Extraction and characterization of collagen from rabbit skin: partial characterization (original) (raw)
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International Journal of Applied Pharmaceutics, 2018
The aim of this study is to produce collagen through the extraction and isolation of porcine skin. Methods: Collagen from porcine skin (Sus scrofa domesticus) was isolated, purified, and characterized. Major amino acid content of collagen (glycine, proline, and hydroxyproline) was determined. Samples were extracted with 0.5 N acetic acid and precipitated with 0.9 M NaCl. Characterization tests included those to determine the organoleptic content, pH, Fourier-transform infrared analysis, moisture content, ash content, viscosity, and Masson's trichrome staining on collagen tissue. The collagen was further analyzed using high-performance liquid chromatography using C-18 ® column and a fluorescence detector at 265 nm and 320 nm, acetic buffer (pH 4.2)-acetonitrile (55:45) as mobile phase, and optimum flow rate of 0.8 mL/min. Results: Our findings indicated that the best method for isolating collagen was with 0.1 M NaOH expressed by average contents of glycine, proline, and hydroxyproline in collagen which were 33.663±0.215%, 12.333±0.128%, and 11.303±0.354%, respectively. Conclusion: Porcine collagen has been successfully obtained with this method.
YMER Digital, 2022
Collagen is a fibrillar protein that forms the connective and conjunctive tissues in humans, essentially bones, joints and skin. Collagen is the mostly available in majority of the living things suitable for its connective function in biological structures. Due to its large quantity, potency and its direct proportionality with skin aging, collagen has obtained obvious attention in cosmetic industry. It is recognized that collagen fibers are prone for damage with time, loses its thickness and potency which is abundantly related to skin aging criteria. The utilization of nutraceuticals such as collagen specifically for skincare is in rise, but complete regulations are deficient on its quality, efficacy and absorption. There are numerous possible health uses that nutraceuticals supplements can offer. However, researchers have not completely studied the assumed health benefits. As with any supplements, the Food and Drug Administration (FDA) did not confirm the allegations that a cosmeti...
Amino Acids Sequence Analysis on Collagen
Bulletin USAMV-CN, 2007
Staring from available information about amino acids properties and sequences on collagen type I chains, the aims of the study were to identify the principal property component and to analyze the similarities within and between collagens on five species. The principal component analysis applied on twentyfour amino acids properties revealed that the hydrophobic or hydrophilic character measured by Wealling et al. is more stable comparing with the other investigated properties. Similarity analysis identified similar and dissimilar within and between studied species from the viewpoint of amino acids sequences on collagen type I alpha 1 and 2 chains.
Identification and Computational Analysis of Chicken Alpha-1 Collagen Sequences
International Journal of Scientific & Engineering Research, 2015
Collagen is a protein that is found in cartilage, bone and other tissues in animals and humans. People utilize collagen from chicken for medicine. It is used to treat joint pain associated with many types of arthritis and surgery, with back pain, neck pain, and pain subsequent injury. So far, 26 genetically distinct collagen types have been described. However, there is not sufficient information to know if chicken collagen is safe or what the side effects might be. Other collagen products, such as bovine collagen and gelatin, have caused allergic reactions whereas chicken collagen has low amount of allergic reactions. It is recently found that collagen alpha-1 is involved in osteogenesis imperfecta phenotype in cattle, but there is no such type of information in case of chicken. So, attempting to figure out information about their structural features chicken alpha-1 collagen sequences are carried out and analyzed. This investigation reports a comparative analysis and characterization of the alpha-1 chain of chicken collagen sequences using different computational tools. Amino acid composition, physico-chemical, secondary structural, functional and phylogenetic classification were done, based on which, Alpha-1 (XIV) collagen, Collagen alpha-1(XIV) chain precursor and Collagen type XII alpha-1, which belong to the Fibril Associated Collagens with Interrupted Triple helices (FACIT) collagen family, can be recognized as potential players in diseased conditions, because of certain unusual properties such as very high aliphatic index, low percentage of Glycine and Proline residues and their proximity in evolutionary history. These collagen molecules might be play crucial role in cosmetics, foods on top of in medical industry.
Amino Acids Sequences Analysis on Collagen
2007
Staring from available information about amino acids properties and sequences on collagen type I chains, the aims of the study were to identify the principal property component and to analyze the similarities within and between collagens on five species. The principal component analysis applied on twentyfour amino acids properties revealed that the hydrophobic or hydrophilic character measured by Wealling et al. is more stable comparing with the other investigated properties. Similarity analysis identified similar and dissimilar within and between studied species from the viewpoint of amino acids sequences on collagen type I alpha 1 and 2 chains.
