scholarly journals Review Article: Fish Bone Collagen

2021 ◽  
pp. 33-39
Author(s):  
Andre Wijaya ◽  
. Junianto
Keyword(s):  
Type I Collagen ◽  
Ph Value ◽  
Amino Acid Content ◽  
Extraction Process ◽  
Fish Bone ◽  
Raw Material ◽  
Bone Collagen ◽  
Type I ◽  
Alternative Source ◽  
Salting Out

Fishbone collagen is an alternative source of bovine and pig collagen. The purpose of this article is to review the types, benefits, extraction methods and characterization of collagen from fish bones, especially freshwater fish. The result of the review shows that the collagen from tilapia bones is shaped like a sheet with a slight porous surface and is of type I. Collagen extraction begins with bone disease from the remaining fat, then degreasing and the next step is extraction. After the extraction process is complete, filtration is carried out to store the filtrate or residue, then the collagen is purified by salting-out with NaCl. Collagen yield and collagen pH value from collagen extraction were different for each type of fish bone. The difference in yield value and protein and amino acid content in the resulting collagen can be caused by differences in the extraction method, the concentration of the solution used, whether acid or alkaline, and the neutralization process and the type of raw material. Fishbone collagen has good benefits in the cosmetic and pharmaceutical fields.

scholarly journals Extraction Optimization and Characterization of Collagen from Yellow Pike Conger Swimbladder with Acid-Hydro-Exctraction Method

2016 ◽  
Vol 19 (2) ◽  
pp. 156 ◽  
Author(s):  
Fernandy Djailani ◽  
Win Trilaksani ◽  
Tati Nurhayati
Keyword(s):  
Amino Acid ◽  
Acid Content ◽  
Type I Collagen ◽  
Amino Acid Content ◽  
Extraction Time ◽  
Yield Response ◽  
Type I ◽  
Alternative Source ◽  
Extraction Optimization ◽  
Ft Ir

Swim bladder is one of marine potential byproducts for alternative source of collagen. This study aimed<br />to optimize hydro-extraction and characterized collagen. Extraction optimization of collagen was determined<br />using Box-behnken design response surface method with three variables: CH3COOH concentration, soaking<br />time and extraction time to yield response. Hydro-extraction collagen was characterization based on the<br />amino acid content, SDS-PAGE, FT-IR and DSC. Acording to the result, the concentration had significantly<br />influence yield. Optimum extraction conditions were variable combinations of acetic acid concentration of<br />0.1 M, for 1 h and hydro-extraction time of 1 h to produce the highest yield 63.35%. collagen was classified<br />as type I collagen by amino acid content, electrophoresis patterns and fourier transform infrared (FTIR)<br />spectra. The glass transition of collagen was 67.23oC, showed high thermal stability that can be applied to<br />the cosmetics industry and nutraceutical.<br /><br />

scholarly journals Extraction Optimization and Characterization of Collagen from Yellow Pike Conger Swimbladder with Acid-Hydro-Exctraction Method

2016 ◽  
Vol 19 (2) ◽  
pp. 156
Author(s):  
Fernandy Djailani ◽  
Wini Trilaksani ◽  
Tati |Nurhayati
Keyword(s):  
Amino Acid ◽  
Acid Content ◽  
Type I Collagen ◽  
Amino Acid Content ◽  
Extraction Time ◽  
Yield Response ◽  
Type I ◽  
Alternative Source ◽  
Extraction Optimization ◽  
Ft Ir

Swim bladder is one of marine potential byproducts for alternative source of collagen. This study aimed to optimize hydro-extraction and characterized collagen. Extraction optimization of collagen was determined using Box-behnken design response surface method with three variables: CH3 COOH concentration, soaking time and extraction time to yield response. Hydro-extraction collagen was characterization based on the amino acid content, SDS-PAGE, FT-IR and DSC. Acording to the result, the concentration had significantly influence yield. Optimum extraction conditions were variable combinations of acetic acid concentration of 0.1 M, for 1 h and hydro-extraction time of 1 h to produce the highest yield 63.35%. collagen was classified as type I collagen by amino acid content, electrophoresis patterns and fourier transform infrared (FTIR) spectra. The glass transition of collagen was 67.23o C, showed high thermal stability that can be applied to the cosmetics industry and nutraceutical.

Collagen-the Ultrastructural Element of the Bone Matrix

2018 ◽  
Vol 69 (7) ◽  
pp. 1706-1709
Author(s):  
Nicoleta Dumitru ◽  
Andra Cocolos ◽  
Andra Caragheorgheopol ◽  
Constantin Dumitrache ◽  
Ovidiu Gabriel Bratu ◽  
...  
Keyword(s):  
Type I Collagen ◽  
Bone Microarchitecture ◽  
Complex Structure ◽  
Bone Matrix ◽  
Organic Matrix ◽  
Bone Diseases ◽  
Bone Collagen ◽  
Type I ◽  
New Therapeutic Approaches ◽  
And Function

There is an increased interest and more studies highlight the fact that bone strength depends not only on bone tissue quantity, but also on its quality, which is characterized by the geometry and shape of bones, trabecular bone microarchitecture, mineral content, organic matrix and bone turnover. Fibrillar type I collagen is the major organic component of bone matrix, providing form and a stable template for mineralization. The biomedical importance of collagen as a biomaterial for medical and cosmetic purposes and the improvement of the molecular, cellular biology and analytical technologies, led to increasing interest in establishing the structure of this protein and in setting of the relationships between sequence, structure, and function. Bone collagen crosslinking chemistry and its molecular packing structure are considered to be distinct features. This unique post-translational modifications provide to the fibrillar collagen matrices properties such as tensile strength and viscoelasticity. Understanding the complex structure of bone type I collagen as well as the dynamic nature of bone tissues will help to manage new therapeutic approaches to bone diseases.

