Characteristics and chemical composition of skins gelatin from cobia (Rachycentron canadum)

Gelatin was obtained from cobia (Rachycentron canadum) skins, which is an important commercial species for marine fish aquaculture, and it was compared with gelatin from croaker (Micropogonias furnieri) skins, using the same extraction methodology (alkaline/acid pre-treatments). Cobia skins gelatin showed values of protein yield, gelatin yield, gel strength, melting point, gelling point and viscosity higher than the values found from croaker skins gelatin. The values of turbidity and Hue angle for cobia and croaker gelatins were 403 and 74 NTU, and 84.8° and 87.3°, respectively. Spectra in the infrared region had the major absorption band in the amide region for both gelatins, but it showed some differences in the spectra. The proline and hydroxyproline contents from cobia skins gelatin (205 residues/1000 residues) was higher than from croaker skins gelatin (188 residues/1000 residues). SDS-PAGE of both gelatins showed a similar molecular weight distribution to that of standard collagen type I. Therefore, cobia skins could be used as a potential marine source of gelatin obtainment for application in diversified industrial fields.     

Rheological and functional properties of gelatin from the skin of Bigeye snapper (Priacanthus hamrur) fish: Influence of gelatin on the gel-forming ability of fish mince

The rheological and functional properties of gelatin from the skin of bigeye snapper (Priacanthus hamrur) fish were assessed. The protein content of dried gelatin was 94.6% and moisture content was 4.2%. The amino acid profile of gelatin revealed high proportion of glycine and imino acids. The bloom strength of solidified gelatin was 108 g. The average molecular weight of fish skin gelatin was 282 kDa as determined by gel filtration technique. The emulsion capacity (EC) of gelatin at a concentration of 0.05% (w/v) was 1.91 ml oil/mg protein and with increase in concentration, the EC values decreased. The gelling and melting temperatures of gelatin were 10 and 16.8 °C, respectively as obtained by small deformation measurements. The flow behavior of gelatin solution as a function of concentration and temperature revealed non-Newtonian behavior with pseudoplastic phenomenon. The Casson and Herschel–Bulkley models were suitable to study the flow behavior. The yield stress was maximum at 10 °C with the concentration of 30 mg/ml. Thermal gelation behavior of threadfin bream (Nemipterus japonicus) mince in presence of different concentration of gelatin was assessed. Gelatin at a concentration of 0.5% yielded higher storage modulus (G′) value than control. Frequency sweep of heat set gel with gelatin revealed strong network formation.     

Characteristics of gelatin from the skins of bigeye snapper, Priacanthus tayenus and Priacanthus macracanthus

Gelatins extracted from the skins containing fine scales of two species of bigeye snapper, Priacanthus tayenus (GT) and Priacanthus macracanthus (GM), were characterised. Both gelatins had the protein as the major component with high content of imino acids (proline & hydroxyproline) (186.29–187.42 mg/g). GT and GM contained calcium at levels of 6.53 and 2.92 g/kg, respectively. Both gelatins contained α1 and α2 chains as the predominant components and some degradation peptides. The absorption bands of both gelatins in Fourier transform infrared (FTIR) spectra were mainly situated in the amide band region (amide I and amide II). GT and GM had a relative solubility greater than 90% in the wide pH ranges (1–10). The bloom strength of GM (254.10 g) was higher than that of GT (227.73 g) (P < 0.05), but was slightly lower than that of commercial bovine gelatin (293.22 g) (P < 0.05). Finer gel structure with smaller strands and voids was observed in GM gel, in comparison with that observed in GT counterpart.     

