Use of lactic acid for extraction of fish skin gelatin

The ability of lactic acid compared to acetic acid for Dover sole (Solea vulgaris) skin swelling and the subsequent gelatin extraction was examined. The resultant gelatins were evaluated in terms of extraction yield, amino acid composition, molecular weight distribution, gel strength, viscoelastic properties, ability to refold into triple helical structures, and aggregation phenomena. Lactic acid (25 mM) proved to be an excellent substitute for acetic acid during the skin swelling process, as the gelatin preparation thus obtained presented quite similar properties to that prepared by using 50 mM acetic acid without the negative organoleptic properties of this acid. However, the application of 50 mM lactic acid gave rise to a highly hydrolysed gelatin, with lower folding ability, gel strength and viscoelastic properties than those obtained using 25 mM lactic acid or 50 mM acetic acid.     

Gelation of gellan – A review

Gellan is an anionic extracellular bacterial polysaccharide discovered in 1978. Acyl groups present in the native polymer are removed by alkaline hydrolysis in normal commercial production, giving the charged tetrasaccharide repeating sequence: → 3)-β-d-Glcp-(1 → 4)-β-d-GlcpA-(1 → 4)-β-d-Glcp-(1 → 4)-α-l-Rhap-(1 →. Deacylated gellan converts on cooling from disordered coils to 3-fold double helices. The coil–helix transition temperature (T_m) is raised by salt in the way expected from polyelectrolyte theory: equivalent molar concentrations of different monovalent cations (Group I and Me₄N⁺) cause the same increase in T_m; there is also no selectivity between different divalent (Group II) cations, but divalent cations cause greater elevation of T_m than monovalent. Cations present as counterions to the charged groups of the polymer have the same effect as those introduced by addition of salt. Increasing polymer concentration raises T_m because of the consequent increase in concentration of the counterions, but the concentration of polymer chains themselves does not affect T_m. Gelation occurs by aggregation of double helices. Aggregation stabilises the helices to temperatures higher than those at which they form on cooling, giving thermal hysteresis between gelation and melting. Melting of aggregated and non-aggregated helices can be seen as separate thermal and rheological processes. Reduction in pH promotes aggregation and gelation by decreasing the negative charge on the polymer and thus decreasing electrostatic repulsion between the helices. Group I cations decrease repulsion by binding to the helices in specific coordination sites around the carboxylate groups of the polymer. Strength of binding increases with increasing ionic size (Li⁺ < Na⁺ < K⁺ < Rb⁺ < Cs⁺); the extent of aggregation and effectiveness in promoting gel formation increase in the same order. Me₄N⁺ cations, which cannot form coordination complexes, act solely by non-specific screening of electrostatic repulsion, and give gels only at very high concentration (above ∼0.6 M). At low concentrations of monovalent cations, ordered gellan behaves like a normal polymer solution; as salt concentration is increased there is then a region where fluid “weak gels” are formed, before the cation concentration becomes sufficient to give true, self-supporting gels. Aggregation and consequent gelation with Group II cations occurs by direct site-binding of the divalent ions between gellan double helices. High concentrations of salt or acid cause excessive aggregation, with consequent reduction in gel strength. Maximum strength with divalent cations comes at about stoichiometric equivalence to the gellan carboxylate groups. Much higher concentrations of monovalent cations are required to attain maximum gel strength. The content of divalent cations in commercial gellan is normally sufficient to give cohesive gels at polymer concentrations down to ∼0.15 wt %. Gellan gels are very brittle, and have excellent flavour release. The networks are dynamic: gellan gels release polymer chains when immersed in water and show substantial recovery from mechanical disruption or expulsion of water by slow compression. High concentrations of sugar (∼70 wt % and above) inhibit aggregation and give sparingly-crosslinked networks which vitrify on cooling. Gellan forms coupled networks with konjac glucomannan and tamarind xyloglucan, phase-separated networks with kappa carrageenan and calcium alginate, interpenetrating networks with agarose and gelling maltodextrin, and complex coacervates with gelatin under acidic conditions. Native gellan carries acetyl and l-glyceryl groups at, respectively, O(6) and O(2) of the 3-linked glucose residue in the tetrasaccharide repeat unit. The presence of these substituents does not change the overall double helix structure, but has profound effects on gelation. l-Glyceryl groups stabilise the double helix by forming additional hydrogen bonds within and between the two strands, giving higher gelation temperatures, but abolish the binding site for metal ions by changing the orientation of the adjacent glucuronate residue and its carboxyl group. The consequent loss of cation-mediated aggregation reduces gel strength and brittleness, and eliminates thermal hysteresis. Aggregation is further inhibited by acetyl groups located on the periphery of the double helix. Gellan with a high content of residual acyl groups is available commercially as “high acyl gellan”. Mixtures of high acyl and deacylated gellan form interpenetrating networks, with no double helices incorporating strands of both types. Gellan has numerous existing and potential practical applications in food, cosmetics, toiletries, pharmaceuticals and microbiology.     

