Physical properties of gelatin extracted from skin of Thai panga fish (original) (raw)
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Physical properties of gelatin extracted from skin of Thai panga fish (Pangasius bocourti Sauvage)
2013
Gelatin from the skin of Thai panga fish (Pangasius bocourti Sauvage) was pretreated with a solution of 0.8 M sodium chloride and 0.1 M sodium hydroxide and extracted by acetic acid solution pH 4.55 at 55°C for 1 h. Physical properties of the obtained fish gelatin and the commercial bovine bone gelatin were compared. The gel strength (513.75 g), viscosity (3.88 cP), turbidity (73.21%), foaming properties (foam formation ability 1.13 and foam stability 0.71), emulsion stability (34.2 to 44.6%) and adhesiveness (-369.1 g.sec) of the fish skin gelatin were higher, but color (L* 43.62, C* 3.66 and h° 45.28), cohesiveness (0.838) and gel elasticity were lower than those of the bovine bone gelatin. Gelling and melting points of the fish skin gelatin (16.40°C and 26.87°C, respectively) were lower than those of the bovine bone gelatin (18.45°C and 29.90°C, respectively). Results obtained suggest that the gelatin extracted from the skin of Thai panga fish was a potential raw material for producing a gelatin film or use as foaming agent, emulsifying agent or thickener, but not suitable for use as gelling agent.
Characteristics and functional properties of gelatin from seabass skin as influenced by defatting
Gelatins from nondefatted and defatted seabass skins were characterised and evaluated for their functional properties in comparison with commercial fish skin gelatin. All gelatins contained a 1-and a 2-chains as the predominant components and showed a high imino acid content (199–201 residues/1000 residues). All gelatins had a relative solubility greater than 90% in the wide pH ranges (1–10). Foaming properties of all gelatins increased with increasing concentrations (1–3%, w/v). Gelatin from defatted skin had higher foam expansion and stability than that extracted from nondefatted skin. Emulsion containing gela-tin from defatted skin had smaller oil droplet size (d 32 , d 43), compared with that having gelatin from non-defatted skin (P < 0.05). After 10 days of storage at room temperature (28–30 °C), emulsion stabilised by gelatin from defatted skin showed the higher stability as indicated by the lower increases in d 32 and d 43 , and lower flocculation factor and coalescence index. Coincidentally, emulsion stabilised by gelatin from defatted skin had higher zeta potential than that containing gelatin from nondefatted skin. Thus, defatting of seabass skin directly affected characteristics and functional properties of resulting gelatin.
Journal of Food Processing and Preservation, 2010
ABSTRACTGelatin was extracted from the skins of rohu and Common carp, and its physicochemical properties were studied. The yield of gelatin obtained from the skin of rohu and Common carp were 12.93 and 12%, respectively. The corresponding viscosity values were 6.06cP and 5.96cP. Rohu and Common carp skin gelatin had high content of imino acids i.e., 20.49 and 19.16%, respectively. Rohu gelatin had a significantly higher (P < 0.05) melting point than that of Common carp skin gelatin. The setting temperature observed for the gels from rohu and Common carp was 18.52 and 17.96C, respectively. Rohu and Common carp skin gelatins were found to have a mild but easily perceivable odor. The gelatins from the skin of rohu and common carp had a snowy white appearance and were light-textured. Rohu skin gelatin had significantly higher gel strength compared with Common carp skin gelatin. Foam formation ability and form stability of Common carp gelatin was significantly lower (P < 0.05) than that of Rohu gelatin. Rohu skin gelatin had the high fat-binding capacity. In this study, the functional properties observed for gelatins from the skin of rohu and Common carp are similar, if not better than many of the gelatins from other fish sources, and can be used as potential substitutes for the same in many applications.Gelatin was extracted from the skins of rohu and Common carp, and its physicochemical properties were studied. The yield of gelatin obtained from the skin of rohu and Common carp were 12.93 and 12%, respectively. The corresponding viscosity values were 6.06cP and 5.96cP. Rohu and Common carp skin gelatin had high content of imino acids i.e., 20.49 and 19.16%, respectively. Rohu gelatin had a significantly higher (P < 0.05) melting point than that of Common carp skin gelatin. The setting temperature observed for the gels from rohu and Common carp was 18.52 and 17.96C, respectively. Rohu and Common carp skin gelatins were found to have a mild but easily perceivable odor. The gelatins from the skin of rohu and common carp had a snowy white appearance and were light-textured. Rohu skin gelatin had significantly higher gel strength compared with Common carp skin gelatin. Foam formation ability and form stability of Common carp gelatin was significantly lower (P < 0.05) than that of Rohu gelatin. Rohu skin gelatin had the high fat-binding capacity. In this study, the functional properties observed for gelatins from the skin of rohu and Common carp are similar, if not better than many of the gelatins from other fish sources, and can be used as potential substitutes for the same in many applications.PRACTICAL APPLICATIONSAmong the cultured carps, rohu (Labeo rohita) and Common carp (Cyprinus carpio) contribute significantly to the Aquaculture production in India. These species are presently being increasingly used for the preparation of mince and fillet-based value added products, with skin forming a major portion of the fishery waste thus generated. Hence, based on the availability and commercial importance and with the objective of efficient utilization of fish skin waste, these species were chosen for studies on gelatin extraction. It was observed that the physicochemical and functional properties for rohu and Common carp skin gelatins are similar, if not better than many of the gelatins from other fish sources and can be used as potential substitutes for the same in many applications. There is a future scope for developing binary blends of these gelatins with animal gelatins that are completely compatible and commercially useful in many applications.Among the cultured carps, rohu (Labeo rohita) and Common carp (Cyprinus carpio) contribute significantly to the Aquaculture production in India. These species are presently being increasingly used for the preparation of mince and fillet-based value added products, with skin forming a major portion of the fishery waste thus generated. Hence, based on the availability and commercial importance and with the objective of efficient utilization of fish skin waste, these species were chosen for studies on gelatin extraction. It was observed that the physicochemical and functional properties for rohu and Common carp skin gelatins are similar, if not better than many of the gelatins from other fish sources and can be used as potential substitutes for the same in many applications. There is a future scope for developing binary blends of these gelatins with animal gelatins that are completely compatible and commercially useful in many applications.