Gel properties of collagens from skins of cod (Gadus morhua) and hake (Merluccius merluccius) and their modification by the coenhancers magnesium sulphate,glycerol and transglutaminase

The gel properties of two different kinds of fish gelatins prepared from cod (Gadus morhua) and hake (Merluccius merluccius) and modified by the coenhancers glycerol, salt and microbial transglutaminase, were examined. Gel strength was substantially increased by the addition of coenhancers although results varied, depending on the species. In gelatin from hake (M. merluccius) skin, the highest values were obtained with 10 mg/g of transglutaminase, whereas magnesium sulphate was more effective at both concentrations (0.1 and 0.5 M) in gelatin from cod (G. morhua) skin. Although, in both gelatins, the addition of any ingredient increased the viscosity modulus (G″), the elastic modulus (G′) was only increased by the addition of glycerol 15% (w/v) and MgSO₄ 0.5 M in hake (M. merluccius) gelatins; in cod (G. morhua) it was increased by all ingredients. The gelling and melting points, very important properties in fish gelatin, showed a notable improvement, the behaviour being different, depending on the species.     

Characteristics of gelatin from the skin of unicorn leatherjacket (Aluterus monoceros) as influenced by acid pretreatment and extraction time

Gelatins from the skin of unicorn leatherjacket (Aluterus monoceros) pretreated with different acids (0.2 M acetic acid or 0.2 M phosphoric acid) and extracted with distilled water at 45 °C for various times (4 and 8 h) were characterized. Yields of 5.23–9.18 or 6.12–11.54% (wet weight basis) were obtained for gelatins extracted from the skin pretreated with 0.2 M acetic acid or 0.2 M phosphoric acid, respectively. Extracted gelatins contained α₁ and α₂ chains as the predominant components and some degradation peptides. The absorption bands of gelatins in FTIR spectra were mainly situated in the amide band region (amide I, amide II and amide ???) and showed the significant loss of molecular order of triple helix. Gelatin samples had a relative solubility greater than 90% in the wide pH ranges (1–10). The gel strength of gelatin from skin pretreated with phosphoric acid (GPA) was higher than that of gelatin from skin pretreated with acetic acid (GAA). Both GPA and GAA had the lower gel strength than that of commercial bovine gelatin (P < 0.05). Net charge of GAA and GPA became zero at pHs of 6.64–7.15 and 6.78–7.26, respectively, as determined by zeta potential titration. Emulsifying and foaming properties of GAA and GPA increased with increasing concentrations (1–3%, w/v). Those properties were governed by pretreatments and extraction time. Thus gelatin can be successfully extracted from unicorn leatherjacket skin using the appropriate acid pretreatment and extraction time.     

Extraction and functional properties of gelatin from the skin of cuttlefish (Sepia officinalis) using smooth hound crude acid protease-aided process

The characteristics and functional properties of gelatin from skin cuttlefish (Sepia officinalis) were investigated and compared to those of halal bovine gelatin (HBG). The gelatin extraction efficiency was improved by an acid-swelling process in the presence of smooth hound crude acid protease extract (SHCAP). The yields of gelatins from cuttlefish skin after 48 h with acid and with crude acid protease (15 units/g alkaline-treated skin) were 2.21% and 7.84%, respectively. The gelatin from skin cuttlefish had high protein (91.35%) but low fat (0.28%) contents. Compared to HBG, the cuttlefish-skin gelatin (CSG) has different amino acids composition than halal bovine gelatin. CSG contained slightly low hydroxyproline and proline (180‰) than HBG (219‰), whereas the content of serine was higher (49‰ versus 29‰). The gel strength of the gelatin gel from CSG (181 g) was lower than that of HBG (259 g) (p < 0.05) possibly due to lower hydroxyproline content. Cuttlefish-skin gelatin exhibited a similar emulsifying activity but greater emulsifying and foam stability than the halal bovine gelatin (p < 0.05). Foam formation ability, foam stability and water-holding capacity of CSG were slightly lower than those of the HBG, but fat-binding capacity was higher in the cuttlefish gelatin.     