Rheological analysis of emulsion-filled gels based on high acyl gellan gum

Emulsion-filled gels are widely used in cosmetic, food, and pharmaceutical industry. As rheological properties of these systems are strongly dependent on the properties of the gelled polymer network, rheological characteristics of gels containing high and low acyl gellan gum were analyzed. Under the processing conditions low acyl emulsions were unstable, thus in the present work the influence of oil and hydrocolloid concentrations on the viscoelastic behavior of emulsion-filled gels containing high acyl gellan gum was studied. Increasing gellan concentration (from 0.1 g/100 g to 0.5 g/100 g) produced stronger gels, while oil fraction (10 g/100 g–30 g/100 g) slightly affected the elastic behavior of the emulsions reinforcing the structure and the elastic characteristics of the gellan matrix. Sauter diameter (d₃₂) was measured for all emulsions and an average value of 12 μm was obtained. Rheological data (oscillatory and creep–recovery tests) were successfully modeled to interpret the structural characteristics of the gelled emulsions. The broadened Baumgaertel–Schausberger–Winter spectrum was used to represent the linear viscoelastic behavior of the continuous phase and the emulsified system, showing that the rheological behavior of the systems was controlled by the highly structured continuous phase rather than the contribution of filler lipid droplet in the emulsion. Relaxation spectra were validated using creep–recovery experiments. Regardless of hydrocolloid concentration, creep compliance of the gel emulsions decreased compared with their respective gels, showing that the inclusion of oil droplets produced a reinforcement of the structure and the gel strength of the matrix.     

Conformational ordering and gelation of gelatin in mixtures with soluble polysaccharides

Previous studies have shown that conformationally disordered, soluble biopolymers cause large enhancements in self-association of calcium pectinate, thermally denatured whey protein and gelling maltodextrin under conditions where the pre-gel solutions remained as a single phase. The purpose of the present work was to screen for similar enhancements in gel strength and rate of conformational ordering of gelatin on incorporation of soluble, disordered polysaccharides. Type B gelatin was used at a fixed concentration of 5.0 wt%, at a pH well above its isoelectric point of ∼4.5. Mixtures were prepared at 45 °C, where the gelatin is in the disordered coil form. Gel strength was characterised as Young's modulus (E), derived from the initial slope of compression curves for gels formed by holding for 16 h at 5 °C. Rate of conformational ordering of gelatin (triple-helix formation) was monitored by changes in optical rotation during and after rapid quenching from 45 to 5 °C. The polysaccharides studied were carboxymethylcellulose (CMC), hydroxypropylmethylcellulose (HPMC), guar gum, gum arabic, dextran and inulin, all of which were used in compression testing. Combinations of gelatin with HPMC and guar gum became immediately turbid on mixing and could not, therefore, be included in the samples characterised by optical rotation. The other mixtures remained homogeneous (i.e. single-phase) on holding at 45 °C. The results obtained were entirely negative. Incorporation of the soluble polysaccharides caused no significant changes in Young's modulus, and optical rotation values remained within ∼10% of those for gelatin alone. It is suggested that the enthalpic advantage of segregation is sufficient to overcome the small reduction in entropy from association of conformationally immobile subunits in gelation of calcium pectinate, whey protein and maltodextrin, but not sufficient to overcome the much greater loss of entropy from conversion of flexible gelatin coils to rigid triple helices.     

Gelation of soybean proteins induced by sequential high-pressure and thermal treatments

The effect of high-pressure treatment on structural and rheological properties of soybean protein dispersions was studied. A sequential high-pressure/thermal treatment was also analyzed. Dissimilar effects on soy protein isolate (SPI) and the enriched soybean protein fractions: β-conglycinin (βCEF) and glycinin (GEF) were observed. High pressure (600 MPa) promoted βCEF gelation, but did not modify the rheological properties of GEF in spite of its complete denaturation. Pressure treatment also induced the establishment of hydrophobic interactions and disulfide bonds that allowed the formation of soluble high molecular mass aggregates from the different polypeptides of both β-conglycinin and glycinin. Protein strands formation was detected in matrix microstructure of HP-treated SPI and βCEF dispersions in accordance with their rheological behavior of weak gels. In the case of GEF modifications induced by HP in the microstructure (apparition of large granules) were not accompanied by rheological changes.     

