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

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.

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

Jurnal Pengolahan Hasil Perikanan Indonesia ◽

10.17844/jphpi.v21i3.24734 ◽

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.

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Isolation and characterisation of collagen from elk antler velvet

Animal Production Science ◽

10.1071/an13281 ◽

2014 ◽

Vol 54 (8) ◽

pp. 1095

Author(s):

Do Hun Lee ◽

Heeok Hong ◽

Gaurav Lodhi ◽

Sun Hee Cheong ◽

Pyo Jam Park ◽

...

Keyword(s):

Cervus Elaphus ◽

Acid Content ◽

High Performance ◽

Type I Collagen ◽

Peptide Mapping ◽

Total Yield ◽

Type I ◽

Soluble Collagen ◽

Electrophoretic Patterns ◽

Imino Acid

Collagen was extracted from the antler velvet of elk (Cervus elaphus). Two types of collagen were prepared namely, acetic acid-soluble collagen and pepsin-soluble collagen. The electrophoretic patterns of both of the collagens showed that they were heterotrimeric, i.e. they consisted of α1α2α3. The total yield of the collagen obtained from the elk antler velvet was 12.1%. Amino acid analysis of the collagen by high-performance liquid chromatography showed that imino acid content such as that of proline and hydroxyproline was high, which might contribute to better visco-elastic properties. The peptide mapping of the collagens showed their similarity with porcine Type I collagen, thereby suggesting that the primary structure of both collagens is identical to that of porcine skin Type I collagen. The thermal denaturation temperature was 37°C, which is comparable to porcine Type I collagen and may also be as a result of high imino acid content.

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

Biotecnia ◽

10.18633/biotecnia.v23i3.1463 ◽

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.

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

Blood ◽

10.1182/blood.v128.22.3133.3133 ◽

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.

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

Advanced Materials Research ◽

10.4028/www.scientific.net/amr.236-238.2926 ◽

2011 ◽

Vol 236-238 ◽

pp. 2926-2934 ◽

Cited By ~ 4

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.

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

Marine Drugs ◽

10.3390/md19110597 ◽

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.

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Isolation of papain-soluble collagen from the skin of snake-head fish (Channa striata)

Canrea Journal: Food Technology, Nutritions, and Culinary Journal ◽

10.20956/canrea.v3i2.367 ◽

2020 ◽

pp. 87-93

Author(s):

Andi Rahmayanti Ramli ◽

Andi Rezky Annisa ◽

Nur Alim Bahmid ◽

Muhammad Dalvi Mustafa

Keyword(s):

Fourier Transform ◽

Moisture Content ◽

Polyacrylamide Gel Electrophoresis ◽

Fourier Transform Infrared ◽

Helical Structure ◽

Collagen Type I ◽

Type I ◽

Fish Skin ◽

Soluble Collagen ◽

Channa Striata

Snake-head fish (Channa striata) skin categorized a byproduct contains a higher concentration of collagen. The collagen can be extracted by using protease, which is known as Papain Soluble Collagen (PaSC). This study aimed to isolate the collagen from the snake-head fish skin using papain. The yield percentage and moisture content of PaSC in the skin was determined. Measurements using SDS-polyacrylamide gel electrophoresis (SDS-PAGE) and Fourier transform infrared spectroscopy (FTIR) were performed to characterize the PaSC and its functional groups. The results showed that the yields and moisture content of PaSC were 8.9% and 6.07%, respectively. The PaSC characterized by two α-chains appeared as collagen type I. Fourier transform infrared (FTIR) spectra of PaSC confirmed a triple-helical structure of collagen. The results indicated that snake-head fish skin could be used as potential resources of collagen and papain can be used as an alternative affordable enzyme.

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

Advanced Materials Research ◽

10.4028/www.scientific.net/amr.781-784.1728 ◽

2013 ◽

Vol 781-784 ◽

pp. 1728-1735 ◽

Cited By ~ 1

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.

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Comprehensive Assessment of Nile Tilapia Skin (Oreochromis niloticus) Collagen Hydrogels for Wound Dressings

Marine Drugs ◽

10.3390/md18040178 ◽

2020 ◽

Vol 18 (4) ◽

pp. 178 ◽

Cited By ~ 5

Author(s):

Baosheng Ge ◽

Haonan Wang ◽

Jie Li ◽

Hengheng Liu ◽

Yonghao Yin ◽

...

Keyword(s):

Wound Dressing ◽

Type I Collagen ◽

Polyacrylamide Gel Electrophoresis ◽

Sodium Dodecyl ◽

Wound Dressings ◽

Type I ◽

Rheological Characterization ◽

Scanning Calorimetry ◽

Soluble Collagen ◽

Collagen Hydrogels

Collagen plays an important role in the formation of extracellular matrix (ECM) and development/migration of cells and tissues. Here we report the preparation of collagen and collagen hydrogel from the skin of tilapia and an evaluation of their potential as a wound dressing for the treatment of refractory wounds. The acid-soluble collagen (ASC) and pepsin-soluble collagen (PSC) were extracted and characterized using sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE), differential scanning calorimetry (DSC), circular dichroism (CD) and Fourier transform infrared spectroscopy (FTIR) analysis. Both ASC and PSC belong to type I collagen and have a complete triple helix structure, but PSC shows lower molecular weight and thermal stability, and has the inherent low antigenicity. Therefore, PSC was selected to prepare biomedical hydrogels using its self-aggregating properties. Rheological characterization showed that the mechanical strength of the hydrogels increased as the PSC content increased. Scanning electron microscope (SEM) analysis indicated that hydrogels could form a regular network structure at a suitable PSC content. Cytotoxicity experiments confirmed that hydrogels with different PSC content showed no significant toxicity to fibroblasts. Skin repair experiments and pathological analysis showed that the collagen hydrogels wound dressing could significantly accelerate the healing of deep second-degree burn wounds and the generation of new skin appendages, which can be used for treatment of various refractory wounds.

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