protein inclusions. In the case of equilibrium separation of the two components, results were expressed in terms of a single adjustable parameter, p (the ratio of solvent to polymer in one phase divided by the corresponding ratio in the other phase), indicating a soya hydrophilicity of ~1.25 times that of milk protein.     

Rheological behaviour of uncross-linked and cross-linked gelatinised waxy maize starch with pectin gels

Rheological characterisation of uncross-linked (UPS) and cross-linked (CPS) waxy maize starch with pectin was conducted to determine the influence of pectin on the properties of the starch. The viscoelastic behaviour of 5% (w/v) gel systems containing UPS and CPS polysaccharides at 25 °C was evaluated by small angle deformation oscillation rheometry. Viscoelasticity measurements of the cross-linked polysaccharides indicated that the elastic component increased after cross-linking. Among all gels studied, the properties of the CPS mixtures (ratios 2:3 and 3:2) showed quite high storage (G′) and loss (G″) moduli (compared with gels of other ratios), indicating that gels of these two particular ratios had the greatest degree of elasticity and were very well structured. The results suggest that cross-linking between starch and pectin molecules can give rise to novel rheological properties.     

Characterization of gelation time and texture of gelatin and gelatin–polysaccharide mixed gels

The effects of cooling rate, holding temperature, pH and polysaccharide concentration on gelation characteristics of gelatin and gelatin–polysaccharide mixtures were investigated using a mechanical rheometer which monitored the evolution of G′ and G″. At low holding temperatures of 0 and 4 °C, elastic gelatin gels were formed whereas a higher holding temperature of 10 °C produced less elastic gels. At slow cooling rates of 1 and 2 °C/min, gelling was observed during the cooling phase in which the temperature was decreased from room temperature to the holding temperature. On the other hand, at higher cooling rates of 4 and 8 °C/min, no gelation was observed during the cooling phase. Good gelling behavior similar to that of commercial Strawberry Jell-O^® Gelatin Dessert was observed for mixtures of 1.5 and 15 g sucrose in 100 ml 0.01 M citrate buffer containing 0.0029–0.0066 g low-acyl gellan. Also, these mixed gels were stronger than Strawberry Jell-O^® Gelatin Desserts as evidenced by higher G′ and gel strength values. At a very low gellan content of 0.0029 g, increasing pH from 4.2 to 4.4 led to a decrease in the temperature at the onset of gelation, G′ at the end of cooling, holding and melting as well as an increase in gel strength. The gelation time was found to decrease to about 40 min for gelatin/sucrose dispersions in the presence of 0.0029 g gellan at pH 4.2 whereas the corresponding time at pH 4.4 was higher (79 min). In general, the gelation time of gelatin/sucrose dispersions decreased by a factor of 2 to 3 in the presence of low-acyl gellan. The addition of low-acyl gellan resulted in an increase in the gelation rate constant from 157.4 to 291 Pa. There was an optimum low-acyl gellan content for minimum gelation time, this optimum being pH dependent. Addition of guar gum also led to a decrease in gelation time to 73 min with a corresponding increase in the gelation rate constant to 211 Pa/min though these values were not sensitive to guar gum content in the range of 0.008–0.05 g. The melting temperature of gelatin/sucrose/gellan as well as gelatin/sucrose/guar mixtures did not differ significantly from that of pure gelatin or Strawberry Jell-O^® Gelatin Desserts. At pH 4.2, the melting rate constant was highest at a low-acyl gellan content of 0.0029 g whereas the rate constant was insensitive to low-acyl gellan content at pH 4.4. Addition of guar did not seem to affect the melting temperature or the melting rate constant.     