Gelation behaviour of gelatin and alginate mixtures

Mixtures of alginate and gelatin were studied by rheology as a function of different parameters, such as temperature, biopolymer concentrations, calcium concentration and ionic strength. In particular conditions, the formation of a mixed gel of alginate and gelatin is obtained. A slow release of calcium ions leads first to an irreversible alginate gel and cooling results in a reversible gelatin gel. Depending on experimental conditions, non-linear behaviours upon gelation of alginate occur and a collapse of alginate gel is directly observable by rheology. These trends are favoured between 35 and 45 °C, by a high total biopolymer concentration or a high calcium concentration and ionic strength. Different mechanisms could be responsible for this collapse, such as a competition between alginate gelation and phase separation in the biopolymer mixture or an over-association of alginate chains at high Ca²⁺ concentration, favoured by the presence of gelatin.     

Effects of Pretreatment on Properties of Gelatin from Perch (Lates Niloticus) Skin

Fish gelatins obtained from perch fish skin pretreated with various solutions containing acetic acid, sodium hydroxide (NaOH) and sodium chloride (NaCl) were successfully characterized for their nanostructure pattern using field emission scanning electron microscopy. Each pretreatment transformed collagen to gelatin with fibril, zigzag cracks, straight rods, and cross-linked rods nanostructure patterns. Pretreatment solutions also affect the gel yield, gel strength, amino acid profile, and functional groups in perch gelatin as analyzed by Fourier transform infrared spectroscopy. Samples pretreated with NaCl, NaOH, and acetic acid solution showed the highest gel yield (22.84%) and gel strength (179.84 g). Fourier transform infrared spectra for perch gelatins also revealed weak C–N amide II and III bond stretches as well as weak C=O bond stretch.     

凝胶淀粉的理化特性研究

用凝胶淀粉中试产品进行理化特性分析:包括粘度测定、热糊与冷糊稳定性;不同pH值、糖、盐存在下淀粉粘度曲线与凝胶强度以及冻融稳定性;颗粒形貌、红外光谱和X-射线分析等。结果表明:本品是一种易分散于冷水,加热易糊化成均匀透明胶体液,其热、冷糊稳定性高;在低或高pH值范围内,用糖或不用糖,不用硬化用盐类均能胶凝。凝胶强度强,尤其耐酸性特好;冻融稳定性增强,保水性亦好;凝胶淀粉与天然淀粉颗粒形貌几乎没有差别,表明交联、水解反应只在淀粉颗粒的表面进行。晶体结构也未发生变化。     

斑点叉尾鮰鱼皮明胶的制备

目的以斑点叉尾鮰鱼皮为原料,采用酸碱法制备鱼皮明胶;方法选用NaOH溶液和H2SO4溶液进行明胶的提取,通过单因素试验和正交试验,确定斑点叉尾鮰鱼皮明胶最佳制备工艺;结果NaOH质量分数为0.3%,H2SO4质量分数为0.4%,处理时间均为120 min,提取温度45℃,提取时间6 h,此时,所得明胶的凝胶强度和黏度分别为672.2 g和9.46 mPa·s,明胶提取率为65.21%.     

Diffusion of probe polymer in gellan gum solutions during gelation process studied by gradient NMR

The diffusion coefficients of pullulan added in gellan gum solutions as a probe polymer were measured using pulsed-field-gradient stimulated-spin-echo (PFG-Ste) ¹H NMR in order to investigate the gelation mechanism and gel structure. The echo intensity of gellan was steeply decreased at around the gelling temperature T_gel indicating stiffening of the gellan chains upon aggregation and formation of the network. The diffusion coefficient of pullulan D_pull increased with decreasing temperature below T_gel. This result suggests that the decrease in concentration of solute gellan in the interspaces of the network below T_gel, as evidenced by the decrease in its echo intensity, leads to an overall decrease of hydrodynamic interactions between gellan and pullulan. The characteristic hydrodynamic shielding length ξ was calculated from the relation D_pull/D_pull,0 = exp(−R_h/ξ), where D_pull,0 is D_pull in dilute solution and R_h is the hydrodynamic radius of pullulan. The temperature dependence of ξ, which was investigated for varying concentrations of several cations, was found to follow closely the gelling temperature, and in particular, showing a very similar thermal hysteresis.     

肉品胶凝技术

肉糜制品不仅有效地利用廉价的肉品原料或碎肉以及其它蛋白质资源,而且可以根据不同的消费需要改变(或改善)肉食品的风味、嫩、质地及外观,从而改进现有肉制品种类、开发新产品.本文通过查阅相关文献,对肉糜凝胶的特性进行研究,分析影响肉糜凝胶的因素,指导肉制品加工,同时降低能量消耗,减少各种浪费.     

