Characteristics of acid and pepsin solubilized collagens from Nile tilapia (Oreochromis niloticus) scale (original) (raw)
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Evaluation of physicochemical properties of Nile tilapia skin collagen extracted in acid médium
Brazilian Journal of Biology, 2024
Tilapia has high-temperature tolerance, can breed in captivity, grow fast, and have excellent cost-benefit. Because of these characteristics, this species is of great interest in aquaculture and, currently, the most produced fish in Brazil. However, by increasing tilapia production, there was also a rise in the amount of organic waste, mainly from filleting, which discards 70% of waste. There are many studies on collagen extraction from tilapia skin as an alternative to reduce these residues and add commercial value. In this work, the extraction of protein concentrate was tested using an acid protocol, in which the tilapia skins underwent a pre-treatment in an acid medium and saline precipitation, with variations in time and concentration. After its extraction, the skin was evaluated for ash, moisture, protein, solubility, and pH. The protein concentrate obtained showed low ash contents, and the humidity is within those presented by the literature. The protein concentrate showed levels from 68.73 to 80.58% of protein and a low solubility between 4.03 to 6.93%. In conclusion, acid extraction is a possible means of collagen extraction, and tilapia skin is a good alternative to reuse waste generated in the fish industry.
International Journal of Biological Macromolecules, 2015
Collagen is considered to be one of the most useful biomaterials with different medical applications. However, collagen properties differ from one source to another. The aim of this study was to extract, purify, characterize and perform preliminary biological evaluation of type I collagen from scales of Egyptian Nile Tilapia. Pepsin-solubilized collagen (PSC) was successfully prepared from Nile Tilapia fish scale waste. Lyophilized collagen was dissolved in dilute HCl to form acidic collagen solutions (ACS) which was neutralized to form gel. To confirm the biocompatibility of the produced gel, baby hamster kidney (BHK-21) fibroblast cells were seeded onto a 3D collagen gel (0.3% and 0.5%, w/v). The results of an SDS-PAGE test showed that the extracted collagens were type I collagen, with ␣ chain composition of (␣1)2␣2. Thermal analysis showed that the denaturation temperature was 32 • C. X-ray diffraction (XRD) analysis and Fourier-transform infrared spectra (FTIR) showed that the extracted collagen had a triple helix structure. Active proliferation of BHK-21 cells with no signs of toxicity was evident with both collagen gel concentrations tested. The results show that Nile Tilapia scales can be an effective source of collagen extraction that could be used as a potential biomaterial in biomedical applications.
2018
Bonylip barb fish is one of the local fish species in Indonesia. This fish has a high egg productivity so that the eggs used as raw materials caviar. One of the waste generated from the production process is the skin of Bonylip barb fish. This study aims to characterize the physical and chemical properties of collagen extracted from the skin of Bonylip barb fish. The extraction method used is soluble collagen enzyme pepsin (Pepsin soluble collagens). The results showed that the yield of collagen extracted from the skin of Bonylip barb fish was 6.18% (wet weight). The collagen has moisture, protein, fat and ash content of 9.04%, 90.09%, 0.56% and 1.28%, respectively. The most common type of amino acid is glycine (16.56%) and the smallest is histidine (0.28%). Based on the amino acid content and functional groups, the collagen extracted from the skin of this fish includes collagen type I. The specific viscosity and reduced at a temperature of 28°C each of 0.1784 cp and 8.922 Dl/g and ...
Biotecnia
Fish by-products consisting of skin, bones, or scales are collagen sources. Acid-soluble collagen (ASC) and pepsin-soluble collagen (PSC) mixed by-products derived from different fish species were extracted and evaluated. The properties evaluated for both collagens were chemical composition, amino acid- and SDS-PAGE- protein profiles, Fourier transform infrared spectroscopy (FTIR), denaturation temperature (Tmax), enthalpy (ΔH), and solubility. The ASC and PSC registered a protein content of 48.56 and 38.80 %, respectively. From the total amino acids detected, hydroxyproline accounted for 7 % and 6 % for ASC and PSC, respectively. The electrophoretic profile showed the presence of the type I collagen bands (α1, α2, β, and γ), whereas FTIR spectrum showed the presence of diverse collagen functional groups (Amide A, B, I, II, and III) for both extracted types, and demonstrated that the extraction process did not affect the collagen´s triple-helical structure. The Tmax of ASC and PSC w...
Acid-Pepsin Soluble Collagen from Saltwater and Freshwater Fish Scales
Engineering Journal, 2019
Extraction and characterization of acid soluble collagen (ASC) and pepsin soluble collagen (PSC) from scales of Giant groupers (saltwater fish) and Nile tilapia (freshwater fish) were carried out in this research. Due to a higher protein content in scales, collagen yield extracted from the Giant groupers scales was higher than that of the Nile tilapia scales. The yield increased as extraction time increased for both ASC and PSC and pepsin extraction resulted in higher yields than acid extraction. Even though there were differences in collagen yields, collagen characteristics were independent of the scale sources but some differences were observed for the ASC and PSC. The peptide hydrolysis patterns of the ASC showed a wide range of molecular weights whereas all of the PSC had similar molecular weight of around 42 kDa. FTIR spectra showed that all the collagens remained the triple helical structure though ASC might be self-aggregated. From zeta potential analysis, net charge of zero was found at pH 3.2-4.0 and the dynamic light scattering suggested that the average particle sizes at pH 11-12 were around 100-200 nm. The denaturation temperatures (Tds) in a range of 35-42 o C indicated that the collagens were considerably thermally stable.
Natural Product Communications, 2019
Collagen from fish scale waste is currently being studied as a promising biological material to replace collagen from animals because of advantages such as safe, fat-free, not suffering from communicable diseases, and easy absorption in human body solutions. Finding the suitable process of extracting fish scale collagen is necessary because extracting collagen from fish scales by chemical methods often requires a long time. Therefore, in this paper, some bases and acids at different concentrations were chosen to find the most suitable condition for extracting fish scale collagen from the wastage of different scale fishes belonging to the familiar Cyprinus genus. The characterizations of the extracted collagen including structure, morphology, element composition, relative molecular weight, amino acid composition, denaturation temperature, crystal structure, and thermal stability were investigated. In addition, the amino acid sequence of the extracted collagen was also determined and ...
Proceedings of the International Conference on Green Technology
Basa fish (Pangasianodon hypopthalmus) is the top fifth most consumed fish in Thailand. The production of Basa fish generates a large number of by-products. Nowadays, most of these residues are recovered as animal feedstocks or fertilizer. However, it is interesting to explore another choice of waste management practice such as the recovery of valuable material. This study aimed to extract collagen from the skin and bone of Basa fish (Pangasianodon hypopthalmus) by using a green solvent. Two extraction methods were carried out. First, the conventional extraction was conducted by using acetic acid and compared with the physical extraction which employed water acidified with carbon dioxide. Conventional extraction was conducted using 0.75 M acetic acid at 4oC and solid-liquid ratio 1:40 (w/v). The physical extraction using water acidified by carbon dioxide was conducted at 37oC, 10 bars and solid-liquid ratio 1:40 (w/v). The extraction time of each technique was varied from 3 to 24 ho...
The Evaluation of the Suitability of Fish Wastes as a Source of Collagen
Fish wastes such as skin, scales, bones and fins are major by-products in the fishery and aquaculture industries which have high collagen content. Therefore, an investigation into making more effective use of under-utilized resources, acid-solubilised collagen (ASC) was extracted from fish skin, scales bones and fins. As a result, the yields of skin, scales, bones and fins collagens are 70.67%, 13.03%, 38.03% and 40%, respectively. SDS-PAGE pattern showed that ASCs of fish skin, scales, bones and fins are all type I collagen, which are composed β, α1 and α2 chains. The molecular weight of fish skin, scale and fin α1, α2 and β chains are 132.044kDa, 120.065kDa and 220.673kDa, whereas the molecular weight of fish bone α1, α2 and β chains are 139.798kDa, 124.72kDa and 229.229kDa. Denaturation temperatures (Td) of ASCs from skin, scales, bones and fins were 32.4C, 35.8C, 37.8C and 32C, respectively. Fourier transform infrared spectroscopy proved that ASCs are integrated and native. ...
2019
Department of Food Science and Technology, Tokyo University of Marine Science and Technology, 4-5-7 Konan, Minato-ku, Tokyo 108-8477, Japan Department of Marine Biosciences, Tokyo University of Marine Science and Technology, 4-5-7 Konan, Minato-ku, Tokyo 108-8477, Japan Center of Excellence in Food Processing Pilot Plant, Faculty of Science, Chulalongkorn University, 254 Phayathai Road, Wangmai, Pathumwan, Bangkok 10330, Thailand
Applied Sciences
The by-product of needlefish (Tylosurus acus melanotus) waste possesses important characteristics that could be used in food applications. Fish by-product collagen may be used in place of mammalian collagen due to ethical and religious considerations over environmental degradation. Different forms of acid-soluble collagen (ASC) were successfully extracted from needlefish skin. Based on dry weight, the collagen extracted using acetic acid (AAC), lactic acid (LAC), and citric acid (CAC) treatments was 3.13% with a significantly difference (p < 0.05), followed by 0.56% and 1.03%, respectively. Based on proximate analysis, the needlefish skin composition was found to be significantly different (p < 0.05) between compositions, with the highest moisture content at 61.65%, followed by protein (27.39%), fat (8.59%), and ash (2.16%). According to the SDS-PAGE results, all extracted collagen were identified as a type 1 collagen. Additionally, ATR-FTIR revealed that all collagens had ami...