gelatin review

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.

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.

Fish solid wastes include different by-products such as bones, scales and hides that are high in collagen content and account for up to 75% of the total body weight. These wastes can be utilised for the extraction of different products such as gelatin that can be used in different food and pharmaceutical industries. Fish gelatin can be used as a replacement for mammalian gelatin due to its nutritional profile as it contains all the amino acids: essential and non-essential. Fish gelatin cannot only be used as a replacement for bovine and porcine gelatin but it also increases the utilisation of fish waste and reduces pollution. This review summarises the potential utilisation of different fish waste byproducts, extraction techniques and its application in different food products as an alternative to commercially available porcine and bovine gelatin.

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.

Open Access Research Journal of Biology and Pharmacy, 2022

Indonesia is one of the countries in Southeast Asia with the largest Muslim population in the world and the number is estimated at around 86%. This amount is actually a separate opportunity in marketing halal products and one of them is gelatin from fish skin. Gelatin is a protein extracted by partial hydrolysis of collagen, with the main component being protein derived from the skin of meat or fish, animal or fish bones and hides. The purpose of this study was to produce good quality fish skin gelatin with acetic acid treatment and soaking time of 12, 24 and 48 hours. The method used in this research is the experimental method on a laboratory scale. The results obtained in this study were that the rendemen of fish skin gelatin ranged from 7.50 to 7.60% with CH3COOH treatment. Meanwhile, the best pH value is acetic acid immersion with a time of 48 hours with a pH value of 2.8-6.2. Furthermore, the best organoleptic values ​​for attributes (color, texture and scent) are as follows; 6...

… Food Research Journal, 2010

The aims of this study were to determine the physicochemical properties of extracted gelatins from four freshwater fish skins: snakehead (Channa striatus), catfish (Clarias batrachus), pangasius catfish (Pangasius sutchi) and red tilapia (Oreochromis niloticus) and compare with those of commercial gelatins from cold water fish skin and bovine skin. The extraction yields for four types of extracted gelatins were high, ranging from 10.78% (w/w) (pangasius catfish gelatin) to 27.79% (w/w) (catfish gelatin). Four extracted gelatins showed lower protein content and higher lipid, moisture and ash content compared to both commercial gelatins. Red tilapia gelatin presented the highest gel strength (487.61 g). At 60°C, the shear viscosity of catfish gelatin (5.24mPa.s) was the highest. Four extracted gelatins had higher pH, isoionic point and turbidity compared to the commercial gelatins. These extracted gelatins were white in appearance and had higher L* value and lower a* value than both commercial gelatins.

Food Hydrocolloids, 2010

Gelatins from the skins of brownbanded bamboo shark (BBS; Chiloscyllium punctatum) and blacktip shark (BTS; Carcharhinus limbatus) were extracted using the distilled water at different temperatures (45, 60 and 75 ฐC) and times (6 and 12 h). Yields of gelatin from the skins of BBS and BTS were 19.06-22.81% and 21.17-24.76% (based on wet weight), respectively. Gelatins from both species extracted at 45 C for 6 h exhibited the highest bloom strength (206-214 g), which was higher than that of commercial bovine bone gelatin (197 g) (p < 0.05). Gelatin gels from BBS skin could set at room temperature (25-26 ฐC) within 24 min. However, gelatin gels from BTS skin was not able to set within 3 h at the same temperature. Scanning electron microscopic study showed that gelatin gel from BBS skin presented the thicker strand than those from BTS skin and bovine bone. Cross-linked components ([beta]- and [gamma]-chains) and [alpha]-chains were more degraded with increasing extraction temperatures, especially at 75 ฐC. Gelatin from BTS skin was more susceptible to hydrolysis than that from BBS skin. Fourier transform infrared (FTIR) study revealed that the major absorption bands of gelatin from the skins of both sharks shifted to a higher wavenumber, compared with their corresponding acid soluble collagen (ASC). Therefore, gelatins from the skin of BBS has a potential to replace mammalian for gelatin, due to its similarity in bloom strength and setting behavior to the commercial bovine bone gelatin.

Iranian Journal of Fisheries Sciences, 2019

One of the mainly popular consumed colloid protein materials in pharmaceutics, medical, food and military industries is Gelatin. Especially from warm-water fish gelatin report posses similar characteristics to mammal’s gelatin .Yellow fin tuna (Thunnus albacares) gelatin skin, lots of waste in form of skin and bone of the fish are produced every day. Analysis factors were extracted alkaline gelatin from skin, physiochemical and rheological test (amino acid composition, SDS- page electrophoreses, FTIR (Fourier transform infrared), moisture content, pH, setting point and setting time, melting point and melting time, color and gelatin yield). In contrast cool water fish gelatin, yellowfin tuna had higher gelatin content (Proline and Hydroxyproline) than mammalian gelatin content. SDS-electrophoresis for yellow fin gelatin showed protein band (α, β, γ) same as mammalian protein band. FTIR (Fourier transform infrared) had the same spectra for both of them. Factors were pH (6.1), Moistur...