Effect of food matrix and heat treatment on the rheological properties of salmon-based baby food

Shelf stable baby foods from Alaskan salmon were developed from red and pink salmon with and without bones. The effect of salmon type, presence of bones and thermal treatment (121 °C for 55 min) on the dynamic (viscoelastic) and flow models were evaluated. Rheological behaviors of all samples were also tested over a temperature range of 25–55 °C. All samples had a higher viscoelastic behavior with consistently higher storage modulus (G′) than loss modulus (G″) over the entire frequency range used (0.5–100 rads/s at 25 °C). Thermal treatment had a significant effect (p < 0.0001) on viscoelastic behavior of baby foods when the exponential model (G′ or G″ = A(ω)^b) was used. A values were higher for the processed food for G′ and G″, and b values. The Casson model was found to be the best for the shear rate – shear stress for all types of tested samples. Retorted samples exhibited lower yield stress than their unretorted counterparts. Retorted samples were susceptible to temperature change more than unretorted samples as shown by energy of activation values (E_a) when the effect of temperature (25–55 °C) was studied with an Arrhenius type model. Red salmon without bone had higher E_a values among all samples and with pink salmon with bone recording a lowest among all of them.     

Physicochemical properties of gelatin gels from walleye pollock (Theragra chalcogramma) skin cross-linked by gallic acid and rutin

Gelatin gels were cross-linked by gallic acid and rutin. The gel strength, viscoelastic properties, thermal stability, swelling property, ultrastructure, X-ray diffraction patterns and FTIR spectra were determined to evaluate the physicochemical properties of the modified gels. The gel strength increased with increasing gallic acid concentration up to 20 mg/g dry gelatin, and then decreased at further elevated gallic acid concentration, while it continuously increased with increasing levels of rutin. Either cross-linking agent could enhance the elastic modulus (G′) and the viscous modulus (G″) of hydrogels, but the gelling and melting points didn’t show a notable improvement. Rutin boosted the thermal stability of xerogels, but decreased the equilibrium swelling ratio significantly, while as for gallic acid, there were no obvious effects on the thermal stability and equilibrium swelling ratio of xerogels. Scanning electron microscopy (SEM) was applied to observe the ultrastructure changes of the modified xerogels suggesting that gelatin xerogel at rutin concentration of 8 mg/g dry gelatin showed the highest cross-linking density. X-ray diffraction revealed that both gallic acid and rutin could enter the spacing of polypeptide chains of gelatin to reinforce the intermolecular interaction. And FTIR spectra verified that gallic acid and rutin molecules mainly interacted with skeletal C–N–C group and carboxyl group of gelatin molecules in the formation of gels. The results suggested that rutin was a better cross-linking agent for gelatin, and gels treated with rutin could be found with different physicochemical properties.     

On solid-like rheological behaviors of globular protein solutions

Dynamic viscoelastic and steady flow properties of β-lactoglobulin, bovine serum albumin, ovalbumin, and α-lactalbumin aqueous solutions were investigated at 20°C. When a sinusoidal strain in the linear viscoelastic region was applied, the solutions of the globular proteins except for α-lactalbumin showed typical solid-like rheological behavior: the storage modulus G′ was always larger than the loss modulus G″ in the entire frequency range examined (0.1–100 rad/s). Under a steady shear flow, strong shear thinning behavior was observed with increasing shear rate from 0.001 to 800 s⁻¹, for the globular proteins except for α-lactalbumin. The values of the steady shear viscosity η were lower than those of the dynamic shear viscosity η* at a comparable time scale of observation, violating the Cox–Merz rule, and thus suggesting that a solid-like structure in a globular protein solution was susceptible to a steady shear strain. During isothermal gelation of the protein colloids at 70°C, no crossover between G′ and G″ was observed so that the gelation point was judged by an abrupt increase in the modulus or a sudden decrease in tanδ.     

Influence of complexing carboxymethylcellulose on the thermostability and gelation of α-lactalbumin and β-lactoglobulin

Thermostability and gelation of the main proteins of whey, α-lactalbumin (α-lac) and β-lactoglobulin (β-lg) recovered by selective complexation with carboxymethylcellulose (CMC) was studied to evaluate its functionality in food systems. Their behavior was compared to the non-complexed proteins. Both complexes showed a maximum stability at pH 4, that is close to the pH of obtention of β-lg/CMC coacervate (pH 4) and α-lac/CMC coacervate (pH 3.2). Protein complexation increased the thermostability of β-lg by approximately 6–8 °C and that of α-lac by approximately 26 °C due to immobilization of protein molecules in a complex, mainly by electrostatic interactions and because of different amounts of bound polysaccharide. The denaturation enthalpy of complexed proteins markedly decreased as compared to free proteins. Storage modulus (G′) and loss modulus (G″) were recorded to reflect the structure development during heating β-lg/CMC and α-lac/CMC complexes at different pH values. β-lg/CMC complex at 20 wt% was a viscoelastic liquid at pH values within 2 and 8 but upon heating turned to a particulate viscoelastic gel. However, α-lac/CMC complex formed before heating opaque, large visible white particulate aggregates that sticked together to give a solid viscoelastic structure that was not further modified by thermal processing.     