Comparative Analysis of the Proteomic Profile of Cattle Hides that Produce Loose and Tight Leather using In-Gel Tryptic Digestion followed by LC-MS/MS

2020 ◽  
Vol 115 (11) ◽  
pp. 399-408
Author(s):  
Catherine Maidment ◽  
Meekyung Ahn ◽  
Rafea Naffa ◽  
Trevor Loo ◽  
Gillian Norris
Keyword(s):  
Type I Collagen ◽  
Raw Material ◽  
Type I ◽  
Collagen Structure ◽  
Proteomic Profile ◽  
Collagen Network ◽  
Collagen Concentration ◽  
Different Types ◽  
Molecular Components ◽  
First Time

Looseness is a defect found in leather that reduces its quality by causing a wrinkly appearance in the finished product, resulting in a reduction in its value. Earlier studies on loose leather using microscopy and Raman spectroscopy reported a change in the collagen structure of loose leather. In this study, proteomics was used to investigate the possible molecular causes of looseness in the raw material, the first time such a study has been carried out. Proteins extracted from two regions of raw hide using two different methods were analysed; those taken from the distal axilla, an area prone to looseness, and those taken from the backbone which is less prone to looseness. Analyses using 1DE-LC-MS/MS showed that although the overall collagen concentration was similar in both areas of the hide, the distribution of the different types of collagen differed.  Specifically, concentrations of type I collagen, and the collagen-associated proteoglycan decorin were lower in samples taken from the distal axilla, symptomatic of a collagen network with excess space seen for these samples using confocal microscopy. This study suggests a possible link between the molecular components of raw cattle hide and looseness and more importantly between the molecular components of skin and skin defects. There is therefore potential to develop biomarkers for looseness which will enable early preventative action.

Radioimmunoassay for the pyridinoline cross-linked carboxy-terminal telopeptide of type I collagen: a new serum marker of bone collagen degradation

1993 ◽  
Vol 39 (4) ◽  
pp. 635-640 ◽  
Author(s):  
J Risteli ◽  
I Elomaa ◽  
S Niemi ◽  
A Novamo ◽  
L Risteli
Keyword(s):  
Type I Collagen ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Bone Collagen ◽  
Collagen Molecule ◽  
Type I ◽  
Serum Samples ◽  
Amino Terminal ◽  
Wide Range ◽  
Carboxy Terminal

Abstract We developed a radioimmunoassay (RIA) for the carboxy-terminal telopeptides of type I collagen (ICTP), cross-linked with the helical domain of another type I collagen molecule, after isolation from human femoral bone. The cross-linked peptide was liberated by digesting insoluble, denatured bone collagen either with bacterial collagenase or with trypsin, and purified by two successive reversed-phase separations on HPLC, with monitoring of pyridinoline-specific fluorescence. The purity of the peptide was verified by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, and its origin in the type I collagen fibers was determined by amino-terminal amino acid sequencing. Polyclonal antibodies and a separation reagent containing second antibody and polyethylene glycol are used in the RIA. An immunologically identical, somewhat larger antigen is present in human serum; its concentration increases in multiple myeloma and in rheumatoid arthritis. The ICTP antigen seems to be cleared from the circulation by the kidneys, because glomerular filtration rates that are two-thirds of normal or less are associated with increased circulating ICTP concentrations. The CVs of the method are between 3% and 8% for a wide range of concentrations. The analysis of 40 serum samples can be completed in 4 h.

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 Effects of extraction conditions on characterization of gelatin from water buffalo (Bubalus bubalis) skin

Food Research ◽  
2020 ◽  
Vol 4 (S6) ◽  
pp. 124-131
Author(s):  
Rabiatul Amirah R. ◽  
Ellya Hazreera A.J. ◽  
Nor Qhairul Izzreen M.N. ◽  
Rozzamri A. ◽  
Umi Hartina M.R.
Keyword(s):  
Water Buffalo ◽  
Extraction Process ◽  
Bubalus Bubalis ◽  
Ash Content ◽  
Raw Material ◽  
Extraction Time ◽  
Foaming Properties ◽  
Alternative Source ◽  
Significant Difference ◽  
Pre Treatment