Research Results on " Characteristics of Gelatin from Fish Bones
2021
The purpose of this review article is to examine the method of making gelatin, the characteristics of gelatin from the results of research that has been carried out in Indonesia and the benefits of fish gelatin. Based on a review of various articles and other literature, it can be concluded that fish bone gelatin can be extracted by the acid method. The production of fishbone gelatin consists of 4 stages, the preparation of raw materials includes removal of non-collagen components from raw materials, conversion of collagen to gelatin, purification of gelatin by filtering and finally drying and powdering. Fishbone gelatin can be applied to both the food and non-food industries.
Food Hydrocolloids, 2009
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 1.91ml oil /mg protein and with increase in concentration, the EC values decreased. The gelling and melting temperatures of gelatin were 10 o and 16.8 o 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 o 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.
2021
Production of gelatin from the aquatic source is gradually replacing the mammalian sources because of some socio-cultural and religious issues. The Pangasius pangasius catfish is a native species and very popular in Bangladesh due to their availability and cheap price. The perspective of this study was to extract the gelatin from the skin and bones of this catfish and compare them with commercial gelatin. Gelatin was extracted by applying the acid-base extraction process and the resultant gelatins were evaluated based on some physical properties. The gelatin yield was found significantly higher from the skin sample (10.85±0.93%) than the bone (5.23±0.39%) of Pangasius. The extracted skin gelatin had higher moisture and fat content than the bone and Commercial gelatin, while the ash content was significantly higher in bone gelatin. Protein content was noted in skin gelatin (81.34±3.45%), bone gelatin (73.44±2.58%), Where commercial gelatin (92.38±3.89%). Skin gelatin exerted significantly higher (p<0.05) viscosity (4.62±0.3 mPa.s) than the extracted bone gelatin (3.11±.24 mPa.s) and lower than the commercial gelatin (5.76±0.34 mPa.s). The melting and setting temperature of this catfish skin and bone gelatin were very near to each other and significantly lower than the commercial gelatin. Skin gelatin had exerted higher water holding capacity (2.36±0.11 ml/g), fat binding capacity (3.23±0.05 ml/g), foaming capacity ratio (1.88±0.07), and foam stability (1.51±0.04). Both the skin and bone gelatins were acidic. In this comparative study, it was noticed that the skin gelatin had better physical properties than the bone gelatin of native Pangasius catfish. Pangasius skin may be recognized as a potential aquatic source of edible gelatin with good yield and desirable physical properties comparing with commercial gelatin.
IOSR Journals , 2019
Gelatin is a hydrocolloid product obtained by hydrolyzing the protein collagen found in the skin, bones and connective tissue. Gelatin is obtained by heat denaturation from collagen. Gelatin has been applied in food as a gelling agent, thickener, emulsifier, pharmaceutical, health, cosmetics and photography industry. gelatin sourced from fish is still small. The purpose of this study was to determine the characteristics of milkfish skin gelatin with acetic acid 4%, 6% and 8%. The results showed that gelatin with the highest percentage of glycine. the best research results at a concentration of 8%, namely gel strength 98.07 g / bloom, Viscosity 6 cP, yield 19.4%. Use of high concentrations of acetic acid can decide which amino acids have been formed so that the amino acid chain of the damaged gelatin causes the gel strength to decrease. While the use of acid solutions with low concentrations can produce small gel strength because collagen is converted into less gelatin.It is also stated that amino acids in the skin of fish contain amino acids, such as Alanine, Arginine, Aspartate Acid, Cysteine, Glutamine, Glysin, Histidine Hydroxyprolin, Isoleucine and explained that the highest amino acid is Glycine. The quality of gelatin is influenced by the stages of the gelatin making process, namely swelling (extraction), extraction, and drying.