Shear-induced structuring of particulate whey protein gels

The effects of steady shear on particulate whey protein isolate (WPI) gels, at pH 5.4, have been investigated by light microscopy (LM) and dynamic oscillatory measurements. The steady shear was performed on suspensions at constant rates between 0.5 and 126/s. The gel point under static conditions (T_g) was around 78 °C and the shearing was performed during heating from 20 to 76 or to 82 °C. The gel point was postponed by the shear up to 82 °C. Steady shear up to 76 °C, at rates less than 6/s, resulted in a weaker storage modulus (G′), less frequency dependence and a higher stress at fracture compared to the unsheared gel. Steady shear up to 82 °C, at rates below 6/s, resulted in the formation of two different types of network structure. One structure was similar in appearance to the unsheared network, showing pores in the range of 50 μm. The other structure was dense, composed of smaller particles than the unsheared network and with pores in the range of 10 μm. The gels composed of two structures showed a lower G′ and stress at fracture compared to the unsheared gel. A shear rate above 24/s up to 76 °C resulted in irregular networks, which were composed of two different types of structures. One was loose and open, similar in appearance to the unsheared network structure. The other structure was dense and compact, and was present as individual aggregates. These gels also showed a weaker G′ than the unsheared gel. A shearing up to 82 °C at rates above 24/s resulted in a coarse, inhomogeneous network structure. The gels showed a weak G′, indicating aggregate break-up during the steady shear.     

Thermomechanical properties of biodegradable films based on blends of gelatin and poly(vinyl alcohol)

The aim of this work was to study the effect of the poly(vinyl alcohol) (PVA) concentration on the thermal and viscoelastic properties of films based on blends of gelatin and PVA using differential scanning calorimetry (DSC) and dynamic-mechanical analysis (DMA). One glass transition was observed between 43 and 49 °C on the DSC curves obtained in the first scanning of the blended films, followed by fusion of the crystalline portion between 116 and 134 °C. However, the DMA results showed that only the films with 10% PVA had a single peak in the tan δ spectrum. However, when the PVA concentration was increased the dynamic mechanical spectra showed two peaks on the tan δ curves, indicating two T_gs. Despite this phase separation behavior the Gordon and Taylor model was successfully applied to correlate T_g as a function of film composition, thus determining k=7.47. In the DMA frequency tests, the DMA spectra showed that the storage modulus values decreased with increasing temperature. The master curves for the PVA–gelatin films were obtained applying the TTS principle (T_r=100 °C). The WLF model was thus applied allowing for the determination of the constants C₁ and C₂. The values of these constants increased with increasing PVA concentrations in the blend: C₁=49–66 and C₂=463–480. These values were used to calculate the fractional free volume of the films at the T_g and the thermal expansion coefficient of the films above the T_g.     

Gelation mechanism and network structure of mixed solution of low- and high-acyl gellan studied by dynamic viscoelasticity, CD and NMR measurements

The gelation mechanism and the change of the network structure during cooling of the mixed solution of high-acyl (HA) and low-acyl (LA) gellan (containing 0.5% HA gellan and 0.5% LA gellan; hereafter called “mixed solution”) were elucidated on the basis of the results of dynamic viscoelasticity, circular dichroism (CD), and NMR measurements, which provide information about the network formation, the structural change due to random coil-double helix (C–H) transition, and the chain mobility of gellan, respectively. It was demonstrated that HA gellan chains in the mixed solution underwent C–H transition individually to form a network structure at the transition temperature for 1% HA gellan solution (75 °C), where storage modulus G′ and loss modulus G″ were steeply increased and the chain mobility of the HA gellan was restricted. The structural change of the HA gellan chains proceeded gradually with further cooling. At 25 °C, which is the C–H transition temperature for 1% LA gellan solution, LA gellan chains in the mixed solution formed a double helix, where G′ and G″ were slightly increased and the chain mobility of LA gellan was restricted. The results suggest that the double helix formation involves only the same kind of gellan chains even in the mixed solution, and that LA gellan chains decrease the mobility and promote the double helix formation of HA gellan chains, and vice versa.     