The study aimed to determine the characteristics of gelatin from water buffalo (Bubalus bubalis) skin pre-treated with NaOH and Ca(OH)2 at different concentrations (0.3 M, 0.5 M and 0.7 M) and extracted at 65˚C for 6 hrs and 24 hrs respectively. The gelatin obtained was evaluated for its moisture, protein and ash content, UV-vis absorption value, colour, emulsifying and foaming properties. The highest yield (20.25%) was observed for gelatin extracted by 0.5 M NaOH at 24 hrs extraction time. For alkaline pre-treatment, it was found that NaOH was more efficient than Ca(OH)2 in terms of preparing the skin for subsequent extraction process. The protein content of the extracted gelatin samples was in the range of 71.76% - 87.83%, showing that the varying processing conditions are sufficiently to recover protein from the raw material. Ash content for all samples was in agreement with USDA standard, which was below than 3%. The extracted gelatin had varying pH values which were from 5.47 to 7.02. The gelatin was colourless with ‘L’ values of more than 80, except for 0.7 M Ca(OH)2 at 24 hrs which showed slightly darker properties. The intensity of the UV-vis absorption spectrum showed that a high absorption peak was observed at 6 hrs of extraction time (230 – 250 nm) compared to 24 hrs extraction time. Emulsifying properties of buffalo gelatin increased with increasing concentrations of alkaline except for 0.7 M NaOH and 0.7 M Ca(OH)2 for both extraction time. Meanwhile, foam expansion of the gelatin extracted from the different extraction conditions was observed to have a significant difference (p < 0.05) for all samples. To our knowledge, buffalo skin has the potential to be an alternative source of gelatin in the diversified industrial application by modifying the extraction conditions in order to produce gelatin with desired quality.

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 The Effect of Different pH in Extraction Process Against Physicochemical Properties of Refined Iota Carrageenan from Eucheuma spinosum Seaweed.

2020 ◽  
Vol 8 (1) ◽  
pp. 14
Author(s):  
Miftakhul Ulumiah ◽  
Mochammad Amin Alamsjah ◽  
Kustiawan Tri Pursetyo
Keyword(s):  
Acetic Acid ◽  
Ph Value ◽  
Chemical Properties ◽  
Extraction Process ◽  
Fish Bone ◽  
Weak Acid ◽  
Gel Strength ◽  
Partial Hydrolysis ◽  
Single Chain ◽  
Randomized Design

Gelatin is a simple protein obtained from the partial hydrolysis of collagen from the skin, bones, joints and connective tissue of animals. One potential material for the manufacture of gelatin is fish bone milkfish (Chanos chanos). Gelatin derived from fish bones with acid process is able to change the triple helix collagen fibers into a single chain, whereas the solvent base only produce double chain. Demineralization of bone or fish skin should use a weak acid is acetic acid, because when using strong acids will produce a strong scent and color gelatin becomes dark. This study aims to determine the effect of the use of acetic acid to the production of fish bone gelatin and the concentration of acetic acid is necessary to produce gelatin with physical and chemical properties of the best. This study uses a Completely Randomized Design (CRD) with four treatments and five replications. The treatments used in this study is the concentration of acetic acid 2%, 4%, 6% and 8%. Based on the research, it was found that the acetic acid solvent effect on the value of the yield and gel strength, but has no effect on the pH value and viscosity. Acetic acid concentration 8% give 4.102% yield value; pH value (acidity) 4.98; 134.313 bloom gel strength and viscosity of 3.6 cP. FTIR analysis results indicate that the fish bone gelatin produced from this research have the same functional group with commercial gelatin.

scholarly journals Effect Collagen Concentration Tilapia Scales on the Quality of Burn Ointment

2021 ◽  
pp. 87-95
Author(s):  
Muhammad Firham Ramadhan ◽  
Junianto . ◽  
Rusky Intan Pratama ◽  
Iis Rostini
Keyword(s):  
Type I Collagen ◽  
Ph Value ◽  
Quality Standard ◽  
National Standard ◽  
Control Treatment ◽  
Type I ◽  
Fish Scale ◽  
Collagen Concentration ◽  
Biomedical Material ◽  
Skin Collagen

Collagen is one of the main connective tissue animal proteins and has been widely used as a biomedical material. Collagen is divided into XIX types. Type I collagen, among others, is obtained from bone, scales and skin. Collagen derived from type I can repair tissue or accelerate tissue regeneration to heal burns. The purpose of this research was to determine the addition of fish scale collagen extract to the characteristics of the burn ointment preparation in accordance with the Indonesian National Standard (SNI) and the best quality. The method used in this research is an experimental method of Completely Randomized Design (CRD) consisting of 4 collagen addition treatments: 0%, 2%, 4% and 6% repeated 5 times. Parameters in this method include physical-chemical parameters (pH, spreadability, shelf life and homogeneity) and organoleptic parameters (appearance, aroma, texture and color). Bayes test results, the concentration of the addition of tilapia scale collagen in the ointment preparation of 4% resulted in a value close to the control treatment. The addition of 4% collagen was the best treatment compared to 2% and 6% with a pH value of 6.12, dispersion of 3.22 cm, safe ointment preparation did not change at all during 28 days of storage. Based on the results of the organoleptic test parameters, the ointment at this concentration had a homogeneous appearance, slightly yellowish white color, a distinctive smell of collagen and a semi-solid texture, this was in accordance with the quality standard of the ointment and had the best quality characteristics.

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