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.

scholarly journals Biocompatibility of Novel Type I Collagen Purified from Tilapia Fish Scale: An In Vitro Comparative Study

2015 ◽  
Vol 2015 ◽  
pp. 1-8 ◽  
Author(s):  
Jia Tang ◽  
Takashi Saito
Keyword(s):  
Cellular Proliferation ◽  
Type I Collagen ◽  
Type I ◽  
Fish Scale ◽  
Porcine Skin ◽  
Religious Issues ◽  
Skin Collagen ◽  
Potential Alternative ◽  
Tilapia Scale

Type I collagen (COL-1) is the prevailing component of the extracellular matrix in a number of tissues including skin, ligament, cartilage, bone, and dentin. It is the most widely used tissue-derived natural polymer. Currently, mammalian animals, including pig, cow, and rat, are the three major sources for purification of COL-1. To reduce the risk of zoonotic infectious diseases transmission, minimize the possibility of immunogenic reaction, and avoid problems related to religious issues, exploration of new sources (other than mammalian animals) for the purification of type I collagen is highly desirable. Hence, the purpose of the current study was to investigate the in vitro responses of MDPC-23 to type I collagen isolated from tilapia scale in terms of cellular proliferation, differentiation, and mineralization. The results suggested that tilapia scale collagen exhibited comparable biocompatibility to porcine skin collagen, indicating it might be a potential alternative to type I collagen from mammals in the application for tissue regeneration in oral-maxillofacial area.

Assembly of Type I Collagen on PVA Film Induced by Glutaraldehyde Vapor

2011 ◽  
Vol 284-286 ◽  
pp. 1794-1799 ◽  
Author(s):  
Yu Lu Wang ◽  
Xue Pin Liao ◽  
Bi Shi
Keyword(s):  
Network Structure ◽  
Type I Collagen ◽  
Collagen Fibers ◽  
Type I ◽  
Collagen Concentration ◽  
Collagen Molecules ◽  
Induced Reaction ◽  
Calf Skin

Type I collagen was isolated from calf skin and its assembly on PVA film induced by glutaraldehyde vapor was investigated. It was found that the collagen molecules were firstly orientationally assembled into collagen fibers under the inducement of glutaraldehyde vapor. Then the collagen fibers could be further aggregated into novel network structure in proper conditions of the induced reaction. The morphology of the assembled collagen fibers was depended on induced time and concentration of collagen. The network arrangement could be obtained after being induced for 72h when collagen concentration was 2.5mg/ml. At higher concentration of collagen (5 mg/ml), the collagen fibers with larger dimension were obtained, but the growth of fibers was almost in one direction.

Maturation process and characterization of a novel thermostable and halotolerant subtilisin-like protease with high collagenolytic but low gelatinolytic activity

2021 ◽  
Author(s):  
Kui Zhang ◽  
Qianqian Huang ◽  
Yu Li ◽  
Lanhua Liu ◽  
Xiao-Feng Tang ◽  
...  
Keyword(s):  
High Temperatures ◽  
Type I Collagen ◽  
Elevated Temperatures ◽  
Catalytic Domain ◽  
Ion Pairs ◽  
Gelatinolytic Activity ◽  
Type I ◽  
Fish Scale ◽  
Collagenolytic Proteases ◽  
Collagenolytic Protease

Enzymatic degradation of collagen is of great industrial and environmental significance; however, little is known about thermophile-derived collagenolytic proteases. Here, we report a novel collagenolytic protease (TSS) from thermophilic Brevibacillus sp. WF146. The TSS precursor comprises a signal peptide, an N-terminal propeptide, a subtilisin-like catalytic domain, a β-jelly roll (βJR) domain, and a prepeptidase C-terminal (PPC) domain. The maturation of TSS involves a stepwise autoprocessing of the N-terminal propeptide and the PPC domain, and the βJR rather than the PPC domain is necessary for correct folding of the enzyme. Purified mature TSS displayed optimal activity at 70°C and pH 9.0, a half-life of 1.5 h at 75°C, and an increased thermostability with rising salinity up to 4 M. TSS possesses an increased number of surface acidic residues and ion pairs, as well as four Ca 2+ -binding sites, which contribute to its high thermostability and halotolerance. At high temperatures, TSS exhibited high activity toward insoluble type I collagen and azocoll, but showed a low gelatinolytic activity, with a strong preference for Arg and Gly at the P1 and P1’ positions, respectively. Both the βJR and PPC domains could bind but not swell collagen, and thus facilitate TSS-mediated collagenolysis via improving the accessibility of the enzyme to the substrate. Additionally, TSS has the ability to efficiently degrade fish scale collagen at high temperatures. IMPORTANCE Proteolytic degradation of collagen at high temperatures has the advantages of increasing degradation efficiency and minimizing the risk of microbial contamination. Reports on thermostable collagenolytic proteases are limited, and their maturation and catalytic mechanisms remain to be elucidated. Our results demonstrate that the thermophile-derived TSS matures in an autocatalytic manner, and represents one of the most thermostable collagenolytic proteases reported so far. At elevated temperatures, TSS prefers hydrolyzing insoluble heat-denatured collagen rather than gelatin, providing new insight into the mechanism of collagen degradation by thermostable collagenolytic proteases. Moreover, TSS has the potential to be used in recycling collagen-rich wastes such as fish scales.

