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.     

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.     

Characteristics of Gelatin from Giant Grouper (Epinephelus Lanceolatus) Skin

Gelatin extraction from the skin of giant grouper (Epinephelus lanceolatus) was conducted by acid process with a yield of 20.27 g/100 g wet skin sample. The characteristics of extracted gelatin from giant grouper was investigated in this study, and further compared to that from commercial tilapia. Results showed that when compared to commercial tilapia, giant grouper had lower levels of bloom strength and foam formation ability, but greater values of viscosity, foam stability, and lightness (L*) on gelatin skin. Sodium dodecyl sulphate-polyacrylamide gel electrophoresis analysis revealed three high-bands intensities of major protein components of giant grouper skin gelatin, representing α1-chain, α2-chain, and β-components, and was similar to that of standard calf skin collagen type I. Compared to giant grouper, commercial tilapia contained extra proteins with molecular weight less than 70 kDa on the sodium dodecyl sulphate-polyacrylamide gel electrophoresis of both skin gelatins.     

Extraction and properties of gelatin from channel catfish (Ietalurus punetaus) skin

Response surface method was used to determine the optimum operating conditions for extracting the gelatin from channel catfish skin. The optimal conditions for maximum gel strength are 68.8 h for the time of treatment with calcium hydroxide solution, 43.2 °C for the extraction temperature, 5.73 h for the extraction time with hot water. The gelatin from channel catfish skin showed a high gel strength, 276±5 g. Compare to porcine skin gelatin, the gelatin from channel catfish skin has different amino acids composition and a lower thermo-stability.     

Chemical compositions and characteristics of farm raised giant catfish (Pangasianodon gigas) muscle

Proximate composition, chemical and physical properties of dorsal, ventral and lateral line cuts of farm raised giant catfish were determined. Protein, fat and ash content of the different cuts averaged 16.88, 4.45 and 1.24 g/100 g, respectively. Dorsal contains higher protein concentrations (19 g/100 g) than other two parts (p < 0.05). Ventral showed the highest hydroxyproline content (0.83 mg/g). Differences in lipid composition and fatty acid profiles were found among different cuts with highest phospholipids in the dorsal and highest triglyceride in both ventral and lateral line (p < 0.05). All the meat cuts contained high saturated fatty acid, followed by mono- and polyunsaturated fatty acid. High muscle hardness and toughness was found in the dorsal than that in the ventral (p > 0.05). The highest content of myoglobin and total pigment in lateral line resulted in the highest redness index (a*/b*) of this part. Three major nitrogenous compositions classified based on solubility in giant catfish muscle were myofibrillar, sarcoplasmic and alkaline soluble proteins.     

Isolation and characterisation of collagens from the skin of largefin longbarbel catfish (Mystus macropterus)

Acid-soluble collagen (ASC) and pepsin-soluble collagen (PSC) were extracted from the skin of largefin longbarbel catfish (Mystus macropterus) with yields of 16.8% and 28.0%, respectively, on the basis of dry weight. Both ASC and PSC contained α1 and α2 chains and the amino acid composition of collagen was close to that of calf skin type ? collagen. The intrinsic viscosities of ASC and PSC were 14.9 dl/g and 14.5 dl/g, respectively. Similar ultraviolet and FTIR spectra of ASC and PSC were observed. However, peptide maps of ASC and PSC, hydrolysed by trypsin, revealed some differences in primary structures between the two fractions. Denaturation temperatures of ASC and PSC were 32.1 °C and 31.6 °C, respectively. The higher T_m showed that it is possible to use largefin longbarbel catfish skin collagen as an alternative source of vertebrate collagens for industrial purposes.     

Preparation and functional characterisation of fish skin gelatin and comparison with commercial gelatin

Gelatin was extracted from the skin of farmed giant catfish (GC) and tilapia (TP) at a yield of 19.50% and 23.34% (wet wt). It was high in protein (84–88%) but low in fat (0.09–1.24%) and ash content (0.15–0.17%). The GC exhibited lower emulsifying activity (24–35%), but greater foam ability (98–110%), water holding capacity (477–844%) and fat binding capacity (2541–3314%) than commercial beef skin gelatin (BF) (P < 0.05). GC and TP showed comparable functional properties to BF. SDS‐PAGE patterns of TP gelatin showed high band intensity for the α‐ and β‐components, while the lowest band intensity of the major component was found in the BF. From the study, it can be concluded that the farmed freshwater fish skin GC and TP is a prospective source for producing a significant gelatin yield with desirable functionalities. Because of these, fish skin gelatin could be more effectively and widely used in food industries as a good food ingredient.     