Characterization of fish gelatin from surimi processing wastes: Thermal analysis and effect of transglutaminase on gel properties

Fish gelatin extraction from wastes of fish Herring species (Tenualosa ilisha) was carried out by a series of pretreatment with 0.2 M Ca(OH)₂ followed by 0.1 M citric acid and final water extraction at 50 °C for 3 h. The resulting fish gelatin preparation was evaluated for its dynamic viscoelastic properties, gelling and melting temperatures and gel strength. The gelling and melting temperatures of gelatin samples (at 6.67%, w/v) were obtained from differential scanning calorimetry and rheological studies. The melting temperature of extracted fish gelatin (EFG) obtained ranged from 16.2 to 16.7 °C compared to that of commercial fish gelatin gel (CFG), from 23.7 to 25.6 °C and halal bovine gelatin (HBG), from 26.5 to 28.7 °C. On the other hand, gelling temperatures of EFG, CFG and HBG ranged from 5.1 to 5.2 °C, 11.9 to 17.46 °C, and 12.6 to 19.33 °C, respectively. EFG gave gels with a considerably lower G′ values than CFG and HBG. The bloom strength of EFG gels at 6.67% (w/v) was 69.03 g which was much lower than HBG (336.2 g) and CFG (435.9 g). Enzyme transglutaminase was added in the amounts of 0.5, 1.0, 3.0 and 5.0 mg/g gelatin to modify the gel properties of the extracted fish gelatin. The modified EFG gels obtained had higher gel strengths of 101.1 g and 90.56 g with added transglutaminase of 1.0 and 3.0 mg/g, respectively. However with addition of 5.0 mg/g enzyme the gel strength increased only up to 75.06 g. SDS-PAGE of extracted gelatin gel showed protein band intensities for α1-chains and 53 kDa but in gels added with higher concentration of transglutaminase, these protein band intensities seemed to disappear.     

Characterizations of fish gelatin films added with gellan and κ-carrageenan

Fish gelatin is known to be inferior to mammalian gelatins. Gellan and κ-carrageenan were added to improve properties of the fish gelatin films. Initially, polysaccharides were added to make fish gelatin gels, and tested for the melting point. Mechanical, barrier, color and microstructure properties, as well as Fourier transform infrared (FTIR) and thermal analysis (DSC) of the modified fish gelatin films were evaluated. The addition of gellan and κ-carrageenan increased the melting point of fish gelatin gels, gellan being more effective. Polysaccharides modified fish gelatin films by increasing tensile strength and barrier against water vapor, but made films slightly darker. Scanning electron microscopy (SEM) microstructure analysis revealed that gellan eliminated cracks present in the film matrix resulting in a more uniform structure. FTIR and DSC analyses showed that both polysaccharides effectively interacted with fish gelatin, and moreover, gellan being more effective. Overall, addition of gellan up to 2 g/100 g of gelatin performed better in enhancing fish gelatin films properties.     

Characteristics of the gelatin extracted from Channel Catfish (Ictalurus Punctatus) head bones

Three gelatins were prepared from channel catfish head bones by hot water after the head was pretreated with alkali protease, quickly desalted by 0.4 mol/L HCl and soaked in 9 g/L Ca(OH)₂. The extraction conditions of gelatins were 5 °C, pH 4.0, 4 h, 82 °C, pH 2.5, 2 h and 90 °C, pH 3.0, 3 h, respectively. The studies showed there were many differences between these gelatins. The first head bone gelatin contained high content of imino residues and more high molecular weight proportions of β and γ components. Gel strengths of the second and third gelatins were 209 ± 7 g and 117 ± 5 g, lower than that of the first head bone gelatin (282 ± 11 g). Furthermore, the first head bone gelatin achieved the highest gelling and melting points. The first head bone gelatin showed strong ability of clarification when it was used to clarify apple juice. At the same time, the nutritional components of apple juice changed a little except Vitamin C.     

