scholarly journals Isolation and properties of collagen extracted from mixed by-products obtained from different fish species

Biotecnia ◽  
2021 ◽  
Vol 23 (3) ◽  
pp. 109-116
Author(s):  
Celia Olivia García-Sifuentes ◽  
Julio Cesar Zamorano-Apodaca ◽  
Marcel Martinez-Porchas ◽  
Susana Maria Scheuren-Acevedo ◽  
Miguel Angel Mazorra-Manzano
Keyword(s):  
Fish Species ◽  
Type I Collagen ◽  
Helical Structure ◽  
Extraction Process ◽  
Type I ◽  
Denaturation Temperature ◽  
Soluble Collagen ◽  
Acid Soluble Collagen ◽  
Sds Page ◽  
By Products

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 were 38.27 and 38.07° C, respectively, whereas ΔH were 0.64 and 0.33 J g-1. The lowest solubility was registered at pH 5 for ASC and pH 9 for PSC. The caractheristics of the collagen extracted, indicated that a mixture of by-products from different species could be an alternative for their reutilization by the local markets.

Extraction and Partial Characterization of Pepsin-Soluble Collagens from the Skin of Amiurus Nebulosus

2011 ◽  
Vol 236-238 ◽  
pp. 2926-2934 ◽  
Author(s):  
Li Li Chen ◽  
Li Zhao ◽  
Hua Liu ◽  
Run Feng Wu
Keyword(s):  
Type I Collagen ◽  
Type I ◽  
Alternative Source ◽  
Soluble Collagen ◽  
Acid Soluble Collagen ◽  
Sds Page ◽  
Skin Collagen ◽  
Maximal Yield ◽  
Pepsin Soluble Collagen

Pepsin-soluble collagen (PSC) was successfully extracted from the skin of Amiurus nebulosus. The skin of Amiurus nebulosus was immersed in 0.3 mol/L acetic acid (1: 20, m: V) for 6 h at 37°C, while pepsin was added, at a level of 5000U/g dosage of defatted skin. The maximal yield of the collagen was 97.44%, which was higher than that of acid-soluble collagen (ASC) at 62.05%. Some properties of pepsin-soluble collagens from the skin of Amiurus nebulosus were characterized. Amino acid composition and SDS-PAGE suggested that the collagen might be classified as type I collagen. Moreover, FTIR investigations showed the existence of helical arrangements in PSC of Amiurus nebulosus skin of collagen. There is a possibility to use Amiurus nebulosus skin collagen as an alternative source of collagen for industrial purposes and subsequently it may maximize the economical value of the fish.

scholarly journals Characterization of Acid-Soluble Collagen from Food Processing By-Products of Snakehead Fish (Channa striata)

Processes ◽  
2021 ◽  
Vol 9 (7) ◽  
pp. 1188
Author(s):  
Thi Mong Thu Truong ◽  
Van Muoi Nguyen ◽  
Thanh Truc Tran ◽  
Thi Minh Thuy Le
Keyword(s):  
Acid Content ◽  
Type I Collagen ◽  
Type I ◽  
Fish Skin ◽  
Soluble Collagen ◽  
Acid Soluble Collagen ◽  
Imino Acid ◽  
Channa Striata ◽  
Α Helix ◽  
By Products

The isolation of acid-soluble collagen (ASC) from by-products of snakehead fish (Channa striata), including skin and the mixture of skin and scale, has been investigated. The recovery yield of fish skin ASC (13.6%) was higher than ASC from fish skin and scale (12.09%). Both ASCs were identified as type I collagen and showed maximal solubility at pH 2. Collagen samples from the mixture of skin and scale had higher imino acid content (226 residues/1000 residues) and lower wavenumber in the amide I and amide III region (1642 and 1203 cm−1, respectively) than the fish skin ASC (the imino acid content was 220 residues/1000 residues and the wavenumber in the amide I and amide III were 1663 and 1206 cm−1, respectively. The difference scanning calorimeter (DSC) showed higher thermal stability in ASC from the mixture of skin and scale (Td of 35.78 °C) than fish skin ASC (34.21 °C). From the result, the denaturation temperature of ASC had a close relationship with the content of imino acid as well as with the degradation of α-helix in amide I and III. These results suggest that collagen could be obtained effectively from snakehead fish by-products and has potential as a realistic alternative to mammalian collagens.