Isolation and characterisation of collagen extracted from the skin of striped catfish (Pangasianodon hypophthalmus)

Acid soluble collagen (ASC) and pepsin soluble collagen (PSC) from the skin of striped catfish (Pangasianodon hypophthalmus) were isolated and characterised. The yields of ASC and PSC were 5.1% and 7.7%, based on the wet weight of skin, respectively, with the accumulated yield of 12.8%. Both ASC and PSC comprising two different α-chains (α1 and α2) were characterised as type I and contained imino acid of 206 and 211 imino acid residues/1000 residues, respectively. Peptide maps of ASC and PSC hydrolysed by either lysyl endopeptidase or V8 protease were slightly different and totally differed from those of type I calf skin collagen, suggesting some differences in amino acid sequences and collagen structure. Fourier transform infrared (FTIR) spectra of both ASC and PSC were almost similar and pepsin hydrolysis had no marked effect on the triple-helical structure of collagen. Both ASC and PSC had the highest solubility at acidic pH. A loss in solubility was observed at a pH greater than 4 or when NaCl concentration was higher than 2% (w/v). T_max of ASC and PSC were 39.3 and 39.6 °C, respectively, and shifted to a lower temperature when rehydrated with 0.05 M acetic acid. Zeta potential studies indicated that ASC and PSC exhibited a net zero charge at pH 4.72 and 5.43, respectively. Thus, ASC and PSC were slightly different in terms of composition and structure, leading to somewhat different 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.     

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.     

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.     

Fatty acid composition of three freshwater fishes under different storage and cooking processes

Fatty acid composition of common carp (Cyprinus carpio), Nile tilapia (Oreochromis niloticus) and tambacu, a hybrid of tambaqui (Colossoma macropomum) and pacu (Piaractus mesopotamicus), was evaluated by gas chromatography. Raw, roasted and steamed fishes with and without skin were analyzed fresh and after 15, 30 and 45 storage days at −20 °C. Total lipid content was 9.3 g/100 g in carp, 0.79 g/100 g in tilapia and 1.3 g/100 g in tambacu with skin, with reductions of about 63%, 39% and 71% in the fishes without skin, respectively. The carp showed a high content of monounsaturated fatty acids (about 50%). In tilapia, palmitic and oleic acids were present in larger proportion, 26.55% and 23.86%, respectively. In tambacu, the fatty acid profile was 37% saturated, 34% monounsaturated and 21% polyunsaturated. Fatty acid composition did not present wide variations due to storage time and preparation, indicating that the storage and cooking methods used did not interfere in fatty acid composition.     

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.     

Marine and farmed fish in the Polish market: Comparison of the nutritional value

The proximate composition and fatty acids profiles of the muscle tissues of nine fish species that are popular on the Polish market were examined. The nine studied fish species were: Baltic fish (cod, herring, salmon), fish farmed in Poland (carp, trout), oceanic fish imported from China (walleye pollock, sole), and farmed fish imported from Vietnam and China (sutchi catfish, tilapia). The lowest lipid content (below 0.1%) was noted in the muscle tissues of Baltic cod and walleye pollock caught in the Pacific. The muscle tissue of walleye pollock also had the lowest protein content (12.2 ± 2.0%). The highest lipid content was noted in the muscle tissues of Baltic salmon (13.1 ± 2.4%). The highest percentage content of eicosapentaenoic (C20:5 n − 3 – EPA) and docosahexaenoic (C22:6 n − 3 – DHA) acids (over 40%) was noted in the fat extracted from the oceanic fish and Baltic cod. However, due to the low fat content, the concentrations of EPA + DHA in these fish species and in imported farmed fish expressed in mg/100 g of muscle tissues are the lowest and range on average from 24.8 ± 5.7 mg/100 g (sutchi catfish) to 207.4 ± 125.4 mg/100 g (sole). This is why the consumption of these fish species has no significant meaning for coronary heart disease prevention. Consumers with symptoms of cardiovascular diseases should include the following fish species, which have high concentrations of EPA + DHA: Baltic salmon (3807.2 ± 666.3 mg/100 g); Polish farmed trout (1804.0 ± 279.2 mg/100 g); and Baltic herring (940.9 ± 306.6 mg/100 g) in their diets. However, the consumption of Baltic salmon must be limited on account of the levels of persistent organic pollutants found in it.     