Acid-induced gelation of natural actomyosin from Atlantic cod (Gadus morhua) and burbot (Lota lota)

The acid-induced gelation of natural actomyosin (NAM) from burbot (Lota lota) and Atlantic cod (Gardus morhua) added with d-gluconic acid-δ-lactone (GDL) during incubation at room temperature (22–23 °C) for 48 h was investigated. During acidification, pH values of both NAMs reached 4.6 within 48 h. Both NAMs underwent aggregation during acidification as evidenced by increases in turbidity and particle size, especially after 6 h of incubation. The decreases in Ca²⁺-ATPase activity and salt solubility of both NAMs were observed during incubation. Decreases in total sulphydryl content with the concomitant increases in disulphide bond content of NAM from both species were also noticeable. Additionally, surface hydrophobicity of NAM increased, suggesting the conformational changes in NAM induced by acidification. The storage modulus (G′) values increased with increasing incubation time and G′ development was greater in Atlantic cod NAM, compared with burbot NAM. Differential scanning calorimetry (DSC) revealed that T_max and enthalpy of myosin peak shifted to the lower values and endothermic peak of actin completely disappeared. In general, gel development was more pronounced in Atlantic cod NAM, compared with the burbot counterpart. As visualised by transmission electron microscopy, network strands of aggregates from Atlantic cod were finer and more uniform than those of the burbot counterpart. Acid-induced gelation of NAM from both fish species therefore involved both denaturation and aggregation processes. However, gelation varied with fish species and had an impact on the resulting gels.     

Comparative study on acid-induced gelation of myosin from Atlantic cod (Gardus morhua) and burbot (Lota lota)

Physicochemical and rheological properties of myosin from Atlantic cod and burbot during acid-induced gelation at room temperature (22–23 °C) by d-gluconic acid-δ-lactone (GDL) were monitored. Turbidity and particle size of both myosins increased and salt soluble content decreased when pH decreased, suggesting the formation of protein aggregates caused by acidification. The formation of disulphide bonds in myosin gelation was induced by acid. Ca²⁺-ATPase activity of myosin decreased (p < 0.05), while surface hydrophobicity increased during acidification (p < 0.05). Furthermore, the decreases in maximum transition temperature (T_max) and the denaturation enthalpies (ΔH) were found in both myosins. During acidification, the increases in storage modulus (G′) and loss modulus (G″) of myosin were observed (p < 0.05), revealing the formation of elastic gel matrix. Thus, gelation of myosin from Atlantic cod and burbot could take place under acidic pH via denaturation and aggregation. However, myosin from Atlantic cod was generally more favourable to gelation than was burbot myosin.     

Structural and mechanical properties of fish gelatin as a function of extraction conditions

The effect of 18 different extraction conditions on yield, weight average molecular weight, dynamic storage modulus, gelling and melting temperature, and helix recovery was studied. Gelatins were extracted from saithe (Pollachius virens) skins with an average yield of 8.9 ± 0.8% (average ± S.D.; n = 54), on a wet weight basis. High weight average molecular weight gelatins extracted at room temperature exhibit higher resulting dynamic storage modulus, higher gelling and melting temperatures and more helix formation compared to highly hydrolyzed gelatins extracted under harsher conditions. The storage modulus was increased 5 times compared to commercial cold water fish gelatin. The highest gelling and melting temperatures observed for 5% (w/v) fish gelatin were 8 °C and 16 °C, respectively. The present study suggests that the dynamic storage modulus, gelling and melting temperatures and helix content are related and increase with increasing weight average molecular weight up to about 250 kg/mol. The dynamic storage modulus correlates with the helix concentration according to the previously published correlation between dynamic storage modulus and helix concentration, which has been defined as the master curve for gelatin.     

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.     

Effects of partial hydrolysis and plasticizer content on the properties of film from cuttlefish (Sepia pharaonis) skin gelatin