Chemical composition and characteristics of skin gelatin from grey triggerfish (Balistes capriscus)

Gelatin was extracted from the skin of grey triggerfish (Balistes capriscus) by the acid extraction process with a yield of 5.67 g/100 g skin sample on the basis of wet weight. The chemical composition and functional properties of gelatin were investigated. The gelatin had high protein (89.94 g/100 g) but low fat (0.28 g/100 g) contents. Differences in the amino acid composition between grey triggerfish skin gelatin (GSG) and halal bovine gelatin (HBG) were observed. GSG contained a lower number of imino acids (hydroxyproline and proline) (176 residues per 1000 residues) than HBG (219 residues per 1000 residues), whereas the content of serine was higher (40 versus 29 residues per 1000 residues, respectively). The gel strength of the GSG (168.3 g) was lower than that of HBG (259 g) (p < 0.05) possibly due to lower hydroxyproline content. Grey triggerfish skin gelatin exhibited a slightly lower emulsifying activity and water-holding capacity but greater emulsifying and foam stability, foam formation ability and fat-binding capacity than the halal bovine gelatin (p < 0.05). SDS-PAGE of GSG showed high band intensity for the major protein components, especially, α- and β-components and a similar molecular weight distribution to that of standard calf skin collagen type I.     

The characteristics of gelatin extracted from sturgeon (Acipenser baeri) skin using various pretreatments

The physicochemical characteristics of gelatin obtained by different pretreatments of sturgeon (Acipenser baeri) skin with alkaline and/or acidic solutions have been studied. Visual appearance, pH, gel strength, viscosity and amino acid profile of the gelatins were evaluated. Pretreatment with alkaline solutions of Ca(OH)₂ and/or acetic acid (HAC) provided gelatin with a favourable colour. Pretreatment with alkali removed noncollagenous proteins effectively, whilst acid induced some loss of collagenous proteins. Gel strength and viscosity of gelatin pretreated with HAC or alkali followed by HAC were as high as gelatin extracted in the presence of protease inhibitors. Amino acid composition had no significant effect on the gelatin characteristics. The total acid concentration for the highest gel strength was inversely proportional to ionisation strength, and the preferred pH for extracting gelatin with the optimum gel strength was approximately 5.0. The results showed that any available protons, regardless of the type or concentration of the acid, inhibit protease activity, which significantly affects the gelatin characteristics.     

Characteristics and functional properties of gelatin from zebra blenny (Salaria basilisca) skin

Gelatin was extracted from alkali-pretreated skin of zebra blenny (Salaria basilisca) using commercial pepsin with a yield of 18 g/100 g of skin sample. The polypeptides pattern, gel strength, viscosity, textural parameters and functional properties of the zebra blenny skin gelatin (ZBSG) were investigated. Amino acid analysis revealed that ZBSG contained almost all essential amino acids, with glycine being the most predominant one. ZBSG was identified as a type I gelatin, containing α₁ and α₂-chains as the major constituents. Its gel strength and viscosity were 170.2 g and 5.95 cP, respectively. Fourier transformed infrared spectroscopy (FT-IR) spectra showed helical arrangements in its structure. Its solubility and functional properties were concentration-dependent. While foam expansion (FE) and foam stability (FS) increased with the increase of concentration, emulsifying activity index (EAI) and emulsion stability index (ESI) were noted to decrease. ZBSG also showed strong clarification ability particularly for apple juice, without affecting nutritional value.     

Study on the properties of gelatins from skin of carp (Cyprinus carpio) caught in winter and summer season

The objective of this work was to compare the physiochemical (molecular weight distribution and amino acid composition) and rheological (viscosity property, gel strength and melting point) properties of gelatins from skins of carp caught in winter to those obtained for the summer equivalents. Gelatins from winter and summer fish skins were extracted at 60, 70 and 80 °C. SDS-PAGE patterns for gelatins extracted under the same conditions showed that the degradation of gelatins from winter fish skins were more severe than that of the summer ones. The imino acid contents of the winter and summer gelatins extracted at 60 °C were very similar, showing 190 and 188 residues/1000 residues, respectively. The gelatins from summer fish presented higher melting points and gel strengths, as well as better viscosity properties than the winter equivalents (P < 0.05). The differences in the rheological properties between winter and summer gelatins may be explained by different thermostability of interstitial collagen molecules (from which gelatins were derived) in the two seasons.