Soybean seeds and its by-product okara as sources of dietary fibre. Measurement by AOAC and Englyst methods

The composition of soybean seeds and its by-product okara has been studied in this work. Dietary fibre was analysed by Englyst et al. method, by enzymatic–gravimetric methods of AOAC and by the quantification of the monomers obtained from the AOAC residues after acid hydrolysis (AOAC plus hydrolysis). Total dietary fibre by the enzymatic–gravimetric methods of AOAC in okara (55.48 g/100 g dry matter) is more than twice that of soybean seeds (24.37 g/100 g dry matter). The proportion IF/SF is 11 in okara and 6 in soybean seeds. Dietary fibre results from enzymatic–gravimetric AOAC methods are higher in okara and soybean seed samples than those from the Englyst method (okara: 41.14 g/100 g dry matter; soybean seeds: 15.05 g/100 g dry matter), and AOAC plus hydrolysis (okara: 44.91 g/100 g dry matter; soybean seeds: 16.38 g/100 g dry matter). In the case of the insoluble fibre from both samples, AOAC plus hydrolysis gives significantly (p < 0.001) higher values than the Englyst method, whilst for soluble fibre the opposite occurs (p < 0.001). The main monomers in soybean seeds and okara fibre are glucose, galactose, uronic acids, arabinose and xylose. The proportion of each monomer is similar in soybean seeds and okara, so the healthy properties of soybean seeds fibre are also claimed for okara.     

Properties of gelatin films from giant catfish skin and bovine bone: a comparative study

Edible films were prepared from the gelatin of farmed giant catfish skin (GC) (Pangasianodon gigas), bovine bone gelatin (BB) and their combination. The physical, mechanical, thermal and chemical properties of the resulting films were characterized and compared. The molecular weight distributions of the giant catfish skin gelatin-containing samples had high quantities of α-chains, β-components and high molecular weight cross-links. The bovine bone gelatin-containing samples showed low contents of major bands with high degradation band components. The GC films had higher water activity (0.45) and mechanical properties [tensile strength: TS 41 MPa and elongation at break: EAB 34 (%)] but lower thickness (38 μm) and water vapor permeability than those of BB films. The lowest light transmission (200–800 nm) and film transparency (3.34) were found in the GC films. However, the color attribute (L, a and b) of BB films was closer to the low-density polyethylene commercial film (ΔE 1.2). The highest value of film and protein solubility (100%) was found in BB film, while the lowest value (41–56%) was found in GC film. The GC films showed the most compact, smooth and continuous surface without porous structures, which corresponds to the greater properties of films.     

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.     

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.     

Decrease of available lysine in thermally treated gelatin followed by LC–UV: Influence on molar mass and ability to helixes’ formation

Available lysine (AL) content, weight-average molar mass (M_w) and kinetic of α helixes’ formation have been determined in thermally treated gelatin (75 °C) during 2, 6 and 8 days. Quantification of available lysine in gelatin sample by LC–UV has been developed. Thermal treatment during 8 days led to a decrease of AL content from 3.1 g/100 g of gelatin to 2.3 g/100 g of gelatin. In the same time, M_w increased from 6.7 × 10⁵ g mol⁻¹ to more than 2.0 × 10⁶ g mol⁻¹ and α helixes’ formation ability was strongly affected. Thermal treatment led to the reaction of available lysine group with other functions present in its environment. Intermolecular cross-links led to a high molar mass compounds’ formation and limited protein chain unfolding which is an essential step for helixes’ formation.     

New trends in the seafood market. Sutchi catfish (Pangasius hypophthalmus) fillets from Vietnam: Nutritional quality and safety aspects

Sutchi catfish (Pangasius hypophthalmus) produced in the freshwater basins of Vietnam, available on the Italian market as frozen or thawed fillets, were studied for their nutritional quality and safety aspects. Proximate composition, mineral content, fatty acid profile, unsaponifiable components of the lipid fraction and drip loss during thawing at 5 °C were determined on the fillets. Fillets were characterised by high moisture levels (80–85%) and low protein (12.6–15.6%) and lipid (1.1–3.0%) contents. Total lipids were characterised by low cholesterol levels (21–39 mg/100 g), high percentages of saturated fatty acids (41.1–47.8% of total fatty acid) and low percentages of polyunsaturated fatty acids (12.5–18.8% of total fatty acids), which were mainly represented by linoleic acid (44–59% of total polyunsaturated fatty acids). The mineral composition was characterised by a high sodium content (222–594 mg/100 g), probably partially due to the sodium tripolyphosphate (E 451) used to retain moisture. As regards safety aspects, the quality of the samples analysed was good, with low residue levels of mercury, organochlorine pesticides and polychlorinated biphenyls.