scholarly journals Extraction of Type I Collagen from Tilapia Scales Using Acetic Acid and Ultrafine Bubbles

Processes ◽  
2021 ◽  
Vol 9 (2) ◽  
pp. 288
Author(s):  
Junko Kuwahara
Keyword(s):  
Carbon Dioxide ◽  
Acetic Acid ◽  
Type I Collagen ◽  
Acetic Acid Solution ◽  
Type I ◽  
Collagen Concentration ◽  
Carbon Dioxide Gas ◽  
Collagen Denaturation ◽  
Sds Page ◽  
Medical Materials

Type I collagen is commonly used in medical materials and cosmetics. While it can be extracted from the skin and bones of mammals, marine collagen has attracted attention recently, since the use of mammalian collagen could result in zoonosis, and products containing mammalian collagen are avoided due to some religious beliefs. Chemical extractions using strong acids and alkalis, thermal extractions, and other nonconventional methods have been used for collagen extraction. However, there are few reports on environmentally friendly methods. Although heat extractions provide higher yields of collagen, they often cause collagen denaturation. Therefore, dilute acetic acid and ultrafine bubbles of oxygen, carbon dioxide, and ozone were used to extract type I collagen from tilapia scales. The extraction performance of the different conditions employed was qualitatively analyzed by SDS-PAGE electrophoresis, and the collagen concentration was quantified using circular dichroism spectroscopy by monitoring the peak intensity at 221 nm, which is specific to the triple helix of type I collagen. Collagen was extracted from tilapia scales with a yield of 1.58% by the aeration of ultrafine bubbles of carbon dioxide gas in a 0.1 M acetic acid solution for 5 h.

scholarly journals Effects of acetic acid on efficiency of collagen extraction from jellyfish \(\textit{Rhopilema hispdium}\) (Vanhöffen, 1888)

2021 ◽  
Vol 21 (1) ◽  
pp. 57-65
Author(s):  
Kha Pham Thi ◽  
Thu Pham The ◽  
Ha Tran Manh ◽  
Thuoc Chu Van ◽  
Hoang Hiep Le Ba
Keyword(s):  
Acetic Acid ◽  
Acid Solution ◽  
Disease Transmission ◽  
Type I Collagen ◽  
High Efficiency ◽  
Acetic Acid Solution ◽  
The Body ◽  
Type I ◽  
Marine Animals ◽  
Promising Alternative

Collagen is an extremely important fibrous protein in the body. It is the main structural material of all tissues: Skin, bones, ligaments, tendons, cartilage. The source of traditional collagen production is mainly from the skin and bones of animals. However, marine animals are currently a promising alternative source of materials with low risk of disease transmission, no religious barriers to consumption, abundant raw materials, and high-efficiency extraction. In present study, the effects of several factors: Acetic acid concentration, the ratio of jellyfish and acetic acid solution (w:v), as well as the time of extraction on efficiency of collagen extraction process from jellyfish (Rhopilema hispidum Vanhoffen, 1888) were investigated. The results showed that the collagen which was extracted from jellyfish in 0.1M acetic acid, with the ratio 1:3 between the jellyfish and acetic acid solution (w:v) in 5-day extraction had high extraction efficiency. Extracted collagen in present study was mainly type I collagen, consisting of 3 polypeptide chains: β chain (~ 250 kDa), α1 chain (~ 40 kDa) and α2 chain (~ 100 kDa).

scholarly journals PENGARUH KONSENTRASI ASAM ASETAT DAN WAKTU EKSTRAKSI TERHADAP MUTU KOLAGEN KULIT NILA HITAMPENGARUH KONSENTRASI ASAM ASETAT DAN WAKTU EKSTRAKSI TERHADAP MUTU KOLAGEN KULIT NILA HITAM

2011 ◽  
Vol 1 (1) ◽  
Author(s):  
Latif Sahubawa ◽  
A.B. Naro Putra
Keyword(s):  
Acetic Acid ◽  
Type I Collagen ◽  
Value Added ◽  
Extraction Time ◽  
Quantitative Composition ◽  
Type I ◽  
Industry Waste ◽  
Sds Page ◽  
Acid Molarity

The objective of the research was studied the effect of  acetic acid concentration and extraction time on the collagen quality of black tilapia leather. Black tilapia leather processed into collagen  as an alternative to increasing value-added of fisheries industry waste. Collagen of black tilapia was extracted by the treatment of acetic acid molarity, each: 0.25 M, 0.50 M, and 0.75 M (A factor) and  extraction time of 16 and 48 hours (B factor). Based on the analysis of variance, is known that the interaction of those treatments (AB) didn’t significantly effect on the yield  (p>0.05). Collagen extraction of tilapia leather with 0.75 M of acetic acid at 16 hours, produces the greatest yield  (5.97%), with denaturation temperature is 35.75oC, and quantitative composition of glisine, alanine, and glutamic amino acids were: 5395.82 ppm (52.99%), 2979.15 ppm (22.08%), and 1684.42 ppm (7.45%). Based on the analysis of SDS-PAGE, is known that the collagen contained were α component and β component, so that collagen of tilapia leather has type I collagen.

scholarly journals Relative rates of biosynthesis of collagen type I, type V and type VI in calf cornea

1991 ◽  
Vol 274 (2) ◽  
pp. 615-617 ◽  
Author(s):  
P Kern ◽  
M Menasche ◽  
L Robert
Keyword(s):  
Type I Collagen ◽  
Collagen Type ◽  
Corneal Stroma ◽  
Collagen Type I ◽  
Type I ◽  
Type Vi Collagen ◽  
Sds Page ◽  
Proline Incorporation ◽  
Type V

The biosynthesis of type I, type V and type VI collagens was studied by incubation of calf corneas in vitro with [3H]proline as a marker. Pepsin-solubilized collagen types were isolated by salt fractionation and quantified by SDS/PAGE. Expressed as proportions of the total hydroxyproline solubilized, corneal stroma comprised 75% type I, 8% type V and 17% type VI collagen. The rates of [3H]proline incorporation, linear up to 24 h for each collagen type, were highest for type VI collagen and lowest for type I collagen. From pulse-chase experiments, the calculated apparent half-lives for types I, V and VI collagens were 36 h, 10 h and 6 h respectively.

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.

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.

Cysteine proteinase activities in the fish pathogenPhilasterides dicentrarchi(Ciliophora: Scuticociliatida)

Parasitology ◽  
2004 ◽  
Vol 128 (5) ◽  
pp. 541-548 ◽  
Author(s):  
A. PARAMÁ ◽  
R. IGLESIAS ◽  
M. F. ÁLVAREZ ◽  
J. LEIRO ◽  
F. M. UBEIRA ◽  
...  
Keyword(s):  
Crude Extract ◽  
Type I Collagen ◽  
Cysteine Proteinase ◽  
Cysteine Proteases ◽  
Cysteine Protease Inhibitor ◽  
Type I ◽  
Molecular Weights ◽  
Reducing Conditions ◽  
Sds Page

This study investigated protease activities in a crude extract andin vitroexcretion/secretion (E/S) products ofPhilasterides dicentrarchi, a ciliate fish parasite causing economically significant losses in aquaculture. Gelatin/SDS–PAGE analysis (pH 4, reducing conditions) detected 7 bands with gelatinolytic activity (approximate molecular weights 30–63 kDa) in the crude extract. The banding pattern observed in analysis of E/S products was practically identical, except for 1 low-molecular-weight band detected in the crude extract but not in the E/S products. In assays with synthetic peptidep-nitroanilide substrates, the crude extract hydrolysed substrates characteristic of cysteine proteases, namely Z-Arg-Arg pNA, Bz-Phe-Val-Arg pNA and Z-Phe-Arg pNA. These activities were strongly inhibited by the cysteine protease inhibitor E-64 and by Ac-Leu-Val-Lys aldehyde, a potent inhibitor of cysteine proteases of the cathepsin B protease subfamily. The proteases present in the crude extract degraded both type-I collagen and haemoglobinin vitro, consistent with roles in tissue invasion and nutrition respectively. Again, E-64 completely (collagen) or markedly (haemoglobin) inhibited this degradation. Finally, the histolytic activity of the ciliate in turbot fibroblast monolayers was strongly reduced in the presence of E-64, confirming the importance of secreted cysteine proteinases in the biology ofPhilasterides dicentrarchi.

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.

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.

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