Triple helical structure of acid-soluble collagen derived from Nile tilapia skin as affected by extraction temperature

2016 ◽  
Vol 96 (11) ◽  
pp. 3795-3800 ◽  
Author(s):  
Mantaka Thuanthong ◽  
Nualpun Sirinupong ◽  
Wirote Youravong
Keyword(s):  
Nile Tilapia ◽  
Helical Structure ◽  
Extraction Temperature ◽  
Soluble Collagen ◽  
Acid Soluble Collagen ◽  
Triple Helical Structure

scholarly journals The effect of ultraviolet irradiation on acid-soluble collagen

1967 ◽  
Vol 105 (3) ◽  
pp. 965-969 ◽  
Author(s):  
R. J. Davidson ◽  
D. R. Cooper
Keyword(s):  
Conformational Changes ◽  
Ultraviolet Irradiation ◽  
Irradiation Dose ◽  
Helical Structure ◽  
Neutral Salt ◽  
Soluble Collagen ◽  
Acid Soluble Collagen ◽  
Skin Collagen ◽  
Principal Effect ◽  
Chain Lengths

1. A study has been made of the effect of ultraviolet irradiation on the conformational changes taking place in cooled solutions of thermally denatured acid-soluble calf-skin collagen. 2. The increase in negative rotation and viscosity at 15° for irradiated and thermally denatured collagen solutions becomes less as the irradiation dose is increased. 3. The principal effect of ultraviolet irradiation is the fission of the primary collagen chains, eventually yielding chain lengths incapable of stabilizing a helical structure. 4. The effects of ultraviolet irradiation on acid-soluble collagen may be closely correlated with similar effects on neutral salt-soluble collagen.

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.

scholarly journals Isolation and properties of collagen extracted from mixed by-products obtained from different fish species

Biotecnia ◽  
2021 ◽  
Vol 23 (3) ◽  
pp. 109-116
Author(s):  
Celia Olivia García-Sifuentes ◽  
Julio Cesar Zamorano-Apodaca ◽  
Marcel Martinez-Porchas ◽  
Susana Maria Scheuren-Acevedo ◽  
Miguel Angel Mazorra-Manzano
Keyword(s):  
Fish Species ◽  
Type I Collagen ◽  
Helical Structure ◽  
Extraction Process ◽  
Type I ◽  
Denaturation Temperature ◽  
Soluble Collagen ◽  
Acid Soluble Collagen ◽  
Sds Page ◽  
By Products

Fish by-products consisting of skin, bones, or scales are collagen sources. Acid-soluble collagen (ASC) and pepsin-soluble collagen (PSC) mixed by-products derived from different fish species were extracted and evaluated. The properties evaluated for both collagens were chemical composition, amino acid- and SDS-PAGE- protein profiles, Fourier transform infrared spectroscopy (FTIR), denaturation temperature (Tmax), enthalpy (ΔH), and solubility. The ASC and PSC registered a protein content of 48.56 and 38.80 %, respectively. From the total amino acids detected, hydroxyproline accounted for 7 % and 6 % for ASC and PSC, respectively. The electrophoretic profile showed the presence of the type I collagen bands (α1, α2, β, and γ), whereas FTIR spectrum showed the presence of diverse collagen functional groups (Amide A, B, I, II, and III) for both extracted types, and demonstrated that the extraction process did not affect the collagen´s triple-helical structure. The Tmax of ASC and PSC were 38.27 and 38.07° C, respectively, whereas ΔH were 0.64 and 0.33 J g-1. The lowest solubility was registered at pH 5 for ASC and pH 9 for PSC. The caractheristics of the collagen extracted, indicated that a mixture of by-products from different species could be an alternative for their reutilization by the local markets.

Triple-Helical Structure of(1→3)-β-D-Glucan

1980 ◽  
Vol 13 (6) ◽  
pp. 1466-1471 ◽  
Author(s):  
Y. Deslandes ◽  
R. H. Marchessault ◽  
A. Sarko
Keyword(s):  
Helical Structure ◽  
Triple Helical Structure

Effect of aqueous ethanol on the triple helical structure of collagen

2014 ◽  
Vol 43 (12) ◽  
pp. 643-652 ◽  
Author(s):  
Arun Gopinath ◽  
Samala Murali Mohan Reddy ◽  
Balaraman Madhan ◽  
Ganesh Shanmguam ◽  
Jonnalagadda Raghava Rao
Keyword(s):  
Aqueous Ethanol ◽  
Helical Structure ◽  
Triple Helical Structure

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
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