Properties of film from cuttlefish (Sepia pharaonis) ventral skin gelatin with different degree of hydrolysis (DH: 0.40, 0.80 and 1.20%) added with glycerol as plasticizer at various levels (10, 15 and 20%, based on protein) were investigated. Films prepared from gelatin with all DH had the lower tensile strength (TS) and elongation at break (EAB) but higher water vapor permeability (WVP), compared with the control film (without hydrolysis) (p < 0.05). At the same glycerol content, both TS and EAB decreased, while WVP increased (p < 0.05) with increasing %DH. At the same DH, TS generally decreased as glycerol content increased (p < 0.05), however glycerol content had no effect on EAB when gelatins with 0.80 and 1.20% DH were used (p > 0.05). DH and glycerol content had no marked impact on color and the difference in color (ΔE^∗) of resulting films. Electrophoretic study revealed that degradation of gelatin and their corresponding films was more pronounced with increased %DH, resulting in the lower mechanical properties of films. Based on FTIR spectra, with the increasing %DH as well as glycerol content, higher amplitudes for amide-A and amide-B peaks were observed, compared with film from gelatin without hydrolysis (control film) due to the increased –NH₂ group caused by hydrolysis and the lower interaction of –NH₂ group in the presence of higher glycerol. Thermo-gravimetric analysis indicated that film prepared from gelatin with 1.20% DH exhibited the higher heat susceptibility and weight loss in the temperature range of 50–600 °C, compared with control film. Thus, both chain length of gelatin and glycerol content directly affected the properties of cuttlefish skin gelatin films.     

Rheological properties of channel catfish (Ictalurus punctaus) gelatine from fish skins preserved by different methods

Gelatins were extracted from channel catfish skins preserved by different methods using 50 mmol/l acetic acid. Molecular weight distribution, gel strength and viscoelastic properties of gelatin samples were studied. Compared to gelatins from fresh and frozen skins, gelatin from dried channel catfish skin exhibited higher gel strength. This can be explained by the large α-chains content of gelatin from the dried skins. The gelling point and melting point of dried channel catfish skin gelatin solution were similar to those of fresh skin gelatin solution, but distinctly different from those of frozen skin gelatin. After maturation at low temperature, melting points of gelatins increased. But the melting point of frozen skin gelatin was still the highest among the three gelatin samples studied.     

Chemical compositions and characterisation of skin gelatin from farmed giant catfish (Pangasianodon gigas)

Gelatin was extracted from the skin of farmed giant catfish (Pangasianodon gigas) with a yield of 20.1 g/100 g skin sample on the basis of wet weight. The chemical composition and properties of gelatin were characterised. The gelatin had high protein (89.1 g/100 g) but low fat (0.75 g/100 g) content and contained a high number of imino acids (proline and hydroxyproline) (211 residues per 1000 residues). Giant catfish skin gelatin had a slightly different amino acid composition than calf skin gelatin. The bloom strength of the gelatin gel from giant catfish skin gelatin (153 g) was greater than that of calf skin gelatin (135 g) (P < 0.05). Viscosity, foam capacity and foam stability of gelatin from giant catfish skins were in general greater than those of the gelatin from calf skin tested. SDS-PAGE of giant catfish skin gelatin showed a high band intensity for the major protein components, especially, α-, β- and γ-components and was similar to that of standard calf skin collagen type I.     

Indigenous proteases in the skin of unicorn leatherjacket (Alutherus monoceros) and their influence on characteristic and functional properties of gelatin

Indigenous proteases in the skin of unicorn leatherjacket (Alutherus monoceros) were characterised using autolytic study. Maximised autolysis was found at pH 7 and 50 °C. Autolysis was markedly inhibited by 0.04 mM soybean trypsin inhibitor (SBTI), suggesting that heat activated serine protease was predominant in the skin. The impact of indigenous proteases on the properties of gelatin extracted from unicorn leatherjacket skin was investigated. Gelatin was extracted from unicorn leatherjacket skin using distilled water at 50 °C for 12 h in the presence and absence of 0.04 mM SBTI. In the presence of SBTI, the degradation was markedly inhibited, but a lower gelatin extraction yield was obtained (P < 0.05). Extracted gelatins contained α₁ and α₂ chains as the predominant components with some degradation peptides. FTIR spectra indicated a greater loss of molecular order of the triple helix and a higher degradation was found in gelatin extracted in the absence of 0.04 mM SBTI. The net charge of gelatin samples extracted with and without 0.04 mM SBTI became zero at pHs of 8.45 and 7.31, respectively, as determined by ζ-potential titration. Higher gel strength (320.68 ± 3.02 g) was obtained in gelatin extracted with SBTI, compared with that of gelatin extracted without SBTI (288.63 ± 1.44 g). High emulsifying activity index but lower emulsifying stability index was observed in the former. Therefore, heat-activated serine protease was involved in the degradation of gelatin molecules, thereby affecting the yield, proteinaceous components and properties of gelatin from unicorn leatherjacket skin.     