Effects of nisin concentration on properties of gelatin film-forming solutions and their films

The addition of nisin into a gelatin matrix can change properties of the film. The aim of this work was to develop gelatin-based films containing different nisin concentrations in order to study their influence on the film's antimicrobial and physical properties and their rheological properties as a film-forming solution (FFS). The FFS was characterised by rheological assays, and the gelatin-based active films were characterised and assessed by the effects of nisin concentrations on their various properties, including antimicrobial activity. Nisin's concentration affected not only its viscoelastic properties of FFS but also its film solubility in water, film surface roughness and light barrier. The addition of nisin also slightly modified the water contact angle and the mechanical properties of the gelatin films. Finally, the films demonstrated activity against Staphylococcus aureus and Listeria monocytogenes at concentrations above 56 mg of nisin g⁻¹ of gelatin.     

Associative and segregative interactions between gelatin and low-methoxy pectin: Part 2—co-gelation in the presence of Ca

The effect of segregative interactions with gelatin (type B; pI=4.9; 0–10 wt%) on the networks formed by low-methoxy pectin on cooling in the presence of stoichiometric Ca²⁺ at pH 3.9 has been investigated by rheological measurements under low-amplitude oscillatory shear. Samples were prepared and loaded at 85 °C, cooled (1 °C/min) to 5 °C, held for 100 min, and re-heated (1 °C/min) to 85 °C, with measurement of storage and loss moduli (G′ and G″) at 10 rad s⁻¹ and 2% strain. The final values of G′ at 5 °C for mixtures prepared at the same pH without Ca²⁺ were virtually identical to those observed for the same concentrations (0.5–10.0 wt%) of gelatin alone, consistent with the conclusion from the preceding paper that electrostatic (associative) interactions between the two polymers become significant only at pH values below 3.9. Increases in moduli on cooling in the presence of Ca²⁺ occurred in two discrete steps, the first coincident with gelation of calcium pectinate alone and the second with gelation of gelatin. Both processes were fully reversible on heating, but displaced to higher temperature (by 10 °C), as was also observed for the individual components. The magnitude of the changes occurring over the temperature range of the gelatin sol–gel and gel–sol transitions demonstrates that the gelatin component forms a continuous network; survival of gel structure after completion of gelatin melting shows that the calcium pectinate network is also continuous (i.e. that the co-gel is bicontinuous). On progressive incorporation of NaCl (to induce phase separation before, or during, pectin gelation) the second melting process, coincident with loss of calcium pectinate gel structure, was progressively abolished, indicating conversion to a gelatin-continuous network with dispersed particles of calcium pectinate. These qualitative conclusions are supported by quantitative analyses reported in the following paper.     

Rheology and granule size distributions of corn starch dispersions from two genotypes and grown in four regions

Starch was extracted from corn of two genotypes (Clint and P3730) grown during the 1997 season in four regions in New Zealand and Australia. The granule size distributions in unheated and heated (80°C, 2–120 min) 2.6% starch dispersions (STDs) were different. Most of the heated STDs exhibited shear-thinning behavior, but dispersions of a Clint starch exhibited shear-thickening behavior at shear rates >300 s⁻¹. The power law consistency coefficient of the STDs increased, but their flow behavior index decreased with heating time. Values of the consistency coefficient of all the STDs were found to be related to the cube of the mean granule diameter. Frequency versus storage modulus (G′) data of a 5% Clint STD heated at 80°C, 30 min, showed increase in G′ with ω in a convex down manner, while the other STDs showed typical increase in a convex up manner.     

