scholarly journals Isolation and characterization of acid and pepsin soluble collagen extracted from sharpnose stingray (Dasyatis zugei) skin

Food Research ◽  
2020 ◽  
Vol 5 (3) ◽  
Author(s):  
T.Y. Ong ◽  
M.I. Shaik ◽  
N.M. Sarbon
Keyword(s):  
Helical Structure ◽  
Alternative Source ◽  
Soluble Collagen ◽  
Isolation And Characterization ◽  
Fibrous Network ◽  
Acid Soluble Collagen ◽  
Maximum Temperatures ◽  
Surface Morphologies ◽  
Pepsin Soluble Collagen

This study aimed to isolate and characterize the acid soluble collagen (ASC) and pepsin soluble collagen (PSC) from the skin of the sharpnose stingray (Dasyatis zugei). Isolated ASC and PSC were subjected to chemical and physical characterizations. The yield of PSC (34.84±1.26%) was significantly higher than that of ASC (20.48±4.41%) (p<0.05). There were no significant differences between ASC and PSC in terms of chemical composition (p>0.05). Both ASC and PSC were thermally stable at high temperatures, with denaturation temperatures of 24.1°C and 25.2°C, respectively, and maximum temperatures of 31.94±0.13°C and 31.79±0.23°C, respectively. Fourier transform infrared (FTIR) investigations showed the presence of triple helical structure with strong hydrogen bonding in both ASC and PSC. Meanwhile, both collagens were highly solubilized at acidic pH but at different optimal pH. The surface morphologies of ASC and PSC were loose and possessed slender, less uniform and irregular fibrous network structures with large and irregular pores observed between the fibrils. This finding showed that the alternative source of marine collagen possesses good physicochemical properties which highly potential for nutraceutical, pharmaceutical or cosmeceutical application.

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 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

Isolation and Characterization of Acid-Soluble Collagen from the Skin of Amiurus nebulosus

2013 ◽  
Vol 781-784 ◽  
pp. 1728-1735 ◽  
Author(s):  
Li Li Chen ◽  
Li Zhao ◽  
Mei Lan Yuan ◽  
Wei Su ◽  
Hua Liu
Keyword(s):  
Type I Collagen ◽  
Raw Materials ◽  
Type I ◽  
Alternative Source ◽  
Shrinkage Temperature ◽  
Soluble Collagen ◽  
Isolation And Characterization ◽  
Acid Soluble Collagen ◽  
Commercial Applications ◽  
Effective Use

During fish processing, a large amount of waste, of the original raw materials is generated, such as skin, bone, scale, viscera and head. These useful resources have been mainly used as feedstuff or fertiliser with low value. To make more effective use of underutilized resources, collagen was isolated from the skin of Amiurus nebulosus using acetic acid and characterized for their potential usage in commercial applications. The yield of acid-soluble collagen (ASC) was 62.05% while the maximum absorbance of ASC was at 234 nm. Amino acid composition and SDS - PAGE suggested that the collagen is possibly possessive of type I collagen. Moreover, FTIR investigations showed the existence of helical arrangements of collagen where the denaturation temperature (Td) and shrinkage temperature (Ts) were 29.8°C and 65.12°C, respectively. There is a possibility that ASC could be utilized as an alternative source of collagen for food, cosmetic, biomedical and pharmaceutical purposes.

scholarly journals ISOLASI DAN KARAKTERISASI KOLAGEN DARI KULIT IKAN PATIN (Pangasius sp.)

2018 ◽  
Vol 8 (1) ◽  
pp. 8 ◽  
Author(s):  
Pipih Suptijah ◽  
Dini Indriani ◽  
Supriyono Eko Wardoyo
Keyword(s):  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Ph Value ◽  
Helical Structure ◽  
Color Analysis ◽  
Alternative Source ◽  
Isolation And Characterization ◽  
Naoh Solution

Isolation and Characterization of Collagen from the Skin of Catfish (Pangasius sp.)           Skin of catfish is one of aquatic by-products which could be used as an alternative source of collagen. This research is aimed to isolate and characterize collagen from skin of catfish. Methods of  isolation of collagen included three stages, the first was deproteinization using NaOH solution with concentration of 0.05 M; 0.10 M; 0.15 M; 0.20 M for 12 hours, the second was soaking in CH3COOH solution with concentration of 0.05 M; 0.10 M; 0.15 M; and 0.20 M for 2 hours, and the third was extraction in water at a temperature of 40 0C for 2 hours; characterization of collagen was included chemical and physical properties. The results showed that the best extraction method ofcollagen from skin of catfish was soaking the skin in 0.05 M NaOH solution for 12 hours and soaking the skin in 0.05 M acetic acid for 2 hours. Extraction yields of collagen was 12.15%. Chemical characteristics included proximate and amino acid composition. Proximate value of collagen consisted of moisture was 6.55%, ash 1.80%,  protein 64.74% and fat 8.85%.  The major amino acid composition of collagen were glycine, proline, alanine, arginine and glutamate. Physical characteristics of collagen resulted from FTIR analysis showed amide A, amide B, amide I, amide II and amide III, triple helical structure of the amide I and amide III indicates that the compound produced was collagen; color analysis was 66.39%; thermal analysis showed a melting temperature peak was 154.47 0C and pH value was 5.34.Keywords : Catfish, isolation, characterization, collagen, skin ABSTRAK          Kulit ikan patin merupakan salah satu limbah hasil perairan yang dapat digunakan sebagai sumber alternatif kolagen. Penelitian ini bertujuan untuk mengisolasi dan karakterisasi kolagen yang diperoleh dari kulit ikan patin. Isolasi kolagen yang dilakukan meliputi tiga tahap, yaitu tahap pertama adalah proses deproteinisasi menggunakan larutan NaOH dengan konsentrasi, yaitu 0,05 M; 0,10 M; 0,15 M; 0,20 M dan lama waktu perendaman selama 12 jam; tahap kedua, yaitu perendaman dalam larutan CH3COOH dengan empat konsentrasi CH3COOH yaitu 0,05 M; 0,10 M; 0,15 M; dan 0,20 M dan lama waktu perendaman selama 2 jam; dan tahap ketiga, yaitu ekstraksi dengan air pada suhu 40 0C selama 2 jam; serta karakterisasi kolagen yang dilakukan, meliputi sifat kimia dan fisik. Hasil penelitian menunjukkan bahwa metode ekstraksi kolagen dari kulit ikan patin  terbaik diperoleh melalui proses perendaman kulit dalam larutan NaOH 0,05 M selama 12 jam dan  perendaman kulit dalam asam asetat 0,05 M selama 2 jam.  Rendemen serbuk kolagen yang dihasilkan sebesar 12,15 %. Karakteristik kimia meliputi proksimat dan komposisi asam amino. Nilai proksimat kolagen terdiri dari kadar air 6,55 %,  abu 1,80 %, protein 64,74 % dan lemak 8,85 %. Komposisi asam amino yang dominan pada kolagen adalah glisina, prolina, alanina, arginina dan glutamat. Karakteristik fisik kolagen yang dihasilkan adalah analisis FTIR menunjukkan adanya gugus amida A, amida B, amida I, amida II dan amida III, struktur triple heliks pada amida I dan amida III mengindikasikan bahwa senyawa yang dihasilkan adalah kolagen; analisis warna  yaitu 66,39 %; analisis termal yang menunjukkan suhu puncak pelelehan adalah 154,47 0C dan nilai pH kolagen yaitu 5,34. Kata kunci : Ikan patin, isolasi, karakterisasi, kolagen, kulit 

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