Properties of a protein-based film from round scad (Decapterus maruadsi) as affected by muscle types and washing

The effects of muscle types and washing on the properties of a protein-based film from round scad (Decapterus maruadsi) mince were investigated. Washing resulted in an increase in the protein content with a coincidental decrease in the fat content of mince, especially from whole muscle and dark muscle. Among all types of muscle (ordinary, dark and whole muscle), the ordinary muscle rendered the film with the highest tensile strength (TS) (p < 0.05). TS of films from washed mince was greater than that of films prepared from unwashed mince for the same type of muscle used (p < 0.05). Nevertheless, the water vapour permeability (WVP) of films from unwashed mince was higher than that of films prepared from washed mince (p < 0.05). Films from washed mince had higher solubility but lower protein solubility than those from unwashed mince (p < 0.05). Regardless of washing, films from ordinary muscle showed the highest L^∗-value (p < 0.05). However, films prepared from dark muscle were more yellowish than those prepared from other muscles, as evidenced by the greater b^∗-value. Films from round scad mince and washed mince had excellent barrier properties to UV light at the wavelength of 200–280 nm. Generally, films from round scad mince had a lower preventive effect on visible light transmission than had those from unwashed mince. Among films from all muscles, those prepared from dark muscle exhibited the highest barrier to visible light transmission (p < 0.05). Therefore, the properties of films from round scad meat were governed by muscle type as well as by washing.     

Compositions,functional properties and antioxidative activity of protein hydrolysates prepared from round scad (Decapterus maruadsi)

Composition, functional properties and antioxidative activity of a protein hydrolysate prepared from defatted round scad (Decapterus maruadsi) mince, using Flavourzyme, with a degree of hydrolysis (DH) of 60%, were determined. The protein hydrolysate had a high protein content (48.0%) and a high ash content (24.56%). It was brownish yellow in colour (L^∗ = 58.00, a^∗ = 8.38, b^∗ = 28.32). The protein hydrolysate contained a high amount of essential amino acids (48.04%) and had arginine and lysine as the dominant amino acids. Na⁺ was the predominant mineral in the hydrolysate. The protein hydrolysate had an excellent solubility (99%) and possessed interfacial properties, which were governed by their concentrations. The emulsifying activity index of the protein hydrolysate decreased with increasing concentration (p < 0.05). Conversely, the foaming abilities increased as the hydrolysate concentrations increased (p < 0.05). During storage at 25 °C and 4 °C for 6 weeks, the antioxidative activities and the solubility of round scad protein hydrolysate slightly decreased (p < 0.05). Yellowness (b^∗-value) of the protein hydrolysate became more intense as the storage time increased but the rate of increase was more pronounced at 25 °C than at 4 °C.     

Rheological characteristics of tamarind (Tamarindus indica L.) juice concentrates

The steady-shear and small-amplitude oscillatory rheological properties of tamarind (Tamarindus indica L.) juice concentrate (TJC) were studied in the temperature range of 10-90 °C using a controlled-stress rheometer. Under steady-shear deformation tests, shear stress-shear rate data were adequately fitted to the Herschel-Bulkley and Casson model at lower (10-30 °C) and higher (50−90 °C) temperature range, respectively. The Carreau model was applied to describe the shear-thinning behaviour of the concentrate, and the model parameters estimated empirically showed temperature dependence. Oscillatory shear data of TJC revealed predominating viscous behaviour (G″>G′) at lower frequency range while the elastic modulus predominating over the viscous one (G′>G″) at higher frequency range. The Cox-Merz rule that relates steady shear and dynamic material functions was tested and not followed by most of the temperatures. The specific heat of TJC increased with temperature and the glass transition temperature of the product was found to be −70.74 °C.