Properties of gelatin films from giant catfish skin and bovine bone: a comparative study
European Food Research and …, 2010
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 a-chains, b-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 lm) 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 (DE 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.
Review of Fish Gelatin Extraction, Properties and Packaging Applications
Based on physico-functional properties, gelatin is a biopolymer of great interest in food industry. Especially, its rheological and thermal properties diversify its applications. Mammalian gelatin is the main contributor to total gelatin production, but fish gelatin is also a potential alternative. The extraction method, fish type and intensity of the treatment determines the fate of produced gelatin. However, fish gelatin presents some less desirable properties due to the lesser amount of proline and hydroxyproline residues compared to the mammalian gelatins. Nonetheless, it has a good film forming ability and has been suggested as an alternative to the petroleum-based polymers. This review focusses on extraction, physicochemical properties and film forming ability of fish gelatin. Additionally, studies related to possible improvement in film barrier and mechanical properties are also enlisted. Furthermore, a minor description of legislation regarding toxicity issues of the frequently used active additives (plant extract and nanoparticles) in gelatin films is also presented. Fish gelatin applications should be expanded with the growing technological advances in industrial processes. 1. Introduction: As the global demand for gelatin is continuously on the rise, many potential sources are being sought for combating this growing need. In 2009, the global production of gelatin reached 326 thousand tons; majorly derived from pig skin, bovine hides, bones and others sources contributing 46%, 29.4%, 23.1% and 1.5%, respectively. Due to the fact that half of the production is harvested from porcine source, concerns about Halal or Kosher market strongly dominate. Moreover, in the case of bovine gelatin, the prevalence of spongiform encephalopathy necessitates a look up for possible alternatives (Karim and Bhat, 2009). Thus, fish (skin and bone) and other marine sources, along with insects (melon and sorghum bugs) are being exploited simultaneously. Nevertheless, fish, being in bulk and abundant, accounts more significantly than the insects. A number of studies have addressed the properties of fish skin gelatins, indicating that their properties differ from those of mammalian gelatins and vary among fish species. Technically, the term gelatin, applies for a series of proteins obtained from collagen after partial hydrolysis, obtained from bones, skin, hides, ligaments and cartilages, etc. (Gómez-Guillén and Montero, 2001). In the conversion process of collagen to gelatin, acid or alkali pretreatment hydrolyze the cross-linking bonds between polypeptides and irreversibly results in gelatin (Yang et al., 2008). The gelatin is water soluble and forms thermo-reversible gels with the melting temperature near to the body temperature (Norziah et al., 2009). The quality of resultant gelatin is determined by its physicochemical behavior that is further based on the species as well as the process of manufacture. Moreover, the specific amino acids and their respective amounts determine physical and functional behavior of gelatin. The higher the level of proline and hydroxyproline, the higher will be the melting point and gel strength (Karim and Bhat, 2009). According to one report (Farris et al., 2009) fish gelatin holds around 20% of proline and hydroxyproline than the bovine or porcine gelatins, which lower the gelling and melting by 5-10°C. Generally, compared to mammalian gelatin, fish gelatins hold lower gelling and melting temperatures, and lower gel strength as well (Norland, 1990). Gelatin is one of the most commonly used food additive and is an ingredient of many recipes. The proteinaceous nature of gelatin makes it an ideal food ingredient with high digestibility in certain types of diets (Johnston-Banks, 1990). As an additive, it improves water holding capacity, texture, elasticity, consistency and stability of foods (Zhou and Regenstein, 2005). Additionally, it has been used as a stabilizer, emulsifier, clarifying agent and as a protective coating material. Desserts, ice cream, jelled meat, confectionary, dairy and bakery foods are few of the main consumption areas for gelatin. Moreover, in pharmaceutics, it is used in manufacturing of capsules, tablet coatings, emulsions, ointments and skincare products. Despite the vast applicability of gelatin, theories about structure-function relationship are still under discussion. A 3D model is widely presented using fringed micelle model where microcrystallites are interconnected to amorphous segments of randomly-coiled regions. Some others suggest the presence of quaternary structures that are self-limiting in size, making triple helix or partial triple helix or turn and sheet motifs (Pena et al., 2010).
International Journal of Fisheries and Aquatic Studies, 2020
Gelatin is a derivative product from the hydrolysis of collagen contained in the bones and skin of animals. Gelatin is a polypeptide consisted of covalent bonds and peptide bonds between the amino acids that made it up. Gelatin is obtained by carrying out the hydrolysis process using acidic or alkaline solutions. Skin raw material is the largest raw material used by the gelatin industry because it has a higher collagen content, available in large quantities, and can be continuous. Quality characteristics of gelatin could be seen from several measurement results such as yield, ash content, fat content, protein levels, pH, viscosity, gel strength, isoelectric points, white degrees, amino acid content, and heavy metals content. Nowadays, the utilize of gelatine as the raw material, used in the food and non-food industries.