Characteristics of Physical-Chemical Properties of Collagen Extracted from the Skin of Bonylip Barb Fish (Osteochilus vittatus) (original) (raw)
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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...
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...
Journal of Aquaculture and Fish Health
Collagen is a connective tissue protein that is mostly produced from cattle and pigs. The use of cows and pigs as the manufacture of collagen causes a disease case, among others are bovine spongiform encephalopathy and transmissible spongiform disease. One of the alternative materials in the isolation of collagen is the use of fish skin. The purpose of this study was to determine the effect of the concentration of acetic acid solution on the characteristics of red snapper collagen produced by the hydroextraction method and to determine the optimum concentration of acetic acid solution in the red snapper skin collagen isolation process using the hydroextraction method. This study was experimental with Completely Randomized Design (CRD) consisting of 3 acetic acid treatment: (P1) acetic acid with concentration 0,1 M; (P2) 0,15 M and (P3) 0,2 M. This study showed that the use of different acetic acid had a significant effect (p<0.05) on the yield parameters that is 1.72 – 2.46%, wat...
Emirates Journal of Food and Agriculture
In Thailand, the production of tilapia is about 140,000 tons, which is the sixth tilapia production in the world. From the processing, the scale was generated as waste. To produce a value-added product, the production of collagen from tilapia scale could be an alternative. Generally, collagen from fish scale possesses a less fishy odor and flavor than that from fish bone and skin. From the results, the fish scale is an interesting alternative source for collagen extraction. The objectives of this study were to extract collagen from Nile tilapia (Oreochromis niloticus) scale from the production of frozen tilapia fillet as well as to study its properties. Extraction of acid (ASC) and pepsin soluble collagens (PSC) from Nile tilapia scale, as well as the determination of their yield, amino acid compositions, SDS-PAGE patterns, FTIR spectra, thermal denaturation temperature (Tmax) and zeta potential, was conducted. ASC and PSC had a yield of 0.77 and 0.71% based on dry basis), respectiv...
Preparation and Characterisation of Collagen from Freshwater Fish Scales
Acid-soluble collagen (ASC) and pepsin-solubilized collagen (PSC) were prepared from the waste freshwater carp fish scales. The results of SDS-PAGE showed that purified collagens were composed of at least two different chains which were in accordance with the type I collagen with α chain composition of (α 1) 2 α 2. Compared with the carp fish ordinary muscle type I collagen, porcine dermis type I collagen and other seawater fish collagens, freshwater carp fish scales collagen contained relative high half-cystine (Cys-s), but lower denaturation temperature(Td) than the porcine dermis type I collagen. These collagens had evident absorption at 230 nm by UV-Vis spectra. The spectrum X-ray diffraction showed that the collagen remained single-helix and tri-helix configuration with the minimum values of the repeat spac-ings (d) of about 4.48 Å and 11.87 Å. Therefore, to make more effective use of limited-resources, carp fish scales can be a potential resource for the extraction of type I collagen or gelatin.
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.
Food Chemistry, 2011
Acid soluble collagen (ASC) and pepsin soluble collagen (PSC) were extracted from scale of spotted golden goatfish (Parupeneus heptacanthus) with the yields of 0.46% and 1.20% (based on dry weight basis), respectively. Both ASC and PSC were characterised as type I collagen, containing a 1 and a 2 chains. b and c components were also found in both collagens. Based on FTIR spectra, the limited digestion by pepsin did not disrupt the triple helical structure of collagen. ASC and PSC contained glycine (336-340 residues/1000 residues) as the major amino acid and had imino acids of 186-189 residues/1000 residues. Maximal transition temperatures (T max) were 41.58 and 41.01°C for ASC and PSC, respectively. From zeta potential analysis, net charge of zero was found at pH 4.96 and 5.39 for ASC and PSC, respectively. Both collagens exhibited high solubility in acidic pH (2-4) and were soluble in the presence of NaCl at concentration up to 20 and 30 g/l for ASC and PSC, respectively.
Food Research International, 2013
Acid-solubilized collagen (ASC) and pepsin-solubilized collagen (PSC) were extracted from the skin of sail fish (Istiophorus platypterus) with yields of 5.76% and 2.11% respectively, on the basis of wet weight. According to the electrophoretic pattern, ASC and PSC consisted of two different α chains (α1 and α2) and were characterized as Type I collagen. Peptide maps of ASC and PSC hydrolysed by Achromopeptidase from Achromobacter lyticus exhibited similar banding patterns with human-placenta collagen suggesting, sailfish collagen is a Type I collagen. Fourier transform infrared (FTIR) spectra of ASC and PSC were quite similar and the regions of amides A, I, II and III were 3422 and 3337, 1654 and 1646, 1560 and 1559 and 1240 cm −1 respectively. FTIR results suggest that the pepsin hydrolysis did not affect the secondary structure of collagen, especially triple-helical structure. 1 H NMR analysis revealed the presence of water molecules along with their corresponding singlet medium chemical shift of about 4.6 to 4.8 ppm in ASC and PSC. Scanning electron microscopy (SEM) studies confirmed the presence of collagen in the isolated, as fine globular filaments. Thus, possibility of sail fish collagen as an alternative source for mammalian collagen and also it could be used in nutraceutical and pharmaceutical industries.
Gels
Reducing food waste is critical for sustainability. In the case of fish processing, more than sixty percent of by-products are generated as waste. Lizardfish (Saurida tumbil Bloch, 1795) is an economically important species for surimi production. To address waste disposal and maximize income, an effective utilization of fish by-products is essential. This study aims to isolate and characterize pepsin-soluble collagens from the skin, bone and scales of lizardfish. Significant differences (p < 0.05) in the yields of collagen were noted with the highest yield recorded in pepsin-soluble skin collagen (PSSC) (3.50 ± 0.11%), followed by pepsin-soluble bone collagen (PSBC) (3.26 ± 0.10%) and pepsin-soluble scales collagen (PSCC) (0.60 ± 0.65%). Through SDS–polyacrylamide gel electrophoresis, the presence of two alpha chains were noted and classified as type I. From Fourier transform infrared spectroscopy (FTIR) analysis, the triple-helix structure of the collagen was maintained. The X-r...
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.