Collagen Structure, Synthesis, and Its Applications: A Systematic Review
Cureus
Resorbable collagen has been utilized to treat wounds, close graft, and tooth extraction sites, and enhance recovery. Collagen-based membranes are also used as barriers in periodontal and implant therapy to limit epithelial migration and allow cells with the regenerative capacity to fill the problem area. This systematic review was carried out to analyze the studies focusing on collagen structure, synthesis, and its applications. A detailed and extensive search was performed with the help of the keywords "collagen structure", "collagen synthesis" and "collagen applications". There was extensive literature search in reliable and authentic databases like PubMed, Scopus, Web of Sciences, Ovidsp, and Cochrane library to obtain papers focusing on collagen structure, synthesis, and applications. During the systematic review, data were obtained concerning the following parameters. Type of study, nature of aim of the study, size of the sample in the study, gender and age of the subjects included in the study, prevalence of skin diseases where collagen was used for treatment, dose of collagen used, form in which collagen was used, the origin of collagen used, analysis of different variables, structure, and synthesis of collagen. Twenty-two studies were included in this systematic review. The studies discussed the structure, synthesis, and applications of collagen in treatment. In studies focusing on the application of collagen supplements, most of the study subjects were females (68.3%). The study subjects included both healthy and unhealthy subjects. The study subjects were divided into two categories. One category was the intervention group, while another group was the placebo group. Collagen was administered in hydrolysate form (90%) in some studies, bovine form (2.3%), and porcine form (3.4%) in other studies. Collagen supplementation was found to provide better results in both healthy and unhealthy effects in improving the health of skin, cornea, bone, periodontium, face, etc. It can be concluded that collagen is an integral part of the body. The application of collagen supplements can be pretty effective in maintaining the proper health of several important structures of the body like skin, face, cornea, nails, periodontium, etc. Thus, a detailed study of the molecular structure of collagen and genes associated with each type of collagen is essential for further research and treatment of collagen-associated disorders.
Collagen Extraction from Animal Skin
Biology
Collagen is the most abundant structural protein in animals. It is the major component of skin. It finds uses in cosmetics, medicine, yarn production and packaging. This paper reviews the extraction of collagen from hides of most consumed animals for meat with the focus on literature published since 2000. The different pretreatment and extraction techniques that have been investigated for producing collagen from animal skins are reviewed. Pretreatment by enzymatic, acid or alkaline methods have been used. Extraction by chemical hydrolysis, salt solubilization, enzymatic hydrolysis, ultrasound assisted extraction and other methods are described. Post-extraction purification methods are also explained. This compilation will be useful for anyone wishing to use collagen as a resource and wanting to further improve the extraction and purification methods.
Collagen Sources and Areas of Use
European Journal of Interdisciplinary Studies
Fibrillar collagen type I undenatured represent the major structural component of all organs and connective tissues, which due to low antigenicity and outstanding biocompatibility the possibility of controlling the time of biodegradation by crosslinking, the ease of forming composites with other natural polymers and synthetic, represents one of the most used natural biomaterials . Collagen biomaterials are successfully used in gene therapy for artificial implants. They are used as medical devices, scaffolds for tissue regeneration, supports for drug release. Collagen can be extracted from various sources considering that it is one of the most abundant proteins on earth. It can be extracted from almost every living animal, even including alligators and kangaroos. Nonetheless, common sources of collagen for tissue engineering applications include bovine skin and tendons, porcine skin and rat tail among others. Marine life forms are also a considerable source of collagen, which can be ...
Collagen and Its Modifications-Crucial Aspects with Concern to Its Processing and Analysis
Macromolecular Materials and Engineering, 2017
scaffolds; however, they also make up the key proteins for a range of vital processes at work within the organism. [1] To date, some 30 various types of collagen have been identified. [2] The most abundant collagens consist of so-called fibrilforming collagens (up to 90% of all human collagens) with their characteristic quarter-staggered fibril-array. [3] The most abundant collagens are type I which is present mainly in bone, tendons, skin, dentin, etc., type II mostly in cartilage and type III like in skin. [2] The other minor collagen types are rather organ-specific. Water performs an elemental function in terms of the conservation of the physical properties of collagen. An amount of water at a level of around 20% of the total weight of collagen is necessary for the maintaining of its physical properties. In low hydrated or dehydrated collagen, the polypeptide chains are restricted in their motion; however, with increasing hydration these chains are gradually released. [1] Many connective tissue diseases and defects are associated with poor synthesis or excessive degradation of collagen. The modern tissue engineering approach is to replace the defective site via the implantation of a biocompatible scaffold which serves as a carrier for cell incorporation, proliferation, and growth. Collagen is widely used in the field of clinical medicine in connection with both hard and soft tissue applications. However, certain collagen properties such as poor dimensional stability, poor in vivo mechanical strength, low degree of elasticity, variable nature in terms of enzymatic degradation, crosslinking density, fiber size, trace impurities, and side effects frequently limit both its analysis and application. This review focuses particularly on the processing and modification of collagen type I with respect to its biological and mechanical properties. The processing of collagen into scaffolds is crucial to mimic successfully the extracellular matrices. Moreover, the review suggests several ways in which the most common problems related to the isolation, handling, electrospinning, and crosslinking of collagen can be overcome while maintaining its native character as much as possible. Further, the review provides a summary of the analytical methods available for the physicochemical characterization of collagen with respect to both its molecular and submolecular structure.
Extraction and Characterization of Collagen from Buffalo Skin for Biomedical Applications
Oriental journal of chemistry, 2016
Collagen is widely used for biomedical and pharmaceutical applications due to its excellent biocompatibility, biodegradability and weak antigenicity. However, applicability is limited due to its high cost and probability of disease transmission from the current sources, which are bovine and porcine. In the present study, collagen was extracted from 6 months buffalo skins as alternative save sources. Collagen was characterized by different physico-chemical techniques like ATR-FTIR, Raman, SEM, DSC and amino acids analysis. Proline and hydroxyproline contents of buffalo skin collagen were higher than those of calf skin collagen. Thermal stability of buffalo skin collagen is high with respect to that of calf skin collagen. The obtained buffalo skin collagen shows higher stiffness upon cross-linking with glutaraldehyde. Thus buffalo skin collagen can be used for fabrication of high strength bioactive sponge and sheets for medical applications, like scaffold for tissue engineering, drug delivery and wound dressing system.