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.

scholarly journals Measurement of serum carboxyterminal cross-linked telopeptide of type I collagen concentration in dogs with osteosarcoma

2008 ◽  
Vol 69 (11) ◽  
pp. 1481-1486 ◽  
Author(s):  
John G. Hintermeister ◽  
Pamela D. Jones ◽  
Walter E. Hoffmann ◽  
Arthur M. Siegel ◽  
Nikolaos G. Dervisis ◽  
...  
Keyword(s):  
Type I Collagen ◽  
Type I ◽  
Collagen Concentration

Evaluation of plasma carboxy-terminal cross-linking telopeptide of type I collagen concentration in horses

2004 ◽  
Vol 65 (1) ◽  
pp. 104-109 ◽  
Author(s):  
Bianca Carstanjen ◽  
Nicholas R. Hoyle ◽  
Annick Gabriel ◽  
Olaf Hars ◽  
Charlotte Sandersen ◽  
...  
Keyword(s):  
Type I Collagen ◽  
Cross Linking ◽  
Type I ◽  
Collagen Concentration ◽  
Carboxy Terminal

EFFECT OF COLLAGEN ON THE MORPHOLOGY AND STRUCTURE OF CALCIUM PHOSPHATE NANOPARTICLES

2014 ◽  
Vol 26 (05) ◽  
pp. 1450061
Author(s):  
Hoda Salemi ◽  
Aliasghar Behnamghader ◽  
Mohamadreza Baghaban Eslaminejad ◽  
Mohammad Ataei
Keyword(s):  
Calcium Phosphate ◽  
Electrostatic Interactions ◽  
Type I Collagen ◽  
Bone Matrix ◽  
Control Sample ◽  
Molar Ratio ◽  
Type I ◽  
Sem Images ◽  
Collagen Concentration ◽  
Calcium Phosphate Nanoparticles

Collagen and noncollagenous proteins have an important role in the formation of mineral constituent of bone matrix. In this research, the morphology and phase characteristics of calcium phosphate nanoparticles in presence of collagen were investigated. The synthesis reaction was initiated by mixing H 3 PO 4 as phosphorous source and CaCl 2 as calcium source and type I collagen. Collagen concentration in suspension and Ca to P ratio was 1% and 1.67, respectively. The samples (with collagen and without collagen), were heat treated at 600°C and characterized by X-Ray diffraction (XRD), Fourier transformation infrared (FTIR) and scanning electron microscopy (SEM). More smaller and flake-like shape particles were observed in the SEM images of sample synthesized in the presence of collagen compared to the control sample which was constituted of larger granular particles. The XRD results revealed that the synthesized mineral powders with collagen were composed of hydroxyapatite and octacalcium phosphate. P – O and OH characteristic peaks were identified in FTIR spectra. In hybrid sample, the shift of amides band, revealed the electrostatic interactions between calcium phosphate ions and carboxyl or amino groups of collagen fibrils. The Ca to P molar ratio for sample with collagen was 1.9. It was found that the sample synthesized in the presence of collagen has a similar microstructure to natural bone.

Curcumin loaded nano graphene oxide reinforced fish scale collagen – a 3D scaffold biomaterial for wound healing applications

RSC Advances ◽  
2015 ◽  
Vol 5 (119) ◽  
pp. 98653-98665 ◽  
Author(s):  
Tapas Mitra ◽  
Piyali Jana Manna ◽  
S. T. K. Raja ◽  
A. Gnanamani ◽  
P. P. Kundu
Keyword(s):  
Tissue Engineering ◽  
Wound Healing ◽  
Graphene Oxide ◽  
Type I Collagen ◽  
Type I ◽  
Fish Scale ◽  
3D Scaffold ◽  
Engineering Research ◽  
Nano Graphene ◽  
Tissue Engineering Research

We prepare a highly stabilized nano graphene oxide functionalized with type I collagen to make a 3D scaffold as a novel platform for better tissue engineering research..

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 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.

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