scholarly journals Characterization of Acid Soluble Collagen from Redbelly Yellowtail Fusilier Fish Skin (Caesio cuning)

2016 ◽  
Vol 19 (1) ◽  
pp. 79-93
Author(s):  
Ika Astiana ◽  
◽  
Nurjanah Nurjanah ◽  
Tati Nurhayati
Keyword(s):  
Fish Skin ◽  
Soluble Collagen ◽  
Acid Soluble Collagen

scholarly journals Characterization of Acid Soluble Collagen from Redbelly Yellowtail Fusilier Fish Skin (Caesio cuning)

2016 ◽  
Vol 19 (1) ◽  
pp. 79 ◽  
Author(s):  
Ika Astiana ◽  
Nurjanah Nurjanah ◽  
Tati Nurhayati
Keyword(s):  
Molecular Weight ◽  
Acetic Acid ◽  
Raw Material ◽  
Fish Skin ◽  
Soaking Time ◽  
Soluble Collagen ◽  
Acid Soluble Collagen ◽  
Collagen Protein ◽  
Acid Process

<p>Fish skin can be used as raw material for producing collagen. The collagen can be extracted by chemical<br />or combination of chemical and enzymatic processes. Extraction of collagen chemically can do with the<br />acid process that produces acid soluble collagen (ASC). This study aimed to determine the optimum<br />concentration and time of pretreatment and extraction, also to determine the characteristics of the acid<br />soluble collagen from the skin of yellow tail fish. Extraction of collagen done by pretreatment using NaOH at<br />the concentration of 0.05; 0.1; and 0.15 M and extraction using acetic acid at the concentration of 0.3; 0.5; and<br />0.7 M. Pretreatment NaOH with concentration 0.05 M and soaking time of 8 hours is the best combination<br />for eliminating non collagen protein. Combination treatment of acetic acid at the concentration of 0.3 M<br />for 3 days obtained the best solubility. The yield of collagen ASC was 18.4±1.49% (db) and 5.79±0.47%<br />(wb). Amino acid composition that is dominant in the ASC collagen was glycine (25.09±0.003%), alanine<br />(13.71±0.075%), and proline (12.15±0.132%). Collagen from yellow tail fish skin has α1, α2, β and γ<br />protein structure with the molecular weight of 125, 113, 170-181, and 208 KDa. The transition and melting<br />temperatures of collagen were 67.69oC and 144.4oC. The surface structure of collagen by analysis of SEM has<br />fibers on the surface.<br />Keywords: cholesterol, fatty acids, meat tissue, proximate, red snapper (L. argentimaculatus)</p>

scholarly journals The Characterization of Acid Soluble Collagen from Sheep Tail Tendon

2021 ◽  
Author(s):  
Budjav Jadamba ◽  
Enerelt Urnukhsaikhan ◽  
Anujin Gantulga ◽  
Sugar Lkhagvachuluun ◽  
Enkhsaikhan Lkhagvasuren ◽  
...  
Keyword(s):  
Soluble Collagen ◽  
Acid Soluble Collagen ◽  
Tail Tendon

Fabrication and characterization of acid soluble collagen stabilized Pickering emulsions

2020 ◽  
Vol 106 ◽  
pp. 105875 ◽  
Author(s):  
Qiaomei Zhu ◽  
Yanhong Li ◽  
Shuzhi Li ◽  
Wenhang Wang
Keyword(s):  
Pickering Emulsions ◽  
Soluble Collagen ◽  
Acid Soluble Collagen ◽  
Fabrication And Characterization

Characterization of Acid-soluble Collagen from the Skin of Hammerhead Shark (Sphyrna lewini )

2013 ◽  
Vol 38 (2) ◽  
pp. 236-247 ◽  
Author(s):  
Chang-Feng Chi ◽  
Bin Wang ◽  
Zhong-Rui Li ◽  
Hong-Yu Luo ◽  
Guo-Fang Ding ◽  
...  
Keyword(s):  
Sphyrna Lewini ◽  
Hammerhead Shark ◽  
Soluble Collagen ◽  
Acid Soluble Collagen

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.

scholarly journals Characterization of acid soluble collagen (ASC) and pepsin soluble collagen (PSC) extracted from shortfin scad (Decapterus macrosoma) waste

Food Research ◽  
2020 ◽  
Vol 4 (6) ◽  
pp. 2272-2280
Author(s):  
A.W. Sulaiman ◽  
N.M. Sarbon
Keyword(s):  
Chemical Composition ◽  
Protein Concentration ◽  
Food Ingredient ◽  
Soluble Collagen ◽  
Acid Soluble Collagen ◽  
Kjeldahl Method ◽  
Biuret Method ◽  
The Rich ◽  
Pepsin Soluble Collagen

Fish waste management is one of the biggest impacts towards the environment. However, it is one of the rich sources of protein. Therefore, the aim of this study was to isolate and characterize acid soluble collagen (ASC) and pepsin soluble collagen (PSC) from shortfin scad (Decapterus macrosoma) waste, with the yields of ASC (3.35±3.43%) and PSC (0.10±0.13%) respectively. The isolated ASC and PSC from shortfin scad waste were characterized on chemical composition, protein concentration, structural properties by FTIR, solubility and morphology properties compared to the commercial collagen from tilapia (Oreochromis niloticus) scales. In terms of chemical composition, PSC showed better than ASC, since it contains comparatively higher in protein (26.97±1.02%) by Kjeldahl method and protein concentration (2.69±0.47 mg/mL) by biuret method, compared to ASC. The FTIR investigations also certified the existence of spacial triplehelical structures of collagens that are important for collagen backbones. Solubility results showed that both ASC and PSC are high insolubility at acidic pH with the lowest solubilisation point at the range of alkali condition. The morphological analysis of both ASC and PSC were almost similar too, as there were fibrils and porous structure. Therefore, collagen from shortfin scad waste, could be a useful alternative, with the potential to be used in food ingredient, biomedical, pharmaceutical and nutraceuticals industries

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