A Newly Identified Platelet and Megakaryocyte Lysyl Oxidase-Adhesion to Collagen Axis in Human Primary Myelofibrosis

Blood ◽  
2016 ◽  
Vol 128 (22) ◽  
pp. 3133-3133
Author(s):  
Alessandra Balduini ◽  
Vittorio Abbonante ◽  
Shinobu Matsuura ◽  
Vittorio Rosti ◽  
Katya Ravid
Keyword(s):  
Type I Collagen ◽  
Conflicts Of Interest ◽  
Lysyl Oxidase ◽  
Primary Myelofibrosis ◽  
Collagen Type I ◽  
Type I ◽  
Soluble Collagen ◽  
Peripheral Blood Cd34 ◽  
Acid Soluble Collagen

Abstract Controlling platelet function is central to management of various pathologies, including Primary Myelofibrosis (PMF), which is associated with increased incidence of thrombosis and cardiovascular disease. In recent studies we showed that the matrix cross-linking enzyme, Lysyl Oxidase (LOX) is elevated in platelets and megakartocytes of myelofibrotic mice, and transgenic upregulation of LOX increases platelet and megakaryocyte adhesion to monomeric type I collagen (preferred by alpha2β1 collagen receptors), and augments propensity for in vivo thrombosis. Here, we examined the relevance of these findings to human disease, by first determining platelet LOX level, as well as platelet and megakaryocyte adhesion to collagen using samples derived from PMF patients and matching controls. In analyzing 10 PMF platelet samples (5 males and 5 females; 6 JAK2V617F; 4 CALR mutations; age range 30-55; PMF grade 1-3), we found a nearly 20 fold upregulation of LOX expression compared to matching healthy controls (p<0.001). Intriguingly, there was a significant increase in adhesion (plt/mm2) and spreading (pixel2) of PMF platelets relative to control on monomeric, pepsinated acid soluble collagen (PSCI) (p<0.05), while no differences were observed between the samples on native triple helical acid soluble collagen type I collagen (ASCI). To examine the role of LOX in this phenotype, we treated control and PMF-derived human megakaryocytes, differentiated from peripheral blood CD34+ cells, grown in presence or not of LOX inhibitor, β-aminopropionitrile (BAPN) from day 2 of culture. Our preliminary data, based on a cohort of 2 controls and 5 PMF samples, demonstrated that although on ASCI megakaryocyte adhesion is not altered by BAPN treatment both in CTRL and PMF derived megakaryocytes, on PSCI the adhesion of PMF derived megakaryocytes was reduced by about a 50% by BAPN treatment, while the adhesion of CTRL derived MKs was not significantly affected. Taken together, we identified LOX level to be upregulated in human PMF platelets and megakaryocytes, and LOX activity to be important for PMF cells adhesion to collagen. These newly identified properties are highly relevant to megakaryocyte adhesion to the niche, and to platelet activation in PMF. Disclosures No relevant conflicts of interest to declare.

scholarly journals Preparation and Characterization of Thermally Stable Collagens from the Scales of Lizardfish (Synodus macrops)

Marine Drugs ◽  
2021 ◽  
Vol 19 (11) ◽  
pp. 597
Author(s):  
Junde Chen ◽  
Guangyu Wang ◽  
Yushuang Li
Keyword(s):  
Type I Collagen ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Type I ◽  
Salting Out ◽  
Soluble Collagen ◽  
Acid Soluble Collagen ◽  
Skin Collagen ◽  
Rat Tail

Marine collagen is gaining vast interest because of its high biocompatibility and lack of religious and social restrictions compared with collagen from terrestrial sources. In this study, lizardfish (Synodus macrops) scales were used to isolate acid-soluble collagen (ASC) and pepsin-soluble collagen (PSC). Both ASC and PSC were identified as type I collagen with intact triple-helix structures by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and spectroscopy. The ASC and PSC had high amino acids of 237 residues/1000 residues and 236 residues/1000 residues, respectively. Thus, the maximum transition temperature (Tmax) of ASC (43.2 °C) was higher than that of PSC (42.5 °C). Interestingly, the Tmax of both ASC and PSC was higher than that of rat tail collagen (39.4 °C) and calf skin collagen (35.0 °C), the terrestrial collagen. Solubility tests showed that both ASC and PSC exhibited high solubility in the acidic pH ranges. ASC was less susceptible to the “salting out” effect compared with PSC. Both collagen types were nontoxic to HaCaT and MC3T3-E1 cells, and ASC was associated with a higher cell viability than PSC. These results indicated that ASC from lizardfish scales could be an alternative to terrestrial sources of collagen, with potential for biomedical applications.

scholarly journals Extraction and characterization of acid-soluble collagen and pepsin-soluble collagen from the dry scales of the striped snakehead (Channa striatus)