Development of films based on blends of gelatin and poly(vinyl alcohol) cross linked with glutaraldehyde

Both gelatin and poly(vinyl alcohol) (PVA) can be cross linked with glutaraldehyde (GLU). In the case of gelatin, the GLU reacts with each ε-NH2 functional group of adjacent lysine residues, while for PVA, the GLU reacts with two adjacent hydroxyl groups, forming acetal bridges. Thus it can be considered possible to cross link adjacent macromolecules of gelatin and PVA using GLU. In this context, the aims of this work were the development of biodegradable films based on blends of gelatin and poly(vinyl alcohol) cross linked with GLU, and the characterization of some of their main physical and functional properties. All the films were produced from film-forming solutions (FFS) containing 2 g macromolecules (PVA + gelatin)/100 g FFS, 25 g glycerol/100 g macromolecules, and 4 g GLU (25% solution)/100 g FFS. The FFS were prepared with two concentrations of PVA (20 or 50 g PVA/100 g macromolecules) and two reaction temperatures: 90 or 55 °C, applied for 30 min. The films were obtained after drying (30 °C/24 h) and conditioning at 25 °C and 58% of relative humidity for 7 days, and were then characterized. The results for the color parameters, mechanical properties, phase transitions and infrared spectra showed that some chemical modifications occurred, principally for the gelatin. However, in general, all the characteristics of the films were either typical of films based on blends of these macromolecules without cross linking, or slightly higher. A greater improvement in the properties of this material was probably not observed due to the crystallinity of the PVA, which has a melting point above 90 °C. The presence of microcrystals in the polymer chain probably reduced macromolecular mobility, hindering the reaction. Thus more research is necessary to produce biodegradable films with improved properties.     

Mechanical properties of mammalian and fish gelatins based on their weight average molecular weight and molecular weight distribution

Acid porcine skin gelatins (type A), lime bone gelatins (type B) and gelatin from different cold water fish species were compared on the basis of low deformation mechanical properties, Bloom value, weight average molecular weight, molecular weight distribution and isoelectric point. The dynamic storage modulus and Bloom value for all types of gelatin increased with increasing weight average molecular weight. Type A and type B gelatins with similar weight average molecular weight exhibited different dynamic storage modulus (G′) and different Bloom values. This is most probably due to a different molecular weight distribution as well as the presence of different hydrolytic fragments. The present study suggests that it may be possible to improve the mechanical properties by removing low molecular weight molecules from a gelatin sample. The Bloom values for gelatin from haddock, saithe and cod were determined to be 200, 150 and 100 g from a linear correlation between G′ and Bloom.     

Effects of xanthan gum on physicochemical properties and stability of corn oil-in-water emulsions stabilized by polyoxyethylene (20) sorbitan monooleate

The influence of added xanthan gum on rheological and dispersion characteristics and stability of concentrated (50% w/w) corn oil-in-water emulsions, stabilized with 5% (percentage on oil amount) polyoxyethylene (20) sorbitan monooleate (Tween 80), have been investigated. Emulsion with no xanthan indicated coalescence and poor creaming stability. All emulsions, with and without xanthan, showed shear-thinning flow behavior. Addition of xanthan protected emulsions from coalescence during 15 days of storage. Increase in xanthan concentration led to decrease in droplet average radius and creaming index, and increase in elastic properties of emulsions. Decrease in the emulsions flow behavior indexes, which suggested the extent of non-Newtonian behavior of emulsions, was influenced by increase in xanthan concentration. Above 0.04% of xanthan concentration, G′ and G″ values indicated formation of weak gels. Gel structure existence arises from droplet network association, due to depletion flocculation. Standard deviation of emulsions droplet size mean diameter decreased while concentration of added xanthan increased.     

Phase transitions of pigskin gelatin

Edible films are flexible thin materials based on biopolymers. It is therefore necessary to know the physicochemical properties of those macromolecules in order to obtain films with desirable characteristics. Dried gelatin is a partially crystalline polymer that exhibits glass and helix–coil transitions. The knowledge of phase properties is important for the choice of the type and concentration of the plasticizer to be utilized to obtain a flexible and easy-to-handle film. The objective of this work is to determine the phase transitions of pigskin gelatin as a function of moisture content in the hygroscopic domain. Pure gelatin was conditioned over different saturated salt solutions at 25°C to allows samples with various moisture content. After equilibrium was established, the samples and an empty pan, as reference, were heated twice between −100 and 250°C at the rate of 5°C/min, in a DSC (TA 2010) after quench-cooling with liquid nitrogen. Gelatin was placed in a pan with a perforated cover, and maintained at 105°C for 24 h in the DSC cell before thermal analyses, to obtain completely dried samples. The glass transition temperature of these samples was found to be 220.2°C. The DSC traces obtained in the first scan, except those conditioned at 11% relative humidity, showed a glass transition followed by two endothermic peaks due to two sol–gel transitions in the gelatin. The plasticizing effect of moisture on Tg was observed in all the samples conditioned by absorption and in the second scan with the samples conditioned by desorption. This behavior was well represented by the Gordon and Taylor model, with κ=5.26 and R²=0.96. Also, a plasticizing effect of moisture over the sol–gel transitions was observed. The Flory-Huggins model was applied to experimental data with: χ₁=1.94 and R²=0.999, for the first peak Tm, and χ₁=1.90 and R²=0.989, for the second peak.     

Effects of adding fish gelatin on Alaska pollock surimi gels

Fish gelatin is a food additive obtained after hydrolysis of collagen from fish skin. The importance of fish gelatin as a food additive is increasing due to its increased commercial availability. Surimi is washed minced fish meat used as the raw material for seafood analogs like crabmeat substitutes. The most important attributes of surimi are gelling and whiteness. The objective of this work was to determine the effect of using fish gelatin as an additive in surimi to improve the mechanical and functional properties of gels. Surimi gels were prepared by mixing grade A or FA surimi (Alaska pollock) with salt (20 g/kg w/w) and commercial fish gelatin at 0 (control), 5, 7.5, 10, or 15 g/kg (w/w) previously dissolved in water (200 mL/kg surimi). The solubilized paste was incubated at 40 °C for 30 min followed by cooking at 90 °C for 15 min. Changes in mechanical properties (torsion test), a functional property (expressible water content) and color attributes of surimi gels were measured. Grade FA surimi gels containing 7.5–15 g/kg of fish gelatin showed an improved expressible moisture. However, gelatin added at 15 g/kg showed a disruptive effect detrimental to the mechanical properties. Color parameters were modified slightly. Whiteness attribute as affected by increasing the fish gelatin was instrumentally detected but not observed by sensory panelists. Gelatin did not change the overall color attributes and all gels remained in the grayish region. These results indicated that fish gelatin did not have an advantage for using as a functional additive in Alaska pollock surimi grades A or FA. However, it can be used at up to 10 g/kg without a negative effect on the mechanical properties.     

Characterization of gelatin films prepared from under-utilized blue shark (Prionace glauca) skin

Gelatin film from blue shark (Prionace glauca) skin was investigated in order to utilize what is one of the most serious marine wastes in Japan. Film properties from shark skin such as tensile strength (TS), elongation at break (EAB) were evaluated. The TS of gelatin film from shark skin was affected by the protein concentration (1, 2 and 3%) of the film-forming solution (FFS). TS of the film from a 2% protein FFS was the highest. EAB and water vapor permeability (WVP) increased with increasing FFS protein concentration. WVP of shark skin gelatin was evidently low as compared to gelatin films from other fish. An increase in the FFS protein concentration decreased transparency at almost all wavelengths. Furthermore, opacity at 280 nm was characteristically high as compared to films from bony fish skin. The addition of glycerol improved flexibility and enhanced the UV barrier property at 280 nm. However, transparency at the visible range and WVP increased with increasing glycerol content.From the above, it was suggested that shark skin gelatin film technology can be applied to pharmaceutical products or rich-fat food due to its excellent water and UV barrier properties.     

Maturation effects in fish gelatin and HPMC composite gels

This study assessed the effectiveness of using hydroxylpropylmethylcellulose (HPMC) to enhance mechanical strength and thermal stability in fish skin gelatin (FG). The significant increase in absorbance (A₄₀₀) observed after HPMC had been added to FG and then matured indicated successful formation of a composite gel. Increased gel strength and storage modulus (G′) indicated the enhanced gelation ability of the matured composite gel, while increased melting temperature (T_m) and enthalpy (ΔH) indicated its improved thermal stability. Maturation-related rheological property improvements were more noticeable at 4 °C than 10 °C, but no apparent differences in T_m improvement were observed between 4 °C and 10 °C maturation. Nevertheless, the composite gel exhibited reversible cold and thermal gelation properties.