Isolation and characterization of acid-soluble collagen from the scales of marine fishes from Japan and Vietnam

2014 ◽  
Vol 149 ◽  
pp. 264-270 ◽  
Author(s):  
Le Thi Minh Thuy ◽  
Emiko Okazaki ◽  
Kazufumi Osako
Food Research ◽  
2020 ◽  
Vol 5 (3) ◽  
Author(s):  
T.Y. Ong ◽  
M.I. Shaik ◽  
N.M. Sarbon

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.


2021 ◽  
Author(s):  
Budjav Jadamba ◽  
Enerelt Urnukhsaikhan ◽  
Anujin Gantulga ◽  
Sugar Lkhagvachuluun ◽  
Enkhsaikhan Lkhagvasuren ◽  
...  

2013 ◽  
Vol 38 (2) ◽  
pp. 236-247 ◽  
Author(s):  
Chang-Feng Chi ◽  
Bin Wang ◽  
Zhong-Rui Li ◽  
Hong-Yu Luo ◽  
Guo-Fang Ding ◽  
...  

2004 ◽  
Vol 85 (2) ◽  
pp. 495-505 ◽  
Author(s):  
Christina Mork ◽  
Paul Hershberger ◽  
Richard Kocan ◽  
William Batts ◽  
James Winton

The initial characterization of a rhabdovirus isolated from a single, asymptomatic starry flounder (Platichthys stellatus) collected during a viral survey of marine fishes from the northern portion of Puget Sound, Washington, USA, is reported. Virions were bullet-shaped and approximately 100 nm long and 50 nm wide, contained a lipid envelope, remained stable for at least 14 days at temperatures ranging from −80 to 5 °C and grew optimally at 15 °C in cultures of epithelioma papulosum cyprini (EPC) cells. The cytopathic effect on EPC cell monolayers was characterized by raised foci containing rounded masses of cells. Pyknotic and dark-staining nuclei that also showed signs of karyorrhexis were observed following haematoxylin and eosin, May–Grunwald Giemsa and acridine orange staining. PAGE of the structural proteins and PCR assays using primers specific for other known fish rhabdoviruses, including Infectious hematopoietic necrosis virus, Viral hemorrhagic septicemia virus, Spring viremia of carp virus, and Hirame rhabdovirus, indicated that the new virus, tentatively termed starry flounder rhabdovirus (SFRV), was previously undescribed in marine fishes from this region. In addition, sequence analysis of 2678 nt of the amino portion of the viral polymerase gene indicated that SFRV was genetically distinct from other members of the family Rhabdoviridae for which sequence data are available. Detection of this virus during a limited viral survey of wild fishes emphasizes the void of knowledge regarding the diversity of viruses that naturally infect marine fish species in the North Pacific Ocean.


2011 ◽  
Vol 236-238 ◽  
pp. 2926-2934 ◽  
Author(s):  
Li Li Chen ◽  
Li Zhao ◽  
Hua Liu ◽  
Run Feng Wu

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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