2018 ◽  
Vol 21 (3) ◽  
pp. 513
Author(s):  
Bagus Fajar Pamungkas ◽  
Supriyadi Supriyadi ◽  
Agnes Murdiati ◽  
Retno Indrati
Keyword(s):  
Type I Collagen ◽  
Raw Materials ◽  
Acid Group ◽  
Extraction Methods ◽  
Type I ◽  
Channa Striatus ◽  
Soluble Collagen ◽  
Acid Soluble Collagen ◽  
Imino Acid ◽  
Pepsin Soluble Collagen

Characteristics of collagen are influenced by the source of raw materials and extraction methods used. The aim of this research was to characterize the acid- and pepsin-soluble collagens from the dry scales of the striped snakehead (Channa striatus). Collagen was extracted using to methods including 0.5 M acetic acid and 0.1% pepsin. The yield of acid soluble collagen (KLA-SH) and pepsin soluble collagen (KLP-SH) were 0.98% and 1.94%, respectively. KLA-SH and KLP-SH contained glycine as the major amino acid and had high imino acid group content i.e 226 and 230 residues/1.000 residues, respectively. FTIR spectra of KLA-SH and KLP-SH showed that of the structure of collagen could be maintained in the form of triple helix structure. KLA-SH and KLP-SH consisted of α1- and α2-chain, β-chain, and γ-chain and is suggested as type I collagen.

scholarly journals Salt-Cured Atlantic Cod Skin: A Sustainable Source of Acid-Soluble Type I Collagen

2021 ◽  
Author(s):  
Ezequiel Coscueta ◽  
María Emilia Brassesco ◽  
Manuela Pintado
Keyword(s):  
Gadus Morhua ◽  
Type I Collagen ◽  
Atlantic Cod ◽  
Electrophoretic Pattern ◽  
Helical Structure ◽  
Extraction Yield ◽  
Type I ◽  
Acid Soluble Collagen ◽  
Typical Type ◽  
Alternative Sources

Collagen is the most abundant protein in the animal kingdom. Industrial collagen is mainly bovine and porcine origin. However, due to religious beliefs, allergic issues, and infectious diseases, alternative sources of collagen as marine are gaining increasing interest. In this work, the acid-soluble collagen (ASC) were extracted from salt-cured Atlantic cod (Gadus morhua) skin and characterized. The extraction yield was about 2.0%, equivalent to the extraction yield reported for other fish skins. The electrophoretic pattern showed the typical type I structure (&alpha;, &beta; and &gamma; chains). UV-VIS and FTIR absorbance spectra suggested a very pure ASC with an intact triple helical structure. The integrity and the adequate porosity required for different applications were then confirmed by electron micrograph. Our findings allow us to say that, for the first time, we extracted acid-soluble type I collagen from salt-cured Atlantic cod skin, with characteristics suitable for application in various fields, such as biomedical.

Isolation and Characterization of Acid-Soluble Collagen from the Skin of Amiurus nebulosus

2013 ◽  
Vol 781-784 ◽  
pp. 1728-1735 ◽  
Author(s):  
Li Li Chen ◽  
Li Zhao ◽  
Mei Lan Yuan ◽  
Wei Su ◽  
Hua Liu
Keyword(s):  
Type I Collagen ◽  
Raw Materials ◽  
Type I ◽  
Alternative Source ◽  
Shrinkage Temperature ◽  
Soluble Collagen ◽  
Isolation And Characterization ◽  
Acid Soluble Collagen ◽  
Commercial Applications ◽  
Effective Use

During fish processing, a large amount of waste, of the original raw materials is generated, such as skin, bone, scale, viscera and head. These useful resources have been mainly used as feedstuff or fertiliser with low value. To make more effective use of underutilized resources, collagen was isolated from the skin of Amiurus nebulosus using acetic acid and characterized for their potential usage in commercial applications. The yield of acid-soluble collagen (ASC) was 62.05% while the maximum absorbance of ASC was at 234 nm. Amino acid composition and SDS - PAGE suggested that the collagen is possibly possessive of type I collagen. Moreover, FTIR investigations showed the existence of helical arrangements of collagen where the denaturation temperature (Td) and shrinkage temperature (Ts) were 29.8°C and 65.12°C, respectively. There is a possibility that ASC could be utilized as an alternative source of collagen for food, cosmetic, biomedical and pharmaceutical purposes.

Analysis and improvement of stability of pepsin-solubilized collagen from skin of carp (Cyprinus carpio)

2012 ◽  
Vol 66 (7) ◽  
Author(s):  
Rui Duan ◽  
Jun-Jie Zhang ◽  
Kunihiko Konno ◽  
Mei-Hua Wu ◽  
Jing Li ◽  
...  
Keyword(s):  
Acetic Acid ◽  
Cyprinus Carpio ◽  
Short Peptides ◽  
Type I ◽  
Improved Method ◽  
Soluble Collagen ◽  
Acid Soluble Collagen ◽  
Dialysis Solution ◽  
Sds Page ◽  
Carp Cyprinus Carpio

AbstractPepsin is widely used for the extraction of pepsin-solubilized collagens (PSC) from many resources. PSC-A and PSC-P were prepared from carp skin using 0.1 mol L−1 acetic acid and 0.02 mol L−1 Na2HPO4 (pH 7.2) as the dialysis solution, respectively. SDS-PAGE patterns showed PSC-A and PSC-P as type I collagens, as well as acid soluble collagen (ASC). When incubated at 40°C, no degradation was observed for ASC, but PSC-A and PSC-P were degraded into short peptides, showing lower stability than ASC. The results indicate that pepsin remaining in the PSCs resulted in their degradation, which was confirmed by the inhibition using pepstatin. This research revealed the behavior of the remaining pepsin in pepsin-solubilized collagens and an approach to the PSC stability improvement was proposed. Chromatography profiles showed that new PSC prepared by the improved method had almost the same stability as ASC.

scholarly journals Comparison of Physicochemical Characteristics and Fibril Formation Ability of Collagens Extracted from the Skin of Farmed River Puffer (Takifugu obscurus) and Tiger Puffer (Takifugu rubripes)

Marine Drugs ◽  
2019 ◽  
Vol 17 (8) ◽  
pp. 462 ◽  
Author(s):  
Wang ◽  
Yu ◽  
Sun ◽  
Liu ◽  
Zhou
Keyword(s):  
Type I Collagen ◽  
Molecular Form ◽  
Formation Rate ◽  
Helical Structure ◽  
Fibril Formation ◽  
Takifugu Rubripes ◽  
Type I ◽  
Soluble Collagen ◽  
Skin Collagen ◽  
Tiger Puffer

Acid-soluble collagen (ASC) and pepsin-soluble collagen (PSC) from the skin of river puffer (ASC-RP and PSC-RP) and tiger puffer (ASC-TP and PSC-TP) were extracted and physicochemically examined. Denaturation temperature (Td) for all the collagens was found to be 25.5–29.5 °C, which was lower than that of calf skin collagen (35.9 °C). Electrophoretic patterns indicated all four samples were type I collagen with molecular form of (α1)2α2. FTIR spectra confirmed the extracted collagens had a triple-helical structure, and that the degree of hydrogen bonding in ASC was higher than PSC. All the extracted collagens could aggregate into fibrils with D-periodicity. The fibril formation rate of ASC-RP and PSC-RP was slightly higher than ASC-TP and PSC-TP. Turbidity analysis revealed an increase in fibril formation rate when adding a low concentration of NaCl (less than 300 mM). The fibril formation ability was suppressed with further increasing of NaCl concentration, as illustrated by a reduction in the turbidity and formation degree. SEM analysis confirmed the well-formed interwoven structure of collagen fibrils after 24 h of incubation. Summarizing the experimental results suggested that the extracted collagens from the skin of river puffer and tiger puffer could be considered a viable substitute to mammalian-derived collagens for further use in biomaterial applications.

scholarly journals Cytotoxicity evaluation and physicochemical properties of collagen isolated from silver carp tails as potential biomaterial

2021 ◽  
Vol 26 (4) ◽  
pp. 2808-2817
Author(s):  
PETRUTA PREDA ◽  
ANA-MARIA ENCIU ◽  
MARIOARA AVRAM ◽  
CRISTIANA TANASE ◽  
MARIA DUDAU ◽  
...  
Keyword(s):  
Type I Collagen ◽  
Genetic Diseases ◽  
Silver Carp ◽  
Wound Dressings ◽  
Type I ◽  
Hypophthalmichthys Molitrix ◽  
Alternative Source ◽  
Sds Page ◽  
Fish Collagen ◽  
By Products

Collagen is widely used as a biomaterial in the pharmaceutical and cosmetic industries, in the production of hydrogels, wound dressings, bioactive nano/microfibers, controlled drug delivery systems, etc. The collagen isolated from the aquatic source has a higher biological activity and low risk of transmitting genetic diseases. In recent years the sustainable socio-economic and environmental principles promote the full use of natural resources. Thus, fish collagen extracted from fish by-products (skin, scales, bones and fins) can be valorized as a new collagen alternative source. In this work the enzymatic hydrolysis with pepsin of collagen isolation from silver carp (Hypophthalmichthys molitrix) tails fish has been investigated. We successfully isolated type I collagen with 90-95% purity as determined by FTIR, UV-Vis, EDX and SDS-PAGE analyses. The cytotoxicity of obtained collagen was evaluating